M00113
type: Enzyme
active site residues resources: Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme.
active site residues resources: The transglycosylation reaction of cyclodextrin glucanotransferase is operated by a Ping-Pong mechanism.
active site residues resources: Cyclodextrin formation by the thermostable alpha-amylase of Thermoanaerobacterium thermosulfurigenes EM1 and reclassification of the enzyme as a cyclodextrin glycosyltransferase.
active site residues resources: P05618
active site residues resources: P30920
active site residues resources: P43379
active site residues resources: P31797
active site residues resources: P26827
cath: TIM Barrel
cath: Immunoglobulin-like
csa: 1cdg
csa: 1eo7
ec: https://purl.uniprot.org/enzyme/2.4.1.19
kegg cofactor: Calcium
kegg enzyme: cyclomaltodextrin glucanotransferase
kegg product: Cyclomaltodextrin
kegg product: Maltodextrin
kegg substrate: Maltodextrin
kegg substrate: Starch
macie: M0045
pdb: 1d7fA01
pdb: 1d7fB01
pdb: 1dedA01
pdb: 1dedB01
pdb: 1i75A01
pdb: 1i75B01
pdb: 1pamA01
pdb: 1pamB01
pdb: 1ukqA01
pdb: 1ukqB01
pdb: 1uksA01
pdb: 1uksB01
pdb: 1uktA01
pdb: 1uktB01
pdb: 1v3jA01
pdb: 1v3jB01
pdb: 1v3kA01
pdb: 1v3kB01
pdb: 1v3lA01
pdb: 1v3lB01
pdb: 1v3mA01
pdb: 1v3mB01
pdb: 1cgtA01
pdb: 1cguA01
pdb: 3cgtA01
pdb: 4cgtA01
pdb: 5cgtA01
pdb: 6cgtA01
pdb: 7cgtA01
pdb: 8cgtA01
pdb: 9cgtA01
pdb: 1cdgA01
pdb: 1cgvA01
pdb: 1cgwA01
pdb: 1cgxA01
pdb: 1cgyA01
pdb: 1cxeA01
pdb: 1cxfA01
pdb: 1cxgA01
pdb: 1cxhA01
pdb: 1cxiA01
pdb: 1cxkA01
pdb: 1cxlA01
pdb: 1d3cA01
pdb: 1dijA01
pdb: 1dtuA01
pdb: 1eo5A01
pdb: 1eo7A01
pdb: 1kckA01
pdb: 1kclA01
pdb: 1ot1A01
pdb: 1ot2A01
pdb: 1pezA01
pdb: 1pj9A01
pdb: 1tcmA01
pdb: 1tcmB01
pdb: 2cxgA01
pdb: 2dijA01

Analogue
compound: Maltodextrin
ligand het code: ACR
pdb: 1dedA01

Analogue
compound: Maltodextrin
ligand het code: ACR
pdb: 1dedB01

Analogue
compound: Maltodextrin
ligand het code: NOJ
pdb: 1i75A01

Analogue
compound: Maltodextrin
ligand het code: NOJ
pdb: 1i75B01

Analogue
compound: Maltodextrin
ligand het code: GLC-ACI-GLD-GAL
pdb: 1uksA01

Analogue
compound: Maltodextrin
ligand het code: GLC-ACI-GLD-GAL
pdb: 1uksB01

Analogue
compound: Maltodextrin
ligand het code: ACI-GLD-GLC-GAL
pdb: 1uktA01

Analogue
compound: Maltodextrin
ligand het code: ACI-GLD-GLC-GAL
pdb: 1uktB01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC
pdb: 1cguA01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC
pdb: 5cgtA01

Analogue
compound: Maltodextrin
ligand het code: OPG-DAG-GLC-OPG-DAG-GLC
pdb: 6cgtA01

Analogue
compound: Maltodextrin
ligand het code: TM6
pdb: 8cgtA01

Analogue
compound: Maltodextrin
ligand het code: TM5
pdb: 9cgtA01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC-GLC-GLC
pdb: 1cxeA01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC-GLC-GLC
pdb: 1cxfA01

