T00089
type: Enzyme
active site residues resources: P00929
active site residues resources: 1bks
active site residues resources: 1qoq
active site residues resources: 1ttp
active site residues resources: 1ttq
cath: TIM Barrel
cath: Rossmann fold
csa: 1a50
csa: 1geq
ec: https://purl.uniprot.org/enzyme/4.2.1.20
kegg cofactor: Pyridoxal phosphate
kegg cofactor: Monovalent ion
kegg enzyme: tryptophan synthase
kegg intermediate: Indole
kegg intermediate: External aldimine intermediate (initial stage:PLP-L-Ser)
kegg intermediate: Quinonoid intermediate (PLP-Ser)
kegg intermediate: Aminoacrylate intermediate (PLP-dehydroAla)
kegg intermediate: Quinonoid intermediate (PLP-Trp)
kegg intermediate: External aldimine intermeidate (final stage:PLP-L-TRP)
kegg pathway: Phenylalanine, tyrosine and tryptophan biosynthesis
kegg product: L-Tryptophan
kegg product: D-Glyceraldehyde 3-phosphate
kegg product: H2O
kegg substrate: L-Serine
kegg substrate: 1-(Indol-3-yl)glycerol 3-phosphate
pdb: 1geqA
pdb: 1geqB
pdb: 1a50A
pdb: 1a5aA
pdb: 1a5bA
pdb: 1a5sA
pdb: 1beuA
pdb: 1bksA
pdb: 1c29A
pdb: 1c8vA
pdb: 1c9dA
pdb: 1cw2A
pdb: 1cx9A
pdb: 1fuyA
pdb: 1k3uA
pdb: 1k7eA
pdb: 1k7fA
pdb: 1k8xA
pdb: 1k8yA
pdb: 1k8zA
pdb: 1kfbA
pdb: 1kfcA
pdb: 1kfeA
pdb: 1kfjA
pdb: 1kfkA
pdb: 1qopA
pdb: 1qoqA
pdb: 1ttpA
pdb: 1ttqA
pdb: 1ubsA
pdb: 1wsyA
pdb: 2trsA
pdb: 2tsyA
pdb: 2tysA
pdb: 2wsyA
pdb: 1a50B01
pdb: 1a5aB01
pdb: 1a5bB01
pdb: 1a5sB01
pdb: 1beuB01
pdb: 1bksB01
pdb: 1c29B01
pdb: 1c8vB01
pdb: 1c9dB01
pdb: 1cw2B01
pdb: 1cx9B01
pdb: 1fuyB01
pdb: 1k3uB01
pdb: 1k7eB01
pdb: 1k7fB01
pdb: 1k8xB01
pdb: 1k8yB01
pdb: 1k8zB01
pdb: 1kfbB01

Analogue
compound: 1-(Indol-3-yl)glycerol 3-phosphate
ligand het code: FIP
pdb: 1a50A

Analogue
compound: 1-(Indol-3-yl)glycerol 3-phosphate
ligand het code: FIP
pdb: 1a5sA

Analogue
compound: 1-(Indol-3-yl)glycerol 3-phosphate
ligand het code: IPL
pdb: 1beuA

Analogue
compound: 1-(Indol-3-yl)glycerol 3-phosphate
ligand het code: FIP
pdb: 1fuyA

Analogue
compound: 1-(Indol-3-yl)glycerol 3-phosphate
ligand het code: IAD
pdb: 1k3uA

Analogue
compound: 1-(Indol-3-yl)glycerol 3-phosphate
ligand het code: IAG
pdb: 1k7eA

Analogue
compound: 1-(Indol-3-yl)glycerol 3-phosphate
ligand het code: IAV
pdb: 1k7fA

Analogue
compound: 1-(Indol-3-yl)glycerol 3-phosphate
ligand het code: IAG
pdb: 1k8zA

Analogue
compound: 1-(Indol-3-yl)glycerol 3-phosphate
ligand het code: IPL
pdb: 1kfcA

Analogue
compound: 1-(Indol-3-yl)glycerol 3-phosphate
ligand het code: IPL
pdb: 1qopA

