S00225
type: Enzyme
active site residues resources: Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic base glutamic acid 165 is changed to aspartic acid.
active site residues resources: A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability.
active site residues resources: Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics.
active site residues resources: Inactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface
cath: TIM Barrel
csa: 1hti
csa: 1tph
ec: https://purl.uniprot.org/enzyme/5.3.1.1
kegg enzyme: triose-phosphate isomerase
kegg intermediate: Enediol form of glycerone phosphate
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Inositol metabolism
kegg pathway: Fructose and mannose metabolism
kegg pathway: Carbon fixation in photosynthetic organisms
kegg product: Glycerone phosphate
kegg substrate: D-Glyceraldehyde 3-phosphate
pdb: 1ag1O
pdb: 1ag1T
pdb: 1amkA
pdb: 1aw1A
pdb: 1aw1B
pdb: 1aw1D
pdb: 1aw1E
pdb: 1aw1G
pdb: 1aw1H
pdb: 1aw1J
pdb: 1aw1K
pdb: 1aw2A
pdb: 1aw2B
pdb: 1aw2D
pdb: 1aw2E
pdb: 1aw2G
pdb: 1aw2H
pdb: 1aw2J
pdb: 1aw2K
pdb: 1btmA
pdb: 1btmB
pdb: 1ci1A
pdb: 1ci1B
pdb: 1dkwA
pdb: 1dkwB
pdb: 1hg3A
pdb: 1hg3B
pdb: 1hg3C
pdb: 1hg3D
pdb: 1hg3E
pdb: 1hg3F
pdb: 1hg3G
pdb: 1hg3H
pdb: 1htiA
pdb: 1htiB
pdb: 1i45A
pdb: 1i45B
pdb: 1if2A
pdb: 1iigA
pdb: 1iigB
pdb: 1iihA
pdb: 1iihB
pdb: 1kv5A
pdb: 1kv5B
pdb: 1lyxA
pdb: 1lzoA
pdb: 1lzoB
pdb: 1lzoC
pdb: 1lzoD
pdb: 1m7oA
pdb: 1m7oB
pdb: 1m7pA
pdb: 1m7pB
pdb: 1ml1A
pdb: 1ml1C
pdb: 1ml1E
pdb: 1ml1G
pdb: 1ml1I
pdb: 1ml1K
pdb: 1mssA
pdb: 1mssB
pdb: 1n55A
pdb: 1neyA

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: 129
pdb: 1if2A

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: 3PG
pdb: 1iihB

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: 3PG
pdb: 1m7oA

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: 3PG
pdb: 1m7oB

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: G3H
pdb: 1m7pA

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: G3H
pdb: 1m7pB

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: G2H
pdb: 1woaA

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: G2H
pdb: 1woaB

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: G2H
pdb: 1woaC

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: G2H
pdb: 1woaD

Analogue
compound: D-Glyceraldehyde 3-phosphate
ligand het code: G3P
pdb: 6timB

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tpb1

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tpb2

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tpc1

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tpc2

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tph1

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tph2

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tpuA

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tpuB

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tpvA

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tpvB

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tpwA

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1tpwB

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1trdA

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1trdB

Analogue
compound: Glycerone phosphate
ligand het code: 4PB
pdb: 1tsiA

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 1ttjA

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 3ypiA

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 3ypiB

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 7timA

Analogue
compound: Glycerone phosphate
ligand het code: PGH
pdb: 7timB

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1amkA

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1aw1A

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1aw1B

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1aw1D

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1aw1E

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1aw1G

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1aw1H

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1aw1J

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1aw1K

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1btmA

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1btmB

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 3PP
pdb: 1hg3A

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 3PP
pdb: 1hg3B

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 3PP
pdb: 1hg3C

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 3PP
pdb: 1hg3D

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 3PP
pdb: 1hg3E

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 3PP
pdb: 1hg3F

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 3PP
pdb: 1hg3G

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 3PP
pdb: 1hg3H

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1htiA

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1htiB

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 3PP
pdb: 1iigB

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1kv5A

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1kv5B

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1lyxA

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1lzoB

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1lzoD

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1ml1A

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1ml1C

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1ml1E

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1ml1G

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1ml1I

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1ml1K

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1n55A

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 3PY-PO3
pdb: 1o5xA

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 2PG
pdb: 1o5xB

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1qdsA

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1ssgA

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1ssgB

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1su5A

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1su5B

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1sw0A

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1sw0B

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1sw3A

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1sw3B

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1sw7A

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1sw7B

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 1ttiA

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 2btmA

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 2btmB

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 2ypiA

TransitionStateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: PGA
pdb: 2ypiB

IntermediateAnalogue
compound: Enediol form of glycerone phosphate
ligand het code: 2PG
pdb: 4timB

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.1, p.159-161, p.168-170

ReferenceForCatalyticMechanism
reference index: 4
reference section: Fig.1, p.604, p.607-612

ReferenceForCatalyticMechanism
reference index: 5
reference section: p.120

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 9
reference section: Fig.1, Fig.4

ReferenceForCatalyticMechanism
reference index: 10
reference section: Scheme I, p.3187

ReferenceForCatalyticMechanism
reference index: 11
reference section: Fig.1, p.678

ReferenceForCatalyticMechanism
reference index: 12
reference section: Scheme I

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.1, Fig.2, Fig.4

ReferenceForCatalyticMechanism
reference index: 14
reference section: Scheme I, Scheme II, p.3016-3017

ReferenceForCatalyticMechanism
reference index: 15
reference section: Fig.1, Fig.2

ReferenceForCatalyticMechanism
reference index: 21
reference section: FIG.1

ReferenceForCatalyticMechanism
reference index: 27
reference section: Scheme I

ReferenceForCatalyticMechanism
reference index: 28
reference section: Fig.3, p.241-243

ReferenceForCatalyticMechanism
reference index: 29
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 33
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 34
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 35
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 40
reference section: Fig.3, p.314

ReferenceForCatalyticMechanism
reference index: 42
reference section: Fig.2

ReferenceForCatalyticMechanism
reference index: 43
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 44

ReferenceForCatalyticMechanism
reference index: 45
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 50
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 53
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 54
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 56
reference section: Fig.1, p.232-234

ReferenceForCatalyticMechanism
reference index: 58
reference section: Scheme 1, Scheme 3, Fig.8

ReferenceForCatalyticMechanism
reference index: 67
reference section: Fig.1, p.4395-4396

ReferenceForCatalyticMechanism
reference index: 69
reference section: SCHEME 1

ReferenceForCatalyticMechanism
reference index: 75
reference section: Fig.1, p.5194

ReferenceForCatalyticMechanism
reference index: 77
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 86
reference section: Scheme 1, Fig.1