Analogue
compound: Maltodextrin
ligand het code: ACR
pdb: 1cxgA01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC-GLC-GLC
pdb: 1cxhA01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC-ACI-GLC-GLC
pdb: 1dijA01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC-GLC (chain B)
pdb: 1eo5A01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC (chain B)
pdb: 1eo7A01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC-GLC-GLC (chain B)
pdb: 1kclA01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC-GLC (chain C)
pdb: 1ot1A01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC-GLC (chain C)
pdb: 1ot2A01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC (chain C)
pdb: 1pezA01

Analogue
compound: Maltodextrin
ligand het code: GLC-GLC (chain C)
pdb: 1pj9A01

TransitionStateAnalogue
ligand het code: GLC-ACI-G6D-BGC
pdb: 1ukqA01

TransitionStateAnalogue
ligand het code: GLC-ACI-G6D-BGC
pdb: 1ukqB01

TransitionStateAnalogue
ligand het code: GLC-ACI-GLD-GAL (chain D)
pdb: 1v3lA01

TransitionStateAnalogue
ligand het code: GLC-ACI-GLD-GLC (chain E)
pdb: 1v3lB01

TransitionStateAnalogue
ligand het code: GLC-ACI-GLD-GAL (chain D)
pdb: 1v3mA01

TransitionStateAnalogue
ligand het code: GLC-ACI-GLD-GAL (chain H)
pdb: 1v3mB01

TransitionStateAnalogue
ligand het code: GLC-GLC-GLC-ADH-G6D-GLC (chain C)
pdb: 1dtuA01

TransitionStateAnalogue
ligand het code: GLC-ADH-G6D-GLC (chain B)
pdb: 1kckA01

TransitionStateAnalogue
ligand het code: GLC-ACI-G6D-GLC
pdb: 2cxgA01

TransitionStateAnalogue
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC-ADH-G6D-GLC
pdb: 2dijA01

TransitionStateAnalogue
ligand het code: GTE-GLC-GLC-ACI-G6D-GLC-GLC
pdb: 1a47A01

IntermediateBound
ligand het code: GLC-GLC-G4D
pdb: 1cxlA01

ReferenceForCatalyticMechanism
reference index: 11
reference section: Fig.6, p.9935

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.70

ReferenceForCatalyticMechanism
reference index: 15
reference section: p.598

ReferenceForCatalyticMechanism
reference index: 20
reference section: p.2238-2240

ReferenceForCatalyticMechanism
reference index: 22
reference section: p.1143-1145

ReferenceForCatalyticMechanism
reference index: 23
reference section: p.5913-5914

ReferenceForCatalyticMechanism
reference index: 31
reference section: p.5578-5579

ReferenceForCatalyticMechanism
reference index: 34
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 35
reference section: Fig.2, p.407-408

ReferenceForCatalyticMechanism
reference index: 36
reference section: Fig.1, p.432-433

ReferenceForCatalyticMechanism
reference index: 38
reference section: Fig.1, Fig.6

ReferenceForCatalyticMechanism
reference index: 39
reference section: Fig.4, p.342

ReferenceForCatalyticMechanism
reference index: 57
reference section: Scheme 1

Immunoglobulin-like
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.60.40.10

Immunoglobulin-like
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.60.40.1180

TIM Barrel
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.80

Crystallization of and preliminary crystallographic data for Bacillus stearothermophilus cyclodextrin glucanotransferase.
type: BibliographicResource
authors:
  item: Kubota M
  item: Mikami B
  item: Tsujisaka Y
  item: Morita Y
journal: J Biochem (Tokyo)
pages: 12-3
published year: 1988
volume: 104
references: http://www.ncbi.nlm.nih.gov/pubmed/2975653

Catalytic center of cyclodextrin glycosyltransferase derived from X-ray structure analysis combined with site-directed mutagenesis.
type: BibliographicResource
authors:
  item: Klein C
  item: Hollender J
  item: Bender H
  item: Schulz GE
journal: Biochemistry
pages: 8740-6
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1390660
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Four aromatic residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of replacements on substrate binding and cyclization characteristics.
type: BibliographicResource
authors:
  item: Nakamura A
  item: Haga K
  item: Yamane K
journal: Biochemistry
pages: 9929-36
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8061001