Analogue
compound: Pyridoxal phosphate
ligand het code: PLS
pdb: 1beuB01

Analogue
compound: Pyridoxal phosphate
ligand het code: PLS
pdb: 1kfeB01

Analogue
compound: Pyridoxal phosphate
ligand het code: PLS
pdb: 1kfjB01

Analogue
compound: Pyridoxal phosphate
ligand het code: PLS
pdb: 2trsB01

Analogue
compound: Pyridoxal phosphate
ligand het code: PLS
pdb: 2tsyB01

Analogue
compound: Pyridoxal phosphate
ligand het code: PLT
pdb: 2tysB01

IntermediateBound
compound: External aldimine intermediate (initial stage:PLP-L-Ser)
ligand het code: PLS
pdb: 1beuB01

IntermediateBound
compound: External aldimine intermediate (initial stage:PLP-L-Ser)
ligand het code: PLS
pdb: 1kfeB01

IntermediateBound
compound: External aldimine intermediate (initial stage:PLP-L-Ser)
ligand het code: PLS
pdb: 1kfjB01

IntermediateBound
compound: External aldimine intermediate (initial stage:PLP-L-Ser)
ligand het code: PLP-SER
pdb: 1ubsB01

IntermediateBound
compound: External aldimine intermediate (initial stage:PLP-L-Ser)
ligand het code: PLS
pdb: 2trsB01

IntermediateBound
compound: External aldimine intermediate (initial stage:PLP-L-Ser)
ligand het code: PLS
pdb: 2tsyB01

IntermediateBound
compound: Aminoacrylate intermediate (PLP-dehydroAla)
ligand het code: PLP-SER
pdb: 1a5sB01

IntermediateBound
compound: External aldimine intermeidate (final stage:PLP-L-TRP)
ligand het code: PLT
pdb: 2tysB01

ReferenceForCatalyticMechanism
reference index: 2
reference section: p.28-30

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.15, Fig.16, Fig.17, Fig.18, Fig.19, p.128-151

ReferenceForCatalyticMechanism
reference index: 11
reference section: Scheme I, Scheme II, p.1185
reference step: 9

ReferenceForCatalyticMechanism
reference index: 12
reference section: Scheme I, Fig.1, p.3836-3838
reference step: 9

ReferenceForCatalyticMechanism
reference index: 16
reference section: Scheme I, p.8733
reference step: 8

ReferenceForCatalyticMechanism
reference index: 17
reference section: FIG. 1, p.14930-14931
reference step: 8

ReferenceForCatalyticMechanism
reference index: 21
reference section: Scheme 1, p.9473-9475
reference step: 9

ReferenceForCatalyticMechanism
reference index: 22
reference section: SCHEME I, p.17336-17337
reference step: 5

ReferenceForCatalyticMechanism
reference index: 25
reference section: Scheme 1, p.7384
reference step: 11

ReferenceForCatalyticMechanism
reference index: 26
reference section: Scheme 1
reference step: 11

ReferenceForCatalyticMechanism
reference index: 29
reference section: Scheme 1A, Fig.11, p.7674-7678

ReferenceForCatalyticMechanism
reference index: 32
reference section: Figure 1
reference step: 10

ReferenceForCatalyticMechanism
reference index: 34
reference section: Scheme 1
reference step: 10

ReferenceForCatalyticMechanism
reference index: 35
reference section: Scheme 1B
reference step: 5

ReferenceForCatalyticMechanism
reference index: 36
reference section: FIGURE 2
reference step: 5

ReferenceForCatalyticMechanism
reference index: 38
reference section: SCHEME 1, p.8555
reference step: 2

ReferenceForCatalyticMechanism
reference index: 39
reference section: SCHEME 1, p.33252
reference step: 7

ReferenceForCatalyticMechanism
reference index: 42
reference section: Fig.1, p.12672-12673
reference step: 2

ReferenceForCatalyticMechanism
reference index: 43
reference section: p.16479

ReferenceForCatalyticMechanism
reference index: 44
reference section: Scheme 1, p.7134-7141
reference step: 10

ReferenceForCatalyticMechanism
reference index: 45
reference section: Scheme 1, p.7127-7129
reference step: 6

ReferenceForCatalyticMechanism
reference index: 46
reference section: SCHEME 1, p.31191-31194
reference step: 9

ReferenceForCatalyticMechanism
reference index: 48
reference section: Fig.3, Fig.9, p.118-124, p.127-132

ReferenceForCatalyticMechanism
reference index: 52
reference section: Scheme 1, p.7430-7432
reference step: 6

ReferenceForCatalyticMechanism
reference index: 54
reference section: Scheme 1
reference step: 7