ReferenceForCatalyticMechanism
reference index: 87
reference section: Scheme 1

ReferenceForCatalyticMechanism
reference index: 89
reference section: SCHEME I, SCHEME II, Fig.6

ReferenceForCatalyticMechanism
reference index: 92
reference section: FIG.1

ReferenceForCatalyticMechanism
reference index: 93
reference section: FIG.1, p.52468-52469

ReferenceForCatalyticMechanism
reference index: 94
reference section: Scheme 1, p.47

ReferenceForCatalyticMechanism
reference index: 96
reference section: Fig.1, Fig.3, p.52-54

ReferenceForCatalyticMechanism
reference index: 98

ReferenceForCatalyticMechanism
reference index: 101
reference section: Fig.1, p.229-230

TIM Barrel
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.70

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010

Inositol metabolism
type: KeggPathway
references: KEGG:MAP00031

Fructose and mannose metabolism
type: KeggPathway
references: KEGG:MAP00051

Carbon fixation in photosynthetic organisms
type: KeggPathway
references: KEGG:MAP00710

Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data.
type: BibliographicResource
authors:
  item: Banner DW
  item: Offord RE
  item: Priddle JD
  item: Waley SG
  item: Bloomer AC
  item: Petsko GA
  item: Phillips DC
  item: Pogson CI
  item: Wilson IA
  item: Corran PH
  item: Furth AJ
  item: Milman JD
journal: Nature
medline id: 75175220
pages: 609-14
published year: 1975
volume: 255
references: http://www.ncbi.nlm.nih.gov/pubmed/1134550
references: P00940
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND REVISION.

Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Pompliano DL
  item: Peyman A
  item: Knowles JR
journal: Biochemistry
pages: 3186-94
published year: 1990
volume: 29
references: http://www.ncbi.nlm.nih.gov/pubmed/2185832

Structures of unliganded and inhibitor complexes of W168F, a Loop6 hinge mutant of Plasmodium falciparum triosephosphate isomerase: observation of an intermediate position of loop6.
type: BibliographicResource
authors:
  item: Eaazhisai K
  item: Balaram H
  item: Balaram P
  item: Murthy MR
journal: J Mol Biol
pages: 671-84
published year: 2004
volume: 343
references: http://www.ncbi.nlm.nih.gov/pubmed/15465054
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Computational modeling of the catalytic reaction in triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Guallar V
  item: Jacobson M
  item: McDermott A
  item: Friesner RA
journal: J Mol Biol
pages: 227-39
published year: 2004
volume: 337
references: http://www.ncbi.nlm.nih.gov/pubmed/15001364

Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Kursula I
  item: Salin M
  item: Sun J
  item: Norledge BV
  item: Haapalainen AM
  item: Sampson NS
  item: Wierenga RK
journal: Protein Eng Des Sel
pages: 375-82
published year: 2004
volume: 17
references: http://www.ncbi.nlm.nih.gov/pubmed/15166315
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00225#104
type: BibliographicResource
title: Folding of beta/alpha-unit scrambled forms of S. cerevisiae triosephosphate isomerase: Evidence for autonomy of substructure formation and plasticity of hydrophobic and hydrogen bonding interactions in core of (beta/alpha)8-barrel.
authors:
  item: Shukla A
  item: Guptasarma P
journal: Proteins
pages: 548-57
published year: 2004
volume: 55
references: http://www.ncbi.nlm.nih.gov/pubmed/15103619

Structural considerations for the rational design of selective anti-trypanosomal agents: the role of the aromatic clusters at the interface of triosephosphate isomerase dimer.
type: BibliographicResource
authors:
  item: Espinoza-Fonseca LM
  item: Trujillo-Ferrara JG
journal: Biochem Biophys Res Commun
pages: 922-8
published year: 2005
volume: 328
references: http://www.ncbi.nlm.nih.gov/pubmed/15707966

Molecular dynamics simulations of active site mutants of triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Daggett V
  item: Kollman PA
journal: Protein Eng
pages: 677-90
published year: 1990
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/2217142

Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Blacklow SC
  item: Liu KD
  item: Knowles JR
journal: Biochemistry
pages: 8470-6
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/1883832

Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway.
type: BibliographicResource
authors:
  item: Davenport RC
  item: Bash PA
  item: Seaton BA
  item: Karplus M
  item: Petsko GA
  item: Ringe D
journal: Biochemistry
pages: 5821-6
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/2043623
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95.
type: BibliographicResource
authors:
  item: Komives EA
  item: Chang LC
  item: Lolis E
  item: Tilton RF
  item: Petsko GA
  item: Knowles JR
journal: Biochemistry
pages: 3011-9
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/2007138
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implications.
type: BibliographicResource
authors:
  item: Lodi PJ
  item: Knowles JR
journal: Biochemistry
pages: 6948-56
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/2069953

The application of computational methods to the study of enzyme catalysis by triose-phosphate isomerase and stabilities of variants of bacteriophage T4 lysozyme.
type: BibliographicResource
authors:
  item: Kollman PA
  item: Daggett V
  item: Dang LX
journal: Ciba Found Symp
pages: 91-103; discussion 103-7
published year: 1991
volume: 161
references: http://www.ncbi.nlm.nih.gov/pubmed/1814699

Probing the catalytic sites of triosephosphate isomerase by 31P-NMR with reversibly and irreversibly binding substrate analogues.
type: BibliographicResource
authors:
  item: Schnackerz KD
  item: Gracy RW
journal: Eur J Biochem
pages: 231-8
published year: 1991
volume: 199
references: http://www.ncbi.nlm.nih.gov/pubmed/2065677

Anion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate.
type: BibliographicResource
authors:
  item: Verlinde CL
  item: Noble ME
  item: Kalk KH
  item: Groendijk H
  item: Wierenga RK
  item: Hol WG
journal: Eur J Biochem
pages: 53-7
published year: 1991
volume: 198
references: http://www.ncbi.nlm.nih.gov/pubmed/2040290
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystallographic and molecular modeling studies on trypanosomal triosephosphate isomerase: a critical assessment of the predicted and observed structures of the complex with 2-phosphoglycerate.
type: BibliographicResource
authors:
  item: Noble ME
  item: Verlinde CL
  item: Groendijk H
  item: Kalk KH
  item: Wierenga RK
  item: Hol WG
journal: J Med Chem
pages: 2709-18
published year: 1991
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/1895291
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Atomic coordinates for triose phosphate isomerase from chicken muscle.
type: BibliographicResource
authors:
  item: Banner DW
  item: Bloomer A
  item: Petsko GA
  item: Phillips DC
  item: Wilson IA
journal: Biochem Biophys Res Commun
medline id: 77044751
pages: 146-55
published year: 1976
volume: 72
references: http://www.ncbi.nlm.nih.gov/pubmed/985462
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00940
comment: X-RAY CRYSTALLOGRAPHY.