Replacement of an amino acid residue of cyclodextrin glucanotransferase of Bacillus ohbensis doubles the production of gamma-cyclodextrin.
type: BibliographicResource
authors:
  item: Sin KA
  item: Nakamura A
  item: Masaki H
  item: Matsuura Y
  item: Uozumi T
journal: J Biotechnol
pages: 283-8
published year: 1994
volume: 32
references: http://www.ncbi.nlm.nih.gov/pubmed/7764720

Crystallization and preliminary X-ray studies of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011.
type: BibliographicResource
authors:
  item: Haga K
  item: Harata K
  item: Nakamura A
  item: Yamane K
journal: J Mol Biol
pages: 163-4
published year: 1994
volume: 237
references: http://www.ncbi.nlm.nih.gov/pubmed/8133516

Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form.
type: BibliographicResource
authors:
  item: Lawson CL
  item: van Montfort R
  item: Strokopytov B
  item: Rozeboom HJ
  item: Kalk KH
  item: de Vries GE
  item: Penninga D
  item: Dijkhuizen L
  item: Dijkstra BW
journal: J Mol Biol
pages: 590-600
published year: 1994
volume: 236
references: http://www.ncbi.nlm.nih.gov/pubmed/8107143
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity, and stability.
type: BibliographicResource
authors:
  item: Svensson B
journal: Plant Mol Biol
pages: 141-57
published year: 1994
volume: 25
references: http://www.ncbi.nlm.nih.gov/pubmed/8018865

Characteristic differences in the primary structure allow discrimination of cyclodextrin glucanotransferases from alpha-amylases.
type: BibliographicResource
authors:
  item: Janecek S
  item: MacGregor EA
  item: Svensson B
journal: Biochem J
pages: 685-6
published year: 1995
volume: 305
references: http://www.ncbi.nlm.nih.gov/pubmed/7832788

Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity.
type: BibliographicResource
authors:
  item: Penninga D
  item: Strokopytov B
  item: Rozeboom HJ
  item: Lawson CL
  item: Dijkstra BW
  item: Bergsma J
  item: Dijkhuizen L
journal: Biochemistry
pages: 3368-76
published year: 1995
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/7880832
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Determination of the catalytic activity of cyclomaltodextrin glucanotransferase by maltotriose-methylorange assay.
type: BibliographicResource
authors:
  item: Makela MJ
  item: Korpela TK
journal: J Biochem Biophys Methods
pages: 307-18
published year: 1988
volume: 15
references: http://www.ncbi.nlm.nih.gov/pubmed/2967858

Implications for the catalytic mechanism of glycosidases.
type: BibliographicResource
authors:
  item: Strokopytov B
  item: Penninga D
  item: Rozeboom HJ
  item: Kalk KH
  item: Dijkhuizen L
  item: Dijkstra BW. X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose
journal: Biochemistry
pages: 2234-40
published year: 1995
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/7857935
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products.
type: BibliographicResource
authors:
  item: Knegtel RM
  item: Strokopytov B
  item: Penninga D
  item: Faber OG
  item: Rozeboom HJ
  item: Kalk KH
  item: Dijkhuizen L
  item: Dijkstra BW
journal: J Biol Chem
medline id: 96094317
pages: 29256-64
published year: 1995
volume: 270
references: http://www.ncbi.nlm.nih.gov/pubmed/7493956
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P43379
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus Sp. 1011. Comparison of two independent molecules at 1.8-A resolution.
type: BibliographicResource
authors:
  item: Harata K
  item: Haga K
  item: Nakamura A
  item: Aoyagi M
  item: Yamane K
journal: Acta Crystallogr D Biol Crystallogr
pages: 1136-45
published year: 1996
volume: 52
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05618
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity.
type: BibliographicResource
authors:
  item: Strokopytov B
  item: Knegtel RM
  item: Penninga D
  item: Rozeboom HJ
  item: Kalk KH
  item: Dijkhuizen L
  item: Dijkstra BW
journal: Biochemistry
medline id: 96264806
pages: 4241-9
published year: 1996
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/8672460
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P43379
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH INHIBITOR.