ReferenceForCatalyticMechanism
reference index: 55
reference section: Scheme 1, Scheme 2, p.9998-10000
reference step: 6

ReferenceForCatalyticMechanism
reference index: 59
reference section: Fig.1

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

Rossmann fold
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.1100

H2O
type: KeggProduct
compound type: H2O
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Phenylalanine, tyrosine and tryptophan biosynthesis
type: KeggPathway
references: KEGG:MAP00400

Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.
type: BibliographicResource
authors:
  item: Hyde CC
  item: Ahmed SA
  item: Padlan EA
  item: Miles EW
  item: Davies DR
journal: J Biol Chem
medline id: 89034326
pages: 17857-71
published year: 1988
volume: 263
references: http://www.ncbi.nlm.nih.gov/pubmed/3053720
references: P00929
references: P0A2K1
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Enzymatic properties of mutant Escherichia coli tryptophan synthase alpha-subunits.
type: BibliographicResource
authors:
  item: Lim WK
  item: Sarkar SK
  item: Hardman JK
journal: J Biol Chem
pages: 20205-12
published year: 1991
volume: 266
references: http://www.ncbi.nlm.nih.gov/pubmed/1939081

Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium.
type: BibliographicResource
authors:
  item: Brzovic PS
  item: Kayastha AM
  item: Miles EW
  item: Dunn MF
journal: Biochemistry
pages: 1180-90
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1346502

Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex.
type: BibliographicResource
authors:
  item: Brzovic PS
  item: Ngo K
  item: Dunn MF
journal: Biochemistry
pages: 3831-9
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1567839

Threonine 183 and adjacent flexible loop residues in the tryptophan synthase alpha subunit have critical roles in modulating the enzymatic activities of the beta subunit in the alpha 2 beta 2 complex.
type: BibliographicResource
authors:
  item: Yang XJ
  item: Miles EW
journal: J Biol Chem
pages: 7520-8
published year: 1992
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/1559990

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00089#14
type: BibliographicResource
title: Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.
authors:
  item: Zhao GP
  item: Somerville RL
journal: J Biol Chem
pages: 526-41
published year: 1992
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/1309752

Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration.
type: BibliographicResource
authors:
  item: Saab-Rincon G
  item: Froebe CL
  item: Matthews CR
journal: Biochemistry
pages: 13981-90
published year: 1993
volume: 32
references: http://www.ncbi.nlm.nih.gov/pubmed/8268176

Lysine 87 in the beta subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product release.
type: BibliographicResource
authors:
  item: Lu Z
  item: Nagata S
  item: McPhie P
  item: Miles EW
journal: J Biol Chem
pages: 8727-34
published year: 1993
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/8473317

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00089#17
type: BibliographicResource
title: A single amino acid switch within the "hinge" region of the tryptophan synthase beta subunit of Escherichia coli that leads to diminished association with alpha subunit and arrested conversion of ESII to product.
authors:
  item: Zhao GP
  item: Somerville RL
journal: J Biol Chem
pages: 14921-31
published year: 1993
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/8325869

A study of the tryptophan synthase catalysed H/D exchange of the alpha-protons of amino acids.
type: BibliographicResource
authors:
  item: Milne JJ
  item: Malthouse JP
journal: Biochem Soc Trans
pages: 43S
published year: 1994
volume: 22
references: http://www.ncbi.nlm.nih.gov/pubmed/8206268

Structural and kinetic analysis of a channel-impaired mutant of tryptophan synthase.
type: BibliographicResource
authors:
  item: Schlichting I
  item: Yang XJ
  item: Miles EW
  item: Kim AY
  item: Anderson KS
journal: J Biol Chem
pages: 26591-3
published year: 1994
volume: 269
references: http://www.ncbi.nlm.nih.gov/pubmed/7929385

The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis.
type: BibliographicResource
authors:
  item: Hyde CC
  item: Miles EW
journal: Biotechnology (N Y)
pages: 27-32
published year: 1990
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/1366510

Factors affecting the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine.
type: BibliographicResource
authors:
  item: Milne JJ
  item: Malthouse JP
journal: Biochem J
pages: 1015-9
published year: 1995
volume: 311
references: http://www.ncbi.nlm.nih.gov/pubmed/7487918