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00225#20
type: BibliographicResource
title: Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex.
authors:
  item: Wierenga RK
  item: Noble ME
  item: Vriend G
  item: Nauche S
  item: Hol WG
journal: J Mol Biol
medline id: 91350193
pages: 995-1015
published year: 1991
volume: 220
references: http://www.ncbi.nlm.nih.gov/pubmed/1880808
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04789
comment: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).

Enzyme catalysis: not different, just better.
type: BibliographicResource
authors:
  item: Knowles JR
journal: Nature
pages: 121-4
published year: 1991
volume: 350
references: http://www.ncbi.nlm.nih.gov/pubmed/2005961

The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
type: BibliographicResource
authors:
  item: Noble ME
  item: Wierenga RK
  item: Lambeir AM
  item: Opperdoes FR
  item: Thunnissen AM
  item: Kalk KH
  item: Groendijk H
  item: Hol WG
journal: Proteins
pages: 50-69
published year: 1991
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/2062828
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Wierenga RK
  item: Noble ME
  item: Postma JP
  item: Groendijk H
  item: Kalk KH
  item: Hol WG
  item: Opperdoes FR
journal: Proteins
pages: 33-49
published year: 1991
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/2062827
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE.

Relationship between the catalytic center and the primary degradation site of triosephosphate isomerase: effects of active site modification and deamidation.
type: BibliographicResource
authors:
  item: Sun AQ
  item: Yuksel KU
  item: Gracy RW
journal: Arch Biochem Biophys
pages: 382-90
published year: 1992
volume: 293
references: http://www.ncbi.nlm.nih.gov/pubmed/1536574

Effects of active site modification and reversible dissociation on the secondary structure of triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Sun AQ
  item: Yuksel KU
  item: Rao GS
  item: Gracy RW
journal: Arch Biochem Biophys
pages: 421-8
published year: 1992
volume: 295
references: http://www.ncbi.nlm.nih.gov/pubmed/1586170

Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Sampson NS
  item: Knowles JR
journal: Biochemistry
pages: 8488-94
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1390633

Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Sampson NS
  item: Knowles JR
journal: Biochemistry
pages: 8482-7
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1390632

Simulation analysis of triose phosphate isomerase: conformational transition and catalysis.
type: BibliographicResource
authors:
  item: Karplus M
  item: Evanseck JD
  item: Joseph D
  item: Bash PA
  item: Field MJ
journal: Faraday Discuss
pages: 239-48
published year: 1992
volume: (93)
references: http://www.ncbi.nlm.nih.gov/pubmed/1290934

A TIM barrel protein without enzymatic activity? Crystal-structure of narbonin at 1.8 A resolution.
type: BibliographicResource
authors:
  item: Hennig M
  item: Schlesier B
  item: Dauter Z
  item: Pfeffer S
  item: Betzel C
  item: Hohne WE
  item: Wilson KS
journal: FEBS Lett
pages: 80-4
published year: 1992
volume: 306
references: http://www.ncbi.nlm.nih.gov/pubmed/1628747

On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase.
type: BibliographicResource
authors:
  item: Alber T
  item: Banner DW
  item: Bloomer AC
  item: Petsko GA
  item: Phillips D
  item: Rivers PS
  item: Wilson IA
journal: Philos Trans R Soc Lond B Biol Sci
pages: 159-71
published year: 1981
volume: 293
references: http://www.ncbi.nlm.nih.gov/pubmed/6115415
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystallographic binding studies with triosephosphate isomerases: conformational changes induced by substrate and substrate-analogues.
type: BibliographicResource
authors:
  item: Wierenga RK
  item: Borchert TV
  item: Noble ME
journal: FEBS Lett
pages: 34-9
published year: 1992
volume: 307
references: http://www.ncbi.nlm.nih.gov/pubmed/1639191

Interactions between the catalytic centers and subunit interface of triosephosphate isomerase probed by refolding, active site modification, and subunit exchange.
type: BibliographicResource
authors:
  item: Sun AQ
  item: Yuksel KU
  item: Gracy RW
journal: J Biol Chem
pages: 20168-74
published year: 1992
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/1400336

Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Wierenga RK
  item: Noble ME
  item: Davenport RC
journal: J Mol Biol
medline id: 92235847
pages: 1115-26
published year: 1992
volume: 224
references: http://www.ncbi.nlm.nih.gov/pubmed/1569570
references: P00940
references: P00942
references: P04789
comment: X-RAY CRYSTALLOGRAPHY.

Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformation.
type: BibliographicResource
authors:
  item: Verlinde CL
  item: Witmans CJ
  item: Pijning T
  item: Kalk KH
  item: Hol WG
  item: Callens M
  item: Opperdoes FR
journal: Protein Sci
pages: 1578-84
published year: 1992
volume: 1
references: http://www.ncbi.nlm.nih.gov/pubmed/1304889
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution.
type: BibliographicResource
authors:
  item: Noble ME.M
  item: Zeelen JP
  item: Wierenga RK
  item: Mainfroid V
  item: Goraj K
  item: Gohimont A-C
  item: Martial JA
journal: Acta Crystallogr D Biol Crystallogr
pages: 403-17
published year: 1993
volume: 49(Pt 4)
references: http://www.ncbi.nlm.nih.gov/pubmed/15299515
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A858
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Direct evidence for the exploitation of an alpha-helix in the catalytic mechanism of triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Lodi PJ
  item: Knowles JR
journal: Biochemistry
pages: 4338-43
published year: 1993
volume: 32
references: http://www.ncbi.nlm.nih.gov/pubmed/8476863

Gating of the active site of triose phosphate isomerase: Brownian dynamics simulations of flexible peptide loops in the enzyme.
type: BibliographicResource
authors:
  item: Wade RC
  item: Davis ME
  item: Luty BA
  item: Madura JD
  item: McCammon JA
journal: Biophys J
pages: 9-15
published year: 1993
volume: 64
references: http://www.ncbi.nlm.nih.gov/pubmed/8431552

Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant.
type: BibliographicResource
authors:
  item: Borchert TV
  item: Pratt K
  item: Zeelen JP
  item: Callens M
  item: Noble ME
  item: Opperdoes FR
  item: Michels PA
  item: Wierenga RK
journal: Eur J Biochem
medline id: 93170303
pages: 703-10
published year: 1993
volume: 211
references: http://www.ncbi.nlm.nih.gov/pubmed/8436128
references: P04789
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND REVISION TO 203.