The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251.
type: BibliographicResource
authors:
  item: Penninga D
  item: van der Veen BA
  item: Knegtel RM
  item: van Hijum SA
  item: Rozeboom HJ
  item: Kalk KH
  item: Dijkstra BW
  item: Dijkhuizen L
journal: J Biol Chem
medline id: 97115811
pages: 32777-84
published year: 1996
volume: 271
references: http://www.ncbi.nlm.nih.gov/pubmed/8955113
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P43379
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Crystal structure at 2.3 A resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermonanaerobacterium thermosulfurigenes EM1.
type: BibliographicResource
authors:
  item: Knegtel RM
  item: Wind RD
  item: Rozeboom HJ
  item: Kalk KH
  item: Buitelaar RM
  item: Dijkhuizen L
  item: Dijkstra BW
journal: J Mol Biol
medline id: 96177766
pages: 611-22
published year: 1996
volume: 256
references: http://www.ncbi.nlm.nih.gov/pubmed/8604143
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P26827
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

alpha-Amylase family: molecular biology and evolution.
type: BibliographicResource
authors:
  item: Janecek S
journal: Prog Biophys Mol Biol
pages: 67-97
published year: 1997
volume: 67
references: http://www.ncbi.nlm.nih.gov/pubmed/9401418

Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase.
type: BibliographicResource
authors:
  item: Mosi R
  item: Sham H
  item: Uitdehaag JC
  item: Ruiterkamp R
  item: Dijkstra BW
  item: Withers SG
journal: Biochemistry
pages: 17192-8
published year: 1998
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/9860832

Structure of cyclodextrin glycosyltransferase complexed with a derivative of its main product beta-cyclodextrin.
type: BibliographicResource
authors:
  item: Schmidt AK
  item: Cottaz S
  item: Driguez H
  item: Schulz GE
journal: Biochemistry
medline id: 98226626
pages: 5909-15
published year: 1998
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/9558324
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P30920
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production.
type: BibliographicResource
authors:
  item: Parsiegla G
  item: Schmidt AK
  item: Schulz GE
journal: Eur J Biochem
medline id: 98409292
pages: 710-7
published year: 1998
volume: 255
references: http://www.ncbi.nlm.nih.gov/pubmed/9738912
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P30920
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

A super-secondary structure predicted to be common to several alpha-1,4-D-glucan-cleaving enzymes.
type: BibliographicResource
authors:
  item: MacGregor EA
  item: Svensson B
journal: Biochem J
pages: 145-52
published year: 1989
volume: 259
references: http://www.ncbi.nlm.nih.gov/pubmed/2524186

Engineering of factors determining alpha-amylase and cyclodextrin glycosyltransferase specificity in the cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1.
type: BibliographicResource
authors:
  item: Wind RD
  item: Buitelaar RM
  item: Dijkhuizen L
journal: Eur J Biochem
pages: 598-605
published year: 1998
volume: 253
references: http://www.ncbi.nlm.nih.gov/pubmed/9654055

Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1.
type: BibliographicResource
authors:
  item: Wind RD
  item: Uitdehaag JC
  item: Buitelaar RM
  item: Dijkstra BW
  item: Dijkhuizen L
journal: J Biol Chem
medline id: 98157977
pages: 5771-9
published year: 1998
volume: 273
references: http://www.ncbi.nlm.nih.gov/pubmed/9488711
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P26827
comment: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS).

Effects of mutations in the starch-binding domain of Bacillus macerans cyclodextrin glycosyltransferase.
type: BibliographicResource
authors:
  item: Chang HY
  item: Irwin PM
  item: Nikolov ZL
journal: J Biotechnol
pages: 191-202
published year: 1998
volume: 65
references: http://www.ncbi.nlm.nih.gov/pubmed/9828462

Chemical modification of lysine side chains of cyclodextrin glycosyltransferase from Thermoanaerobacter causes a shift from cyclodextrin glycosyltransferase to alpha-amylase specificity.
type: BibliographicResource
authors:
  item: Alcalde M
  item: Plou FJ
  item: Andersen C
  item: Martin MT
  item: Pedersen S
  item: Ballesteros A
journal: FEBS Lett
pages: 333-7
published year: 1999
volume: 445
references: http://www.ncbi.nlm.nih.gov/pubmed/10094484