Monovalent metal ions play an essential role in catalysis and intersubunit communication in the tryptophan synthase bienzyme complex.
type: BibliographicResource
authors:
  item: Woehl EU
  item: Dunn MF
journal: Biochemistry
pages: 9466-76
published year: 1995
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/7626617

Monovalent cations partially repair a conformational defect in a mutant tryptophan synthase alpha 2 beta 2 complex (beta-E109A).
type: BibliographicResource
authors:
  item: Ruvinov SB
  item: Ahmed SA
  item: McPhie P
  item: Miles EW
journal: J Biol Chem
pages: 17333-8
published year: 1995
volume: 270
references: http://www.ncbi.nlm.nih.gov/pubmed/7615535

The effect of different amino acid side chains on the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the alpha-protons of amino acids.
type: BibliographicResource
authors:
  item: Milne JJ
  item: Malthouse JP
journal: Biochem J
pages: 787-91
published year: 1996
volume: 314
references: http://www.ncbi.nlm.nih.gov/pubmed/8615770

Enzymatic synthesis of alpha-deuterated amino acids.
type: BibliographicResource
authors:
  item: Milne JJ
  item: Malthouse JP
journal: Biochem Soc Trans
pages: 133S
published year: 1996
volume: 24
references: http://www.ncbi.nlm.nih.gov/pubmed/8674622

Evidence of a low-barrier hydrogen bond in the tryptophan synthase catalytic mechanism.
type: BibliographicResource
authors:
  item: Hur O
  item: Leja C
  item: Dunn MF
journal: Biochemistry
pages: 7378-86
published year: 1996
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/8652514

beta-Site covalent reactions trigger transitions between open and closed conformations of the tryptophan synthase bienzyme complex.
type: BibliographicResource
authors:
  item: Pan P
  item: Dunn MF
journal: Biochemistry
pages: 5002-13
published year: 1996
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/8664293

Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex.
type: BibliographicResource
authors:
  item: Rhee S
  item: Parris KD
  item: Ahmed SA
  item: Miles EW
  item: Davies DR
journal: Biochemistry
pages: 4211-21
published year: 1996
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/8672457
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase.
type: BibliographicResource
authors:
  item: Saab-Rincon G
  item: Gualfetti PJ
  item: Matthews CR
journal: Biochemistry
pages: 1988-94
published year: 1996
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/8639683

Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes.
type: BibliographicResource
authors:
  item: Rhee S
  item: Parris KD
  item: Hyde CC
  item: Ahmed SA
  item: Miles EW
  item: Davies DR
journal: Biochemistry
medline id: 97352620
pages: 7664-80
published year: 1997
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/9201907
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00929
references: P0A2K1
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit. Monitoring conformational changes due to substitutions at position 49.
type: BibliographicResource
authors:
  item: Sawada S
  item: Akutsu H
  item: Ogasahara K
  item: Yutani K
journal: Eur J Biochem
pages: 667-73
published year: 1990
volume: 189
references: http://www.ncbi.nlm.nih.gov/pubmed/2190828

Conformational and functional properties of an undecapeptide epitope fused with the C-terminal end of the maltose binding protein.
type: BibliographicResource
authors:
  item: Rondard P
  item: Bregegere F
  item: Lecroisey A
  item: Delepierre M
  item: Bedouelle H
journal: Biochemistry
pages: 8954-61
published year: 1997
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/9220983

Mutational analysis of an antigenic peptide shows recognition in a loop conformation.
type: BibliographicResource
authors:
  item: Rondard P
  item: Goldberg ME
  item: Bedouelle H
journal: Biochemistry
pages: 8962-8
published year: 1997
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/9220984

Protein architecture, dynamics and allostery in tryptophan synthase channeling.
type: BibliographicResource
authors:
  item: Pan P
  item: Woehl E
  item: Dunn MF
journal: Trends Biochem Sci
pages: 22-7
published year: 1997
volume: 22
references: http://www.ncbi.nlm.nih.gov/pubmed/9020588

A comparison of some of the methods available for analysing the substrate dependence of the exchange of the alpha-protons of amino acids catalysed by pyridoxal-phosphate-dependent enzymes.
type: BibliographicResource
authors:
  item: Malthouse JP
  item: Fitzpatrick TB
  item: Mahon MM
journal: Biochem Soc Trans
pages: S66
published year: 1998
volume: 26
references: http://www.ncbi.nlm.nih.gov/pubmed/10909824