Limited proteolysis of triose-phosphate isomerase and characterization of the catalytically active peptide complex.
type: BibliographicResource
authors:
  item: Sun AQ
  item: Yuksel KU
  item: Gracy RW
journal: J Biol Chem
pages: 26872-8
published year: 1993
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/8262920

Replacing the (beta alpha)-unit 8 of E.coli TIM with its chicken homologue leads to a stable and active hybrid enzyme.
type: BibliographicResource
authors:
  item: Mainfroid V
  item: Martial JA
  item: Goraj K
  item: Rentier-Delrue F
  item: Houbrechts A
  item: Loiseau A
  item: Gohimont AC
  item: Noble ME
  item: Borchert TV
  item: Wierenga RK
journal: Protein Eng
medline id: 94143343
pages: 893-900
published year: 1993
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/8309937
references: P0A858
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?
type: BibliographicResource
authors:
  item: Alber TC
  item: Davenport RC Jr
  item: Giammona DA
  item: Lolis E
  item: Petsko GA
  item: Ringe D
journal: Cold Spring Harb Symp Quant Biol
medline id: 88295752
pages: 603-13
published year: 1987
volume: 52
references: http://www.ncbi.nlm.nih.gov/pubmed/3331346
references: P00942
comment: REVIEW.

Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism.
type: BibliographicResource
authors:
  item: Noble ME
  item: Zeelen JP
  item: Wierenga RK
journal: Proteins
pages: 311-26
published year: 1993
volume: 16
references: http://www.ncbi.nlm.nih.gov/pubmed/8356028
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Deamidation of triosephosphate isomerase in reverse micelles: effects of water on catalysis and molecular wear and tear.
type: BibliographicResource
authors:
  item: Garza-Ramos G
  item: Tuena de Gomez-Puyou M
  item: Gomez-Puyou A
  item: Yuksel KU
  item: Gracy RW
journal: Biochemistry
pages: 6960-5
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8204630

Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site.
type: BibliographicResource
authors:
  item: Joseph-McCarthy D
  item: Lolis E
  item: Komives EA
  item: Petsko GA
journal: Biochemistry
pages: 2815-23
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8130194

Triosephosphate isomerase requires a positively charged active site: the role of lysine-12.
type: BibliographicResource
authors:
  item: Lodi PJ
  item: Chang LC
  item: Knowles JR
  item: Komives EA
journal: Biochemistry
pages: 2809-14
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8130193

Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution.
type: BibliographicResource
authors:
  item: Zhang Z
  item: Sugio S
  item: Komives EA
  item: Liu KD
  item: Knowles JR
  item: Petsko GA
  item: Ringe D
journal: Biochemistry
medline id: 94176473
pages: 2830-7
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8130195
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00940
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

The hinged lid of yeast triose-phosphate isomerase. Determination of the energy barrier between the two conformations.
type: BibliographicResource
authors:
  item: Yuksel KU
  item: Sun AQ
  item: Gracy RW
  item: Schnackerz KD
journal: J Biol Chem
pages: 5005-8
published year: 1994
volume: 269
references: http://www.ncbi.nlm.nih.gov/pubmed/7906272

Modular mutagenesis of a TIM-barrel enzyme: the crystal structure of a chimeric E. coli TIM having the eighth beta alpha-unit replaced by the equivalent unit of chicken TIM.
type: BibliographicResource
authors:
  item: Kishan R
  item: Zeelen JP
  item: Noble ME
  item: Borchert TV
  item: Mainfroid V
  item: Goraj K
  item: Martial JA
  item: Wierenga RK
journal: Protein Eng
pages: 945-51
published year: 1994
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/7809033
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms.
type: BibliographicResource
authors:
  item: Kishan KV
  item: Zeelen JP
  item: Noble ME
  item: Borchert TV
  item: Wierenga RK
journal: Protein Sci
pages: 779-87
published year: 1994
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/8061607
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme.
type: BibliographicResource
authors:
  item: Mande SC
  item: Mainfroid V
  item: Kalk KH
  item: Goraj K
  item: Martial JA
  item: Hol WG
journal: Protein Sci
medline id: 94339841
pages: 810-21
published year: 1994
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/8061610
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P60174
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 A resolution.
type: BibliographicResource
authors:
  item: Wierenga RK
  item: Kalk KH
  item: Hol WG
journal: J Mol Biol
medline id: 88118904
pages: 109-21
published year: 1987
volume: 198
references: http://www.ncbi.nlm.nih.gov/pubmed/3430602
references: P04789
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules.
type: BibliographicResource
authors:
  item: Komives EA
  item: Lougheed JC
  item: Liu K
  item: Sugio S
  item: Zhang Z
  item: Petsko GA
  item: Ringe D
journal: Biochemistry
pages: 13612-21
published year: 1995
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/7577950
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00225#51
type: BibliographicResource
title: Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions.
authors:
  item: Delboni LF
  item: Mande SC
  item: Rentier-Delrue F
  item: Mainfroid V
  item: Turley S
  item: Vellieux FM
  item: Martial JA
  item: Hol WG
journal: Protein Sci
medline id: 96164392
pages: 2594-604
published year: 1995
volume: 4
references: http://www.ncbi.nlm.nih.gov/pubmed/8580851
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00943
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8.
type: BibliographicResource
authors:
  item: Borchert TV
  item: Kishan KV
  item: Zeelen JP
  item: Schliebs W
  item: Thanki N
  item: Abagyan R
  item: Jaenicke R
  item: Wierenga RK
journal: Structure
medline id: 96000857
pages: 669-79
published year: 1995
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/8591044
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04789
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS.

The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Komives EA
  item: Lougheed JC
  item: Zhang Z
  item: Sugio S
  item: Narayana N
  item: Xuong NH
  item: Petsko GA
  item: Ringe D
journal: Biochemistry
pages: 15474-84
published year: 1996
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/8952501
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Computer simulation of the triosephosphate isomerase catalyzed reaction.
type: BibliographicResource
authors:
  item: Aqvist J
  item: Fothergill M
journal: J Biol Chem
pages: 10010-6
published year: 1996
volume: 271
references: http://www.ncbi.nlm.nih.gov/pubmed/8626554

Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies.
type: BibliographicResource
authors:
  item: Schliebs W
  item: Thanki N
  item: Eritja R
  item: Wierenga R
journal: Protein Sci
pages: 229-39
published year: 1996
volume: 5
references: http://www.ncbi.nlm.nih.gov/pubmed/8745400

Ab initio models for receptor-ligand interactions in proteins. 4. Model assembly study of the catalytic mechanism of triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Perakyla M
  item: Pakkanen TA
journal: Proteins
pages: 225-36
published year: 1996
volume: 25
references: http://www.ncbi.nlm.nih.gov/pubmed/8811738

Effect of active-site modification on the terminal marking deamidation of triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Talent JM
  item: Zvaigzne AI
  item: Agrawal N
  item: Gracy RW
journal: Arch Biochem Biophys
pages: 27-35
published year: 1997
volume: 340
references: http://www.ncbi.nlm.nih.gov/pubmed/9126273

NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Harris TK
  item: Abeygunawardana C
  item: Mildvan AS
journal: Biochemistry
pages: 14661-75
published year: 1997
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/9398185

Phosphorus-31 nuclear magnetic resonance spectroscopy reveals two conformational forms of chloroacetol phosphate-bound triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Schnackerz KD
  item: Kuan TK
  item: Goux WJ
  item: Gracy RW
journal: Biochem Biophys Res Commun
pages: 736-40
published year: 1990
volume: 173
references: http://www.ncbi.nlm.nih.gov/pubmed/2260979

Protein engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop.
type: BibliographicResource
authors:
  item: Thanki N
  item: Zeelen JP
  item: Mathieu M
  item: Jaenicke R
  item: Abagyan RA
  item: Wierenga RK
  item: Schliebs W
journal: Protein Eng
pages: 159-67
published year: 1997
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/9089815

Mechanical property of a TIM-barrel protein.
type: BibliographicResource
authors:
  item: Kobayashi N
  item: Yamato T
  item: Go N
journal: Proteins
pages: 109-16
published year: 1997
volume: 28
references: http://www.ncbi.nlm.nih.gov/pubmed/9144796

Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability.
type: BibliographicResource
authors:
  item: Auerbach G
  item: Huber R
  item: Grattinger M
  item: Zaiss K
  item: Schurig H
  item: Jaenicke R
  item: Jacob U
journal: Structure
medline id: 98046096
pages: 1475-83
published year: 1997
volume: 5
references: http://www.ncbi.nlm.nih.gov/pubmed/9384563
references: P36204
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PGK, AND REVISIONS.

Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design.
type: BibliographicResource
authors:
  item: Velanker SS
  item: Ray SS
  item: Gokhale RS
  item: Suma S
  item: Balaram H
  item: Balaram P
  item: Murthy MR
journal: Structure
medline id: 97410385
pages: 751-61
published year: 1997
volume: 5
references: http://www.ncbi.nlm.nih.gov/pubmed/9261072
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q07412
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
type: BibliographicResource
authors:
  item: Alvarez M
  item: Zeelen JP
  item: Mainfroid V
  item: Rentier-Delrue F
  item: Martial JA
  item: Wyns L
  item: Wierenga RK
  item: Maes D
journal: J Biol Chem
pages: 2199-206
published year: 1998
volume: 273
references: http://www.ncbi.nlm.nih.gov/pubmed/9442062
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P50921
comment: NUCLEOTIDE SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes.
type: BibliographicResource
authors:
  item: Maldonado E
  item: Soriano-Garcia M
  item: Moreno A
  item: Cabrera N
  item: Garza-Ramos G
  item: de Gomez-Puyou M
  item: Gomez-Puyou A
  item: Perez-Montfort R
journal: J Mol Biol
medline id: 98437380
pages: 193-203
published year: 1998
volume: 283
references: http://www.ncbi.nlm.nih.gov/pubmed/9761683
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P52270
comment: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00225#66
type: BibliographicResource
title: Derivatization of the interface cysteine of triosephosphate isomerase from Trypanosoma brucei and Trypanosoma cruzi as probe of the interrelationship between the catalytic sites and the dimer interface.
authors:
  item: Perez-Montfort R
  item: Garza-Ramos G
  item: Alcantara GH
  item: Reyes-Vivas H
  item: Gao XG
  item: Maldonado E
  item: de Gomez-Puyou MT
  item: Gomez-Puyou A
journal: Biochemistry
pages: 4114-20
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10194326

The role of water in the catalytic efficiency of triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Zhang Z
  item: Komives EA
  item: Sugio S
  item: Blacklow SC
  item: Narayana N
  item: Xuong NH
  item: Stock AM
  item: Petsko GA
  item: Ringe D
journal: Biochemistry
pages: 4389-97
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10194358

Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures.
type: BibliographicResource
authors:
  item: Alvarez M
  item: Wouters J
  item: Maes D
  item: Mainfroid V
  item: Rentier-Delrue F
  item: Wyns L
  item: Depiereux E
  item: Martial JA
journal: J Biol Chem
medline id: 99315861
pages: 19181-7
published year: 1999
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/10383424
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00943
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Hydrogen bonding in enzymatic catalysis: analysis of energetic contributions.
type: BibliographicResource
authors:
  item: Shan SO
  item: Herschlag D
journal: Methods Enzymol
pages: 246-76
published year: 1999
volume: 308
references: http://www.ncbi.nlm.nih.gov/pubmed/10507008

How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases.
type: BibliographicResource
authors:
  item: Blacklow SC
  item: Knowles JR
journal: Biochemistry
pages: 4099-108
published year: 1990
volume: 29
references: http://www.ncbi.nlm.nih.gov/pubmed/2361134

Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane.
type: BibliographicResource
authors:
  item: Gao XG
  item: Maldonado E
  item: Perez-Montfort R
  item: Garza-Ramos G
  item: de Gomez-Puyou MT
  item: Gomez-Puyou A
  item: Rodriguez-Romero A
journal: Proc Natl Acad Sci U S A
medline id: 99398662
pages: 10062-7
published year: 1999
volume: 96
references: http://www.ncbi.nlm.nih.gov/pubmed/10468562
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P52270
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power.
type: BibliographicResource
authors:
  item: Williams JC
  item: Zeelen JP
  item: Neubauer G
  item: Vriend G
  item: Backmann J
  item: Michels PA
  item: Lambeir AM
  item: Wierenga RK
journal: Protein Eng
medline id: 99249704
pages: 243-50
published year: 1999
volume: 12
references: http://www.ncbi.nlm.nih.gov/pubmed/10235625
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P48499
comment: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).

The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures.
type: BibliographicResource
authors:
  item: Maes D
  item: Jaenicke R
  item: Wierenga RK
  item: Zeelen JP
  item: Thanki N
  item: Beaucamp N
  item: Alvarez M
  item: Thi MH
  item: Backmann J
  item: Martial JA
  item: Wyns L
journal: Proteins
medline id: 20058648
pages: 441-53
published year: 1999
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/10591103
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P36204
comment: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF TIM.