The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution.
type: BibliographicResource
authors:
  item: Uitdehaag JC
  item: Kalk KH
  item: van Der Veen BA
  item: Dijkhuizen L
  item: Dijkstra BW
journal: J Biol Chem
pages: 34868-76
published year: 1999
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/10574960
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Trapped in the act of catalysis.
type: BibliographicResource
authors:
  item: Davies GJ
  item: Wilson KS
journal: Nat Struct Biol
pages: 406-8
published year: 1999
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/10331861

X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family.
type: BibliographicResource
authors:
  item: Uitdehaag JC
  item: Mosi R
  item: Kalk KH
  item: van der Veen BA
  item: Dijkhuizen L
  item: Withers SG
  item: Dijkstra BW
journal: Nat Struct Biol
pages: 432-6
published year: 1999
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/10331869
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Introduction of raw starch-binding domains into Bacillus subtilis alpha-amylase by fusion with the starch-binding domain of Bacillus cyclomaltodextrin glucanotransferase.
type: BibliographicResource
authors:
  item: Ohdan K
  item: Kuriki T
  item: Takata H
  item: Kaneko H
  item: Okada S
journal: Appl Environ Microbiol
pages: 3058-64
published year: 2000
volume: 66
references: http://www.ncbi.nlm.nih.gov/pubmed/10877806

http://ezcatdb.cbrc.jp/EzCatDB/reference/M00113#38
type: BibliographicResource
title: Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity.
authors:
  item: Uitdehaag JC
  item: van Alebeek GJ
  item: van Der Veen BA
  item: Dijkhuizen L
  item: Dijkstra BW
journal: Biochemistry
pages: 7772-80
published year: 2000
volume: 39
references: http://www.ncbi.nlm.nih.gov/pubmed/10869182
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Engineering of cyclodextrin glycosyltransferase reaction and product specificity.
type: BibliographicResource
authors:
  item: van der Veen BA
  item: Uitdehaag JC
  item: Dijkstra BW
  item: Dijkhuizen L
journal: Biochim Biophys Acta
pages: 336-360
published year: 2000
volume: 1543
references: http://www.ncbi.nlm.nih.gov/pubmed/11150613

Three-dimensional structure of cyclodextrin glycosyltransferase from Bacillus circulans at 3.4 A resolution.
type: BibliographicResource
authors:
  item: Hofmann BE
  item: Bender H
  item: Schulz GE
journal: J Mol Biol
medline id: 90064533
pages: 793-800
published year: 1989
volume: 209
references: http://www.ncbi.nlm.nih.gov/pubmed/2531228
references: P30920
comment: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).

The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms.
type: BibliographicResource
authors:
  item: van der Veen BA
  item: van Alebeek GJ
  item: Uitdehaag JC
  item: Dijkstra BW
  item: Dijkhuizen L
journal: Eur J Biochem
pages: 658-65
published year: 2000
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/10651801

Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 A resolution.
type: BibliographicResource
authors:
  item: Ishii N
  item: Haga K
  item: Yamane K
  item: Harata K
journal: J Biochem (Tokyo)
pages: 383-91
published year: 2000
volume: 127
references: http://www.ncbi.nlm.nih.gov/pubmed/10731709
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Rational design of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 to increase alpha-cyclodextrin production.
type: BibliographicResource
authors:
  item: van der Veen BA
  item: Uitdehaag JC
  item: Penninga D
  item: van Alebeek GJ
  item: Smith LM
  item: Dijkstra BW
  item: Dijkhuizen L
journal: J Mol Biol
pages: 1027-38
published year: 2000
volume: 296
references: http://www.ncbi.nlm.nih.gov/pubmed/10686101
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structure of asparagine 233-replaced cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011 determined at 1.9 A resolution.
type: BibliographicResource
authors:
  item: Ishii N
  item: Haga K
  item: Yamane K
  item: Harata K
journal: J Mol Recognit
pages: 35-43
published year: 2000
volume: 13
references: http://www.ncbi.nlm.nih.gov/pubmed/10679895
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Trapping of a covalent enzyme intermediate in the reaction of Bacillus macerans cyclomaltodextrin glucanyltransferase with cyclomaltohexaose.
type: BibliographicResource
authors:
  item: Lee SB
  item: Robyt JF
journal: Carbohydr Res
pages: 47-53
published year: 2001
volume: 336
references: http://www.ncbi.nlm.nih.gov/pubmed/11675025