Tryptophan synthase mutations that alter cofactor chemistry lead to mechanism-based inactivation.
type: BibliographicResource
authors:
  item: Jhee KH
  item: McPhie P
  item: Ro HS
  item: Miles EW
journal: Biochemistry
pages: 14591-604
published year: 1998
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/9772188

Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60.
type: BibliographicResource
authors:
  item: Rhee S
  item: Miles EW
  item: Mozzarelli A
  item: Davies DR
journal: Biochemistry
pages: 10653-9
published year: 1998
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/9692955

Loop closure and intersubunit communication in tryptophan synthase.
type: BibliographicResource
authors:
  item: Schneider TR
  item: Gerhardt E
  item: Lee M
  item: Liang PH
  item: Anderson KS
  item: Schlichting I
journal: Biochemistry
pages: 5394-406
published year: 1998
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/9548921
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

A thermodynamic investigation of reactions catalyzed by tryptophan synthase.
type: BibliographicResource
authors:
  item: Kishore N
  item: Tewari YB
  item: Akers DL
  item: Goldberg RN
  item: Miles EW
journal: Biophys Chem
pages: 265-80
published year: 1998
volume: 73
references: http://www.ncbi.nlm.nih.gov/pubmed/9700925

Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49.
type: BibliographicResource
authors:
  item: Rhee S
  item: Miles EW
  item: Davies DR
journal: J Biol Chem
medline id: 98204834
pages: 8553-5
published year: 1998
volume: 273
references: http://www.ncbi.nlm.nih.gov/pubmed/9535826
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00929
references: P0A2K1
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Plasticity of the tryptophan synthase active site probed by 31P NMR spectroscopy.
type: BibliographicResource
authors:
  item: Schnackerz KD
  item: Mozzarelli A
journal: J Biol Chem
pages: 33247-53
published year: 1998
volume: 273
references: http://www.ncbi.nlm.nih.gov/pubmed/9837895

Mechanism of inactivation of the beta 2 subunit of Escherichia coli tryptophan synthase by monoclonal antibodies.
type: BibliographicResource
authors:
  item: Murry-Brelier A
  item: Goldberg ME
journal: J Biol Chem
pages: 7987-93
published year: 1990
volume: 265
references: http://www.ncbi.nlm.nih.gov/pubmed/1692319

Cooperative fluctuations and subunit communication in tryptophan synthase.
type: BibliographicResource
authors:
  item: Bahar I
  item: Jernigan RL
journal: Biochemistry
pages: 3478-90
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10090734

Guanidine hydrochloride exerts dual effects on the tryptophan synthase alpha 2 beta 2 complex as a cation activator and as a modulator of the active site conformation.
type: BibliographicResource
authors:
  item: Fan YX
  item: McPhie P
  item: Miles EW
journal: Biochemistry
pages: 7881-90
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10387029

Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase.
type: BibliographicResource
authors:
  item: Sachpatzidis A
  item: Dealwis C
  item: Lubetsky JB
  item: Liang PH
  item: Anderson KS
  item: Lolis E
journal: Biochemistry
medline id: 99435740
pages: 12665-74
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10504236
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00929
references: P0A2K1
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate.
type: BibliographicResource
authors:
  item: Weyand M
  item: Schlichting I
journal: Biochemistry
pages: 16469-80
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10600108
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactions.
type: BibliographicResource
authors:
  item: Woehl E
  item: Dunn MF
journal: Biochemistry
pages: 7131-41
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10353823

Mechanisms of monovalent cation action in enzyme catalysis: the first stage of the tryptophan synthase beta-reaction.
type: BibliographicResource
authors:
  item: Woehl E
  item: Dunn MF
journal: Biochemistry
pages: 7118-30
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10353822

Catalytic mechanism of the tryptophan synthase alpha(2)beta(2) complex. Effects of pH, isotopic substitution, and allosteric ligands.
type: BibliographicResource
authors:
  item: Ro HS
  item: Wilson Miles E
journal: J Biol Chem
pages: 31189-94
published year: 1999
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/10531312

The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges.
type: BibliographicResource
authors:
  item: Merz A
  item: Knochel T
  item: Jansonius JN
  item: Kirschner K
journal: J Mol Biol
pages: 753-63
published year: 1999
volume: 288
references: http://www.ncbi.nlm.nih.gov/pubmed/10329177