Identification of a potential metal cation-pi binding site in the structure of a thermophilic Bacillus stearothermophilus triosephosphate isomerase mutant.
type: BibliographicResource
authors:
  item: Wouters J
  item: Maes D
journal: Acta Crystallogr D Biol Crystallogr
pages: 1201-3
published year: 2000
volume: 56
references: http://www.ncbi.nlm.nih.gov/pubmed/10957646

The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase.
type: BibliographicResource
authors:
  item: Lambeir AM
  item: Backmann J
  item: Ruiz-Sanz J
  item: Filimonov V
  item: Nielsen JE
  item: Kursula I
  item: Norledge BV
  item: Wierenga RK
journal: Eur J Biochem
pages: 2516-24
published year: 2000
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/10785370
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Structural determinants for ligand binding and catalysis of triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Kursula I
  item: Partanen S
  item: Lambeir AM
  item: Antonov DM
  item: Augustyns K
  item: Wierenga RK
journal: Eur J Biochem
pages: 5189-96
published year: 2001
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/11589711
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The time scale of the catalytic loop motion in triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Rozovsky S
  item: McDermott AE
journal: J Mol Biol
pages: 259-70
published year: 2001
volume: 310
references: http://www.ncbi.nlm.nih.gov/pubmed/11419951

Tiny TIM: a small, tetrameric, hyperthermostable triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Walden H
  item: Bell GS
  item: Russell RJ
  item: Siebers B
  item: Hensel R
  item: Taylor GL
journal: J Mol Biol
pages: 745-57
published year: 2001
volume: 306
references: http://www.ncbi.nlm.nih.gov/pubmed/11243785
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P62003
comment: X-ray crystallography

The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Xiang J
  item: Sun J
  item: Sampson NS
journal: J Mol Biol
pages: 1103-12
published year: 2001
volume: 307
references: http://www.ncbi.nlm.nih.gov/pubmed/11286559

Structure of yeast triosephosphate isomerase at 1.9-A resolution.
type: BibliographicResource
authors:
  item: Lolis E
  item: Alber T
  item: Davenport RC
  item: Rose D
  item: Hartman FC
  item: Petsko GA
journal: Biochemistry
medline id: 90373768
pages: 6609-18
published year: 1990
volume: 29
references: http://www.ncbi.nlm.nih.gov/pubmed/2204417
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00942
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Different strategies to recover the activity of monomeric triosephosphate isomerase by directed evolution.
type: BibliographicResource
authors:
  item: Saab-Rincon G
  item: Juarez VR
  item: Osuna J
  item: Sanchez F
  item: Soberon X
journal: Protein Eng
pages: 149-55
published year: 2001
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/11342710

Modeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8) of triosephosphate isomerase: toward a new substrate specificity.
type: BibliographicResource
authors:
  item: Norledge BV
  item: Lambeir AM
  item: Abagyan RA
  item: Rottmann A
  item: Fernandez AM
  item: Filimonov VV
  item: Peter MG
  item: Wierenga RK
journal: Proteins
pages: 383-9
published year: 2001
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/11151009
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state.
type: BibliographicResource
authors:
  item: Parthasarathy S
  item: Balaram H
  item: Balaram P
  item: Murthy MR
journal: Acta Crystallogr D Biol Crystallogr
pages: 1992-2000
published year: 2002
volume: 58
references: http://www.ncbi.nlm.nih.gov/pubmed/12454456
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00225#83
type: BibliographicResource
title: Catalysis and stability of triosephosphate isomerase from Trypanosoma brucei with different residues at position 14 of the dimer interface. Characterization of a catalytically competent monomeric enzyme.
authors:
  item: Hernandez-Alcantara G
  item: Garza-Ramos G
  item: Hernandez GM
  item: Gomez-Puyou A
  item: Perez-Montfort R
journal: Biochemistry
pages: 4230-8
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/11914068

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00225#84
type: BibliographicResource
title: Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state.
authors:
  item: Parthasarathy S
  item: Ravindra G
  item: Balaram H
  item: Balaram P
  item: Murthy MR
journal: Biochemistry
pages: 13178-88
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/12403619
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis.
type: BibliographicResource
authors:
  item: Kursula I
  item: Partanen S
  item: Lambeir AM
  item: Wierenga RK
journal: FEBS Lett
pages: 39-42
published year: 2002
volume: 518
references: http://www.ncbi.nlm.nih.gov/pubmed/11997014
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Quantum mechanics/molecular mechanics studies of triosephosphate isomerase-catalyzed reactions: effect of geometry and tunneling on proton-transfer rate constants.
type: BibliographicResource
authors:
  item: Cui Q
  item: Karplus M
journal: J Am Chem Soc
pages: 3093-124
published year: 2002
volume: 124
references: http://www.ncbi.nlm.nih.gov/pubmed/11902900

Functional specificities of methylglyoxal synthase and triosephosphate isomerase: a combined QM/MM analysis.
type: BibliographicResource
authors:
  item: Zhang X
  item: Harrison DH
  item: Cui Q
journal: J Am Chem Soc
pages: 14871-8
published year: 2002
volume: 124
references: http://www.ncbi.nlm.nih.gov/pubmed/12475328

Rapid mapping of protein structure, interactions, and ligand binding by misincorporation proton-alkyl exchange.
type: BibliographicResource
authors:
  item: Silverman JA
  item: Harbury PB
journal: J Biol Chem
pages: 30968-75
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/12185208

Catalysis and specificity in enzymes: a study of triosephosphate isomerase and comparison with methyl glyoxal synthase.
type: BibliographicResource
authors:
  item: Cui Q
  item: Karplus M
journal: Adv Protein Chem
pages: 315-72
published year: 2003
volume: 66
references: http://www.ncbi.nlm.nih.gov/pubmed/14631822

Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
type: BibliographicResource
authors:
  item: Lolis E
  item: Petsko GA
journal: Biochemistry
medline id: 90373769
pages: 6619-25
published year: 1990
volume: 29
references: http://www.ncbi.nlm.nih.gov/pubmed/2204418
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00942
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE.

Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme.
type: BibliographicResource
authors:
  item: Najera H
  item: Costas M
  item: Fernandez-Velasco DA
journal: Biochem J
pages: 785-92
published year: 2003
volume: 370
references: http://www.ncbi.nlm.nih.gov/pubmed/12472469

Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation.
type: BibliographicResource
authors:
  item: Desamero R
  item: Rozovsky S
  item: Zhadin N
  item: McDermott A
  item: Callender R
journal: Biochemistry
pages: 2941-51
published year: 2003
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/12627960

Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution.
type: BibliographicResource
authors:
  item: Kursula I
  item: Wierenga RK
journal: J Biol Chem
pages: 9544-51
published year: 2003
volume: 278
references: http://www.ncbi.nlm.nih.gov/pubmed/12522213
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolution.
type: BibliographicResource
authors:
  item: Parthasarathy S
  item: Eaazhisai K
  item: Balaram H
  item: Balaram P
  item: Murthy MR
journal: J Biol Chem
pages: 52461-70
published year: 2003
volume: 278
references: http://www.ncbi.nlm.nih.gov/pubmed/14563846
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The intramolecular mechanism for the second proton transfer in triosephosphate isomerase (TIM): a QM/FE approach.
type: BibliographicResource
authors:
  item: Alagona G
  item: Ghio C
  item: Kollman PA
journal: J Comput Chem
pages: 46-56
published year: 2003
volume: 24
references: http://www.ncbi.nlm.nih.gov/pubmed/12483674

Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity.
type: BibliographicResource
authors:
  item: Aparicio R
  item: Ferreira ST
  item: Polikarpov I
journal: J Mol Biol
pages: 1023-41
published year: 2003
volume: 334
references: http://www.ncbi.nlm.nih.gov/pubmed/14643664

Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.
type: BibliographicResource
authors:
  item: Jogl G
  item: Rozovsky S
  item: McDermott AE
  item: Tong L
journal: Proc Natl Acad Sci U S A
pages: 50-5
published year: 2003
volume: 100
references: http://www.ncbi.nlm.nih.gov/pubmed/12509510
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability.
type: BibliographicResource
authors:
  item: Gonzalez-Mondragon E
  item: Zubillaga RA
  item: Saavedra E
  item: Chanez-Cardenas ME
  item: Perez-Montfort R
  item: Hernandez-Arana A
journal: Biochemistry
pages: 3255-63
published year: 2004
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/15023076

Entropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase.
type: BibliographicResource
authors:
  item: Xiang J
  item: Jung JY
  item: Sampson NS
journal: Biochemistry
pages: 11436-45
published year: 2004
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/15350130

Protein motions promote catalysis.
type: BibliographicResource
authors:
  item: Tousignant A
  item: Pelletier JN
journal: Chem Biol
pages: 1037-42
published year: 2004
volume: 11
references: http://www.ncbi.nlm.nih.gov/pubmed/15324804

Inactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface
type: BibliographicResource
authors:
  item: Tellez-Valencia A
  item: Olivares-Illana V
  item: Hernandez-Santoyo A
  item: Perez-Montfort R
  item: Costas M
  item: Rodriguez-Romero A
  item: Lopez-Calahorra F
  item: Tuena de Gomez-Puyou M
  item: Gomez-Puyou A
journal: J Mol Biol
pages: 1355-1365
published year: 2004
volume: 341
references: http://www.ncbi.nlm.nih.gov/pubmed/15321726
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic base glutamic acid 165 is changed to aspartic acid.
type: BibliographicResource
authors:
  item: Joseph-McCarthy D
  item: Rost LE
  item: Komives EA
  item: Petsko GA
journal: Biochemistry
pages: 2824-9
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/7907502

A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability.
type: BibliographicResource
authors:
  item: Schliebs W
  item: Thanki N
  item: Jaenicke R
  item: Wierenga RK
journal: Biochemistry
pages: 9655-62
published year: 1997
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/9245397

Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics.
type: BibliographicResource
authors:
  item: Rozovsky S
  item: Jogl G
  item: Tong L
  item: McDermott AE
journal: J Mol Biol
pages: 271-80
published year: 2001
volume: 310
references: http://www.ncbi.nlm.nih.gov/pubmed/11419952
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

1neyA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
modified residue: FTR 168
references: 1ney
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ney
comment: mutant W90Y, W157F, W168FTR

1neyB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
modified residue: FTR 168
references: 1ney
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ney
comment: mutant W90Y, W157F, W168FTR

1nf0A
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
modified residue: FTR 168
references: 1nf0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nf0
comment: mutant W90Y, W157F, W168FTR

1nf0B
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
modified residue: FTR 168
references: 1nf0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nf0
comment: mutant W90Y, W157F, W168FTR

1ag1O
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1ag1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ag1

1ag1T
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1ag1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ag1

1amkA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1amk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1amk

1aw1A
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw1

1aw1B
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw1

1aw1D
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw1

1aw1E
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw1

1aw1G
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw1

1aw1H
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw1

1aw1J
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw1

1aw1K
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw1

1aw2A
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw2

1aw2B
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw2

1aw2D
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw2

1aw2E
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw2

1aw2G
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw2

1aw2H
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw2

1aw2J
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw2

1aw2K
type: Pdb
catalytic residue: ASN 9;LYS 11;HIS 97;GLU 169
references: 1aw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aw2

1btmA
type: Pdb
catalytic residue: ASN 8;LYS 10;HIS 94;GLU 166
references: 1btm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1btm

1btmB
type: Pdb
catalytic residue: ASN 8;LYS 10;HIS 94;GLU 166
references: 1btm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1btm

1ci1A
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 168
references: 1ci1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ci1

1ci1B
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 168
references: 1ci1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ci1

1dkwA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1dkw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dkw

1dkwB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1dkw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dkw

1hg3A
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 144
references: 1hg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hg3

1hg3B
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 144
references: 1hg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hg3

1hg3C
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 144
references: 1hg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hg3

1hg3D
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 144
references: 1hg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hg3

1hg3E
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 144
references: 1hg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hg3

1hg3F
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 144
references: 1hg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hg3

1hg3G
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 144
references: 1hg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hg3

1hg3H
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 144
references: 1hg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hg3

1htiA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1hti
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hti

1htiB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1hti
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hti

1i45A
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
modified residue: FTR 168
references: 1i45
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i45
comment: mutant W90Y, W157F, W168FTR

1i45B
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
modified residue: FTR 168
references: 1i45
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i45
comment: mutant W90Y, W157F, W168FTR

1if2A
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1if2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1if2
comment: mutant E65Q

1iigA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1iig
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iig

1iigB
type: Pdb
catalytic residue: ASN 311;LYS 313;HIS 395;GLU 467
references: 1iig
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iig

1iihA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1iih
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iih

1iihB
type: Pdb
catalytic residue: ASN 311;LYS 313;HIS 395;GLU 467
references: 1iih
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iih

1kv5A
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1kv5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kv5
comment: mutant R191S

1kv5B
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1kv5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kv5
comment: mutant R191S

1lyxA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1lyx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lyx

1lzoA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1lzo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lzo

1lzoB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1lzo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lzo

1lzoC
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1lzo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lzo

1lzoD
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1lzo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lzo

1m7oA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1m7o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m7o

1m7oB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1m7o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m7o

1m7pA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1m7p
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m7p

1m7pB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1m7p
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m7p

1ml1A
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1ml1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ml1

1ml1C
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1ml1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ml1

1ml1E
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1ml1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ml1

1ml1G
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1ml1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ml1

1ml1I
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1ml1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ml1

1ml1K
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1ml1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ml1

1mssA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1mss
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mss
comment: mutant F45S, V46S, 68-72 GNADALAS

1mssB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1mss
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mss
comment: mutant F45S, V46S, 68-72 GNADALAS

1n55A
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1n55
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n55
comment: mutant E65Q

1o5xA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1o5x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1o5x
comment: mutant A163V

1o5xB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1o5x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1o5x
comment: mutant A163V