Crystal structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011 complexed with 1-deoxynojirimycin at 2.0 A resolution.
type: BibliographicResource
authors:
  item: Kanai R
  item: Haga K
  item: Yamane K
  item: Harata K
journal: J Biochem (Tokyo)
pages: 593-8
published year: 2001
volume: 129
references: http://www.ncbi.nlm.nih.gov/pubmed/11275559
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase.
type: BibliographicResource
authors:
  item: van der Veen BA
  item: Leemhuis H
  item: Kralj S
  item: Uitdehaag JC
  item: Dijkstra BW
  item: Dijkhuizen L
journal: J Biol Chem
pages: 44557-62
published year: 2001
volume: 276
references: http://www.ncbi.nlm.nih.gov/pubmed/11555657

Enzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase.
type: BibliographicResource
authors:
  item: Uitdehaag JC
  item: van der Veen BA
  item: Dijkhuizen L
  item: Elber R
  item: Dijkstra BW
journal: Proteins
pages: 327-35
published year: 2001
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/11288183

Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase.
type: BibliographicResource
authors:
  item: Leemhuis H
  item: Dijkstra BW
  item: Dijkhuizen L
journal: FEBS Lett
pages: 189-92
published year: 2002
volume: 514
references: http://www.ncbi.nlm.nih.gov/pubmed/11943149

Modulation of cyclizing activity and thermostability of cyclodextrin glucanotransferase and its application as an antistaling enzyme.
type: BibliographicResource
authors:
  item: Lee SH
  item: Choi JH
  item: Kim YB
  item: Park KH
  item: Kim YW
  item: Lee S
  item: Auh JH
  item: Yoo SS
  item: Kim TJ
  item: Kim JW
  item: Kim ST
  item: Rho HJ
journal: J Agric Food Chem
pages: 1411-5
published year: 2002
volume: 50
references: http://www.ncbi.nlm.nih.gov/pubmed/11879012

Maltodextrin-dependent crystallization of cyclomaltodextrin glucanotransferase from Bacillus circulans.
type: BibliographicResource
authors:
  item: Lawson CL
  item: Bergsma J
  item: Bruinenberg PM
  item: de Vries G
  item: Dijkhuizen L
  item: Dijkstra BW
journal: J Mol Biol
pages: 807-9
published year: 1990
volume: 214
references: http://www.ncbi.nlm.nih.gov/pubmed/2143786

Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain.
type: BibliographicResource
authors:
  item: Rashid N
  item: Cornista J
  item: Ezaki S
  item: Fukui T
  item: Atomi H
  item: Imanaka T
journal: J Bacteriol
pages: 777-84
published year: 2002
volume: 184
references: http://www.ncbi.nlm.nih.gov/pubmed/11790748

The remote substrate binding subsite -6 in cyclodextrin-glycosyltransferase controls the transferase activity of the enzyme via an induced-fit mechanism.
type: BibliographicResource
authors:
  item: Leemhuis H
  item: Uitdehaag JC
  item: Rozeboom HJ
  item: Dijkstra BW
  item: Dijkhuizen L
journal: J Biol Chem
pages: 1113-9
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/11696539
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystallization and preliminary X-ray diffraction studies of alpha-cyclodextrin glucanotransferase isolated from Bacillus macerans.
type: BibliographicResource
authors:
  item: Choe HW
  item: Park KS
  item: Labahn J
  item: Granzin J
  item: Kim CJ
  item: Buldt G
journal: Acta Crystallogr D Biol Crystallogr
pages: 348-9
published year: 2003
volume: 59
references: http://www.ncbi.nlm.nih.gov/pubmed/12554949

Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: the role of alanine 230 in acceptor subsite +1.
type: BibliographicResource
authors:
  item: Leemhuis H
  item: Rozeboom HJ
  item: Wilbrink M
  item: Euverink GJ
  item: Dijkstra BW
  item: Dijkhuizen L
journal: Biochemistry
pages: 7518-26
published year: 2003
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/12809508
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activity.
type: BibliographicResource
authors:
  item: Leemhuis H
  item: Rozeboom HJ
  item: Dijkstra BW
  item: Dijkhuizen L
journal: FEBS Lett
pages: 47-51
published year: 2003
volume: 541
references: http://www.ncbi.nlm.nih.gov/pubmed/12706817
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Effects of essential carbohydrate/aromatic stacking interaction with Tyr100 and Phe259 on substrate binding of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp. 1011.
type: BibliographicResource
authors:
  item: Haga K
  item: Kanai R
  item: Sakamoto O
  item: Aoyagi M
  item: Harata K
  item: Yamane K
journal: J Biochem (Tokyo)
pages: 881-91
published year: 2003
volume: 134
references: http://www.ncbi.nlm.nih.gov/pubmed/14769878
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Engineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exo-specificity.
type: BibliographicResource
authors:
  item: Leemhuis H
  item: Kragh KM
  item: Dijkstra BW
  item: Dijkhuizen L
journal: J Biotechnol
pages: 203-12
published year: 2003
volume: 103
references: http://www.ncbi.nlm.nih.gov/pubmed/12890607

Crystal structure of the covalent intermediate of amylosucrase from Neisseria polysaccharea.
type: BibliographicResource
authors:
  item: Jensen MH
  item: Mirza O
  item: Albenne C
  item: Remaud-Simeon M
  item: Monsan P
  item: Gajhede M
  item: Skov LK
journal: Biochemistry
pages: 3104-10
published year: 2004
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/15023061

Single amino acid mutations interchange the reaction specificities of cyclodextrin glycosyltransferase and the acarbose-modifying enzyme acarviosyl transferase.
type: BibliographicResource
authors:
  item: Leemhuis H
  item: Wehmeier UF
  item: Dijkhuizen L
journal: Biochemistry
pages: 13204-13
published year: 2004
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/15476414

Improvement of cyclodextrin glucanotransferase as an antistaling enzyme by error-prone PCR.
type: BibliographicResource
authors:
  item: Shim JH
  item: Spendler T
  item: Moon TW
  item: Park KH
  item: Kim YW
  item: Kim TJ
  item: Chae HY
  item: Park JH
  item: Cha H
  item: Kim JW
  item: Kim YR
  item: Schaefer T
journal: Protein Eng Des Sel
pages: 205-11
published year: 2004
volume: 17
references: http://www.ncbi.nlm.nih.gov/pubmed/15096580

Engineering a heavy atom derivative for the X-ray structure analysis of cyclodextrin glycosyltransferase.
type: BibliographicResource
authors:
  item: Klein C
  item: Vogel W
  item: Bender H
  item: Schulz GE
journal: Protein Eng
pages: 65-7
published year: 1990
volume: 4
references: http://www.ncbi.nlm.nih.gov/pubmed/2149760

Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site.
type: BibliographicResource
authors:
  item: Kanai R
  item: Haga K
  item: Akiba T
  item: Yamane K
  item: Harata K
journal: Protein Sci
pages: 457-65
published year: 2004
volume: 13
references: http://www.ncbi.nlm.nih.gov/pubmed/14739329
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge.
type: BibliographicResource
authors:
  item: Leemhuis H
  item: Rozeboom HJ
  item: Dijkstra BW
  item: Dijkhuizen L
journal: Proteins
pages: 128-34
published year: 2004
volume: 54
references: http://www.ncbi.nlm.nih.gov/pubmed/14705029
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Investigation of the active site of Bacillus macerans cyclodextrin glucanotransferase by use of modified maltooligosaccharides.
type: BibliographicResource
authors:
  item: Abe S
  item: Nagamine Y
  item: Omichi K
  item: Ikenaka T
journal: J Biochem (Tokyo)
pages: 756-61
published year: 1991
volume: 110
references: http://www.ncbi.nlm.nih.gov/pubmed/1838375