Fundamental mechanisms of substrate channeling.
type: BibliographicResource
authors:
  item: Anderson KS
journal: Methods Enzymol
pages: 111-45
published year: 1999
volume: 308
references: http://www.ncbi.nlm.nih.gov/pubmed/10507003

Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein.
type: BibliographicResource
authors:
  item: Zitzewitz JA
  item: Gualfetti PJ
  item: Perkons IA
  item: Wasta SA
  item: Matthews CR
journal: Protein Sci
pages: 1200-9
published year: 1999
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/10386870

Structural basis for catalysis by tryptophan synthase.
type: BibliographicResource
authors:
  item: Miles EW
journal: Adv Enzymol Relat Areas Mol Biol
pages: 93-172
published year: 1991
volume: 64
references: http://www.ncbi.nlm.nih.gov/pubmed/2053470

Regulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligand. Evidence from Arrhenius plots, absorption spectra, and primary kinetic isotope effects.
type: BibliographicResource
authors:
  item: Fan YX
  item: McPhie P
  item: Miles EW
journal: Biochemistry
pages: 4692-703
published year: 2000
volume: 39
references: http://www.ncbi.nlm.nih.gov/pubmed/10769125

Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase.
type: BibliographicResource
authors:
  item: Weyand M
  item: Schlichting I
journal: J Biol Chem
medline id: 20576265
pages: 41058-63
published year: 2000
volume: 275
references: http://www.ncbi.nlm.nih.gov/pubmed/11034989
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00929
references: P0A2K1
comment: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity.
type: BibliographicResource
authors:
  item: Ferrari D
  item: Yang LH
  item: Miles EW
  item: Dunn MF
journal: Biochemistry
pages: 7421-32
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11412095

Entropic stabilization of the tryptophan synthase alpha-subunit from a hyperthermophile, Pyrococcus furiosus. X-ray analysis and calorimetry.
type: BibliographicResource
authors:
  item: Yamagata Y
  item: Ogasahara K
  item: Hioki Y
  item: Lee SJ
  item: Nakagawa A
  item: Nakamura H
  item: Ishida M
  item: Kuramitsu S
  item: Yutani K
journal: J Biol Chem
pages: 11062-71
published year: 2001
volume: 276
references: http://www.ncbi.nlm.nih.gov/pubmed/11118452
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Intermediate trapping via a conformational switch in the Na(+)-activated tryptophan synthase bienzyme complex.
type: BibliographicResource
authors:
  item: Harris RM
  item: Dunn MF
journal: Biochemistry
pages: 9982-90
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/12146962

Proton transfers in the beta-reaction catalyzed by tryptophan synthase.
type: BibliographicResource
authors:
  item: Hur O
  item: Niks D
  item: Casino P
  item: Dunn MF
journal: Biochemistry
pages: 9991-10001
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/12146963

A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role.
type: BibliographicResource
authors:
  item: Hettwer S
  item: Sterner R
journal: J Biol Chem
pages: 8194-201
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/11756459

Crystal structure of the beta Ser178--> Pro mutant of tryptophan synthase. A "knock-out" allosteric enzyme.
type: BibliographicResource
authors:
  item: Weyand M
  item: Schlichting I
  item: Herde P
  item: Marabotti A
  item: Mozzarelli A
journal: J Biol Chem
pages: 10653-60
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/11756454
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structures of a new class of allosteric effectors complexed to tryptophan synthase.
type: BibliographicResource
authors:
  item: Weyand M
  item: Schlichting I
  item: Marabotti A
  item: Mozzarelli A
journal: J Biol Chem
pages: 10647-52
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/11756456
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase.
type: BibliographicResource
authors:
  item: Kulik V
  item: Weyand M
  item: Seidel R
  item: Niks D
  item: Arac D
  item: Dunn MF
  item: Schlichting I
journal: J Mol Biol
pages: 677-90
published year: 2002
volume: 324
references: http://www.ncbi.nlm.nih.gov/pubmed/12460570
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

A comparative study of the kinetics and stereochemistry of the serine hydroxymethyltransferase- and tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine.
type: BibliographicResource
authors:
  item: Malthouse JP
  item: Milne JJ
  item: Gariani LS
journal: Biochem J
pages: 807-12
published year: 1991
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/1849406