1qdsA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1qds
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qds
comment: mutant E65Q

1spqA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1spq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1spq
comment: mutant A176K

1spqB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1spq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1spq
comment: mutant A176K

1sq7A
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1sq7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sq7
comment: mutant K174L, T175W

1sq7B
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1sq7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sq7
comment: mutant K174L, T175W

1ssdA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1ssd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ssd
comment: mutant K174Y, T175S, A176L

1ssdB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1ssd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ssd
comment: mutant K174Y, T175S, A176L

1ssgA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1ssg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ssg
comment: mutant K174Y, T175S, A176L

1ssgB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1ssg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ssg
comment: mutant K174Y, T175S, A176L

1su5A
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1su5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1su5
comment: mutant K174N, T175P, A176N

1su5B
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1su5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1su5
comment: mutant K174N, T175P, A176N

1suxA
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 168
references: 1sux
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sux

1suxB
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 168
references: 1sux
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sux

1sw0A
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1sw0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sw0
comment: mutant K174L, T175W

1sw0B
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1sw0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sw0
comment: mutant K174L, T175W

1sw3A
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1sw3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sw3
comment: mutant T175V

1sw3B
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1sw3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sw3
comment: mutant T175V

1sw7A
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1sw7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sw7
comment: mutant K174N, T175S, A176S

1sw7B
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1sw7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sw7
comment: mutant K174N, T175S, A176S

1tcdA
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 168
references: 1tcd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tcd

1tcdB
type: Pdb
catalytic residue: ASN 12;LYS 14;HIS 96;GLU 168
references: 1tcd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tcd

1timA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tim

1timB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tim

1tmhA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 97;GLU 169
references: 1tmh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tmh
comment: mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242

1tmhB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 97;GLU 169
references: 1tmh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tmh
comment: mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242

1tmhC
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 97;GLU 169
references: 1tmh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tmh
comment: mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242

1tmhD
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 97;GLU 169
references: 1tmh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tmh
comment: mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242

1tpb1
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;
references: 1tpb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpb
comment: mutant E165D

1tpb2
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;
references: 1tpb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpb
comment: mutant E165D

1tpc1
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;
references: 1tpc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpc
comment: mutant S96P, E165D

1tpc2
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;
references: 1tpc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpc
comment: mutant S96P, E165D

1tpdA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1tpd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpd

1tpdB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1tpd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpd

1tpeA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1tpe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpe

1tpfA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1tpf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpf

1tpfB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1tpf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpf

1tph1
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1tph
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tph

1tph2
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1tph
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tph

1tpuA
type: Pdb
catalytic residue: ASN 11;LYS 13; ;GLU 165
references: 1tpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpu
comment: mutant H95N

1tpuB
type: Pdb
catalytic residue: ASN 11;LYS 13; ;GLU 165
references: 1tpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpu
comment: mutant H95N

1tpvA
type: Pdb
catalytic residue: ASN 11;LYS 13; ;GLU 165
references: 1tpv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpv
comment: mutant H95N, S96P

1tpvB
type: Pdb
catalytic residue: ASN 11;LYS 13; ;GLU 165
references: 1tpv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpv
comment: mutant H95N, S96P

1tpwA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1tpw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpw
comment: mutant S96P

1tpwB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 1tpw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpw
comment: mutant S96P

1trdA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1trd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1trd

1trdB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1trd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1trd

1treA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 97;GLU 169
references: 1tre
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tre

1treB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 97;GLU 169
references: 1tre
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tre

1triA
type: Pdb
catalytic residue: ASN 11; ;HIS 95;GLU 167
references: 1tri
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tri
comment: mutant 68-82 GNADALAS, invisible K13

1tsiA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1tsi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tsi

1tsiB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1tsi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tsi

1ttiA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 1tti
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tti
comment: mutant I68G, A69N, K70A, S71D, P81A, A100W, deletion 73-79

1ttjA
type: Pdb
catalytic residue: ASN 11; ;HIS 95;GLU 167
references: 1ttj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ttj
comment: mutant F45S, V46S, invisible K13

1vgaA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1vga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vga
comment: mutant W168F

1vgaB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1vga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vga
comment: mutant W168F

1vgaC
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1vga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vga
comment: mutant W168F

1vgaD
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1vga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vga
comment: mutant W168F

1woaA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1woa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1woa
comment: mutant A163V, W168F

1woaB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1woa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1woa
comment: mutant A163V, W168F

1woaC
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1woa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1woa
comment: mutant A163V, W168F

1woaD
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1woa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1woa
comment: mutant A163V, W168F

1wobA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1wob
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wob
comment: mutant A163V, W168F

1wobB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1wob
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wob
comment: mutant A163V, W168F

1wobC
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1wob
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wob
comment: mutant A163V, W168F

1wobD
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1wob
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wob
comment: mutant A163V, W168F

1ydvA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1ydv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ydv

1ydvB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1ydv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ydv

1ypiA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1ypi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ypi

1ypiB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 1ypi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ypi

2btmA
type: Pdb
catalytic residue: ASN 8;LYS 10;HIS 94;GLU 166
references: 2btm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2btm

2btmB
type: Pdb
catalytic residue: ASN 8;LYS 10;HIS 94;GLU 166
references: 2btm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2btm

2ypiA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 2ypi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ypi

2ypiB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 2ypi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ypi

3timA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 3tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tim

3timB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 3tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tim

3ypiA
type: Pdb
catalytic residue: ASN 10;LYS 12; ;GLU 165
references: 3ypi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ypi
comment: mutant H95Q

3ypiB
type: Pdb
catalytic residue: ASN 10;LYS 12; ;GLU 165
references: 3ypi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ypi
comment: mutant H95Q

4timA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 4tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4tim

4timB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 4tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4tim

5timA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 5tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5tim

5timB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 5tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5tim

6timA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 6tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6tim

6timB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 167
references: 6tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6tim

7timA
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 7tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7tim

7timB
type: Pdb
catalytic residue: ASN 10;LYS 12;HIS 95;GLU 165
references: 7tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7tim

8timA
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 8tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8tim

8timB
type: Pdb
catalytic residue: ASN 11;LYS 13;HIS 95;GLU 165
references: 8tim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8tim

Glycerone phosphate
type: KeggProduct
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: KEGG:C00111
references: CHEBI:16108
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-Glyceraldehyde 3-phosphate
type: KeggSubstrate
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: KEGG:C00118
references: CHEBI:29052
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Enediol form of glycerone phosphate
type: KeggIntermediate
references: KEGG:I00178

phosphotriose isomerase
type: KeggEnzyme

triose phosphoisomerase
type: KeggEnzyme

triose phosphate mutase
type: KeggEnzyme

D-glyceraldehyde-3-phosphate ketol-isomerase
type: KeggEnzyme