The isolated C-terminal (F2) fragment of the Escherichia coli tryptophan synthase beta 2-subunit folds into a stable, organized nonnative conformation.
type: BibliographicResource
authors:
  item: Chaffotte A
  item: Guillou Y
  item: Delepierre M
  item: Hinz HJ
  item: Goldberg ME
journal: Biochemistry
pages: 8067-74
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/1868082

Limited proteolysis of the beta 2-dimer of tryptophan synthase yields an enzymatically active derivative that binds alpha-subunits.
type: BibliographicResource
authors:
  item: Kaufmann M
  item: Schwarz T
  item: Jaenicke R
  item: Schnackerz KD
  item: Meyer HE
  item: Bartholmes P
journal: Biochemistry
pages: 4173-9
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/2021608

1H-NMR conformational analysis of a high-affinity antigenic 11-residue peptide from the tryptophan synthase beta 2 subunit.
type: BibliographicResource
authors:
  item: Delepierre M
  item: Larvor MP
  item: Baleux F
  item: Goldberg ME
journal: Eur J Biochem
pages: 681-93
published year: 1991
volume: 201
references: http://www.ncbi.nlm.nih.gov/pubmed/1718750

1a50B01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1a50
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a50

1a50B02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1a50
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a50

1a5aB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1a5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5a

1a5aB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1a5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5a

1a5bA
type: Pdb
catalytic residue: GLU 49; ;
references: 1a5b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5b
comment: mutant D60N, invisible 177-195

1a5bB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1a5b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5b

1a5bB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1a5b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5b

1a5sB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1a5s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5s

1a5sB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1a5s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5s

1beuB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1beu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1beu

1bksB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1bks
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bks

1bksB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1bks
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bks

1c29B01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1c29
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c29

1c29B02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1c29
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c29

1c8vB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1c8v
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c8v

1c8vB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1c8v
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c8v

1c9dB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1c9d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c9d

1c9dB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1c9d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c9d

1cw2B01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1cw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cw2

1cw2B02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1cw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cw2

1cx9B01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1cx9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cx9

1cx9B02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1cx9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cx9

1fuyB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1fuy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fuy

1fuyB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1fuy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fuy
comment: mutant A169L;C170W

1k3uB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1k3u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k3u

1k3uB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1k3u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k3u

1k7eB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1k7e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k7e

1k7eB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1k7e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k7e

1k7fB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1k7f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k7f

1k8xB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1k8x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k8x

1k8xB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1k8x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k8x

1k8yA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1k8y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k8y
comment: mutant S178P, invisible 179-191

1k8yB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1k8y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k8y

1k8yB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1k8y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k8y

1k8zB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1k8z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k8z

1k8zB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1k8z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k8z

1kfbA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1kfb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfb
comment: mutant T183V, invisivle 180-192

1kfbB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1kfb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfb

1kfcB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1kfc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfc

1kfcB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1kfc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfc

1kfeB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1kfe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfe

1kfjB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1kfj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfj

1kfkB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1kfk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfk

1kfkB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1kfk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfk

1qopB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1qop
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qop

1qopB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1qop
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qop

1qoqA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1qoq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qoq
comment: invisible 179-192

1qoqB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1qoq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qoq

1ttpB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1ttp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ttp

1ttpB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1ttp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ttp

1ttqB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1ttq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ttq

1ttqB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1ttq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ttq

1ubsB01
type: Pdb
catalytic residue: ;GLU 109
references: 1ubs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ubs
comment: mutant K87T

1ubsB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1ubs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ubs

1wsyB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1wsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wsy

2trsB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 2trs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2trs

2tsyA
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 2tsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tsy

2tsyB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 2tsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tsy

2tysB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 2tys
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tys

2wsyB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 2wsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2wsy

2wsyB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 2wsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2wsy

1a50A
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1a50
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a50

1a5aA
type: Pdb
catalytic residue: GLU 49; ;
references: 1a5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5a
comment: mutant D60N, invisible 177-189

1a5sA
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1a5s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5s

1beuA
type: Pdb
catalytic residue: GLU 49; ;
references: 1beu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1beu
comment: mutant D60N, invisible 177-191

1beuB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1beu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1beu

1bksA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1bks
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bks
comment: invisible 178-189

1c29A
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1c29
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c29

1c8vA
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1c8v
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c8v

1c9dA
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1c9d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c9d

1cw2A
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1cw2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cw2

1cx9A
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1cx9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cx9

1fuyA
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1fuy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fuy

1geqA
type: Pdb
catalytic residue: GLU 36;ASP 47;
references: 1geq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1geq
comment: invisible 167-173

1geqB
type: Pdb
catalytic residue: GLU 36;ASP 47;THR 168
references: 1geq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1geq
comment: invisible 170-172

1k3uA
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1k3u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k3u

1k7eA
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1k7e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k7e

1k7fA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1k7f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k7f
comment: invisible 179-192

1k7fB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1k7f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k7f

1k8xA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1k8x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k8x
comment: mutant T183V, invisible 178-195

1k8zA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1k8z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k8z
comment: mutant S178P, invisible 179-189

1kfbB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1kfb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfb

1kfcA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1kfc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfc
comment: mutant T183V, invisivle 179-192

1kfeA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1kfe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfe
comment: mutant T183V, invisivle 178-193

1kfeB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1kfe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfe

1kfjA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1kfj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfj
comment: invisible 178-191

1kfjB01
type: Pdb
catalytic residue: LYS 87;GLU 109
cofactor binding residue: LYS 87(PLP binding)
references: 1kfj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfj

1kfkA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1kfk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfk
comment: invisible 178-193

1qopA
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 1qop
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qop

1qoqB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1qoq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qoq

1ttpA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1ttp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ttp
comment: invisible 178-189

1ttqA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1ttq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ttq
comment: invisible 178-189

1ubsA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1ubs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ubs
comment: invisible 181-191

1wsyA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 1wsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wsy
comment: invisible 178-191

1wsyB02
type: Pdb
catalytic residue: HIS 86;ASP 305
cofactor binding residue: GLY 232;PHE 306;SER 308(Monovalent ion binding)
references: 1wsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wsy

2trsA
type: Pdb
catalytic residue: GLU 49;ASP 60;THR 183
references: 2trs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2trs

2trsB01
type: Pdb
catalytic residue: ;GLU 109
references: 2trs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2trs
comment: mutant K87T

2tsyB01
type: Pdb
catalytic residue: ;GLU 109
references: 2tsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tsy
comment: mutant K87T

2tysA
type: Pdb
catalytic residue: GLU 49;ASP 60;
references: 2tys
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tys
comment: invisible 179-191

2tysB01
type: Pdb
catalytic residue: ;GLU 109
references: 2tys
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tys
comment: mutant K87T

2wsyA
type: Pdb
catalytic residue: GLU 49; ;
references: 2wsy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2wsy
comment: invisible 54-62, 177-195

Monovalent ion
type: KeggCofactor
compound type: organic ion
references: KEGG:C99999

Pyridoxal phosphate
type: KeggCofactor
compound type: aromatic ring (with nitrogen atoms)
compound type: phosphate group/phosphate ion
references: KEGG:C00018
references: CHEBI:18405
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1-(Indol-3-yl)glycerol 3-phosphate
type: KeggSubstrate
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: KEGG:C03506
references: CHEBI:51793
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-Glyceraldehyde 3-phosphate
type: KeggProduct
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

L-Serine
type: KeggSubstrate
compound type: amino acids
compound type: carbohydrate
references: KEGG:C00065
references: CHEBI:17115
references: CHEBI:33384
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Tryptophan
type: KeggProduct
compound type: amino acids
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
references: KEGG:C00078
references: CHEBI:16828
references: CHEBI:57912
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Indole
type: KeggIntermediate
references: KEGG:C00463

External aldimine intermediate (initial stage:PLP-L-Ser)
type: KeggIntermediate
references: KEGG:I00043

Aminoacrylate intermediate (PLP-dehydroAla)
type: KeggIntermediate
references: KEGG:I00171

External aldimine intermeidate (final stage:PLP-L-TRP)
type: KeggIntermediate
references: KEGG:I00181

Quinonoid intermediate (PLP-Ser)
type: KeggIntermediate
references: KEGG:I00182

Quinonoid intermediate (PLP-Trp)
type: KeggIntermediate
references: KEGG:I00183

L-tryptophan synthetase
type: KeggEnzyme

indoleglycerol phosphate aldolase
type: KeggEnzyme

tryptophan desmolase
type: KeggEnzyme

tryptophan synthetase
type: KeggEnzyme

L-serine hydro-lyase (adding indoleglycerol-phosphate)
type: KeggEnzyme