Structure of cyclodextrin glycosyltransferase refined at 2.0 A resolution.
type: BibliographicResource
authors:
  item: Klein C
  item: Schulz GE
journal: J Mol Biol
medline id: 91171298
pages: 737-50
published year: 1991
volume: 217
references: http://www.ncbi.nlm.nih.gov/pubmed/1826034
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P30920
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

The transglycosylation reaction of cyclodextrin glucanotransferase is operated by a Ping-Pong mechanism.
type: BibliographicResource
authors:
  item: Nakamura A
  item: Haga K
  item: Yamane K
journal: FEBS Lett
pages: 66-70
published year: 1994
volume: 337
references: http://www.ncbi.nlm.nih.gov/pubmed/8276116

Cyclodextrin formation by the thermostable alpha-amylase of Thermoanaerobacterium thermosulfurigenes EM1 and reclassification of the enzyme as a cyclodextrin glycosyltransferase.
type: BibliographicResource
authors:
  item: Wind RD
  item: Liebl W
  item: Buitelaar RM
  item: Penninga D
  item: Spreinat A
  item: Dijkhuizen L
  item: Bahl H
journal: Appl Environ Microbiol
pages: 1257-65
published year: 1995
volume: 61
references: http://www.ncbi.nlm.nih.gov/pubmed/7747949

Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme.
type: BibliographicResource
authors:
  item: Fujiwara S
  item: Kakihara H
  item: Woo KB
  item: Lejeune A
  item: Kanemoto M
  item: Sakaguchi K
  item: Imanaka T
journal: Appl Environ Microbiol
pages: 4016-25
published year: 1992
volume: 58
references: http://www.ncbi.nlm.nih.gov/pubmed/1476442

1cxkA01
type: Pdb
catalytic residue: ; ;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cxk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxk
comment: mutant D229N, E257Q

1d3cA01
type: Pdb
catalytic residue: ; ;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1d3c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d3c
comment: mutant D229N, E257Q

1pj9A01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1pj9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pj9
comment: mutant T185S, T186Y, N188D, K192R

3cgtA01
type: Pdb
catalytic residue: ASP 229; ;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 3cgt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3cgt
comment: mutant E257A

5cgtA01
type: Pdb
catalytic residue: ;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 5cgt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5cgt
comment: mutant D229A

1a47A01
type: Pdb
catalytic residue: ASP 230;GLU 258;HIS 328;ASP 329
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 140;ILE 191;ASP 200;HIS 234(Calcium-2)
references: 1a47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a47

1cdgA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cdg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cdg

1cgtA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cgt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cgt

1cguA01
type: Pdb
catalytic residue: ;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cgu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cgu
comment: mutant D229A

1cgvA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cgv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cgv
comment: mutant Y195F

1cgwA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cgw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cgw
comment: mutant Y195G

1cgxA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cgx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cgx
comment: mutant Y195L

1cgyA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cgy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cgy
comment: mutant Y195W

1ciuA01
type: Pdb
catalytic residue: ASP 230;GLU 258;HIS 328;ASP 329
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 140;ILE 191;ASP 200;HIS 234(Calcium-2)
references: 1ciu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ciu

1cxeA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cxe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxe

1cxfA01
type: Pdb
catalytic residue: ; ;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cxf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxf
comment: mutant D229N, E257Q

1cxgA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cxg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxg

1cxhA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxh

1cxiA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxi

1cxlA01
type: Pdb
catalytic residue: ASP 229; ;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1cxl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxl
comment: mutant E257Q

1cygA01
type: Pdb
catalytic residue: ASP 225;GLU 253;HIS 323;ASP 324
cofactor binding residue: ASP 24;ASN 26;ASN 29;ASN 30;GLY 48;ASP 50(Calcium-1);ASN 135;ILE 186;ASP 195;HIS 229(Calcium-2)
references: 1cyg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cyg

1d7fA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199; (Calcium-2)
references: 1d7f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d7f
comment: mutant H233N

1d7fB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199; (Calcium-2)
references: 1d7f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d7f
comment: mutant H233N

1dedA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199; (Calcium-2)
references: 1ded
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ded
comment: mutant H233N

1dedB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199; (Calcium-2)
references: 1ded
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ded
comment: mutant H233N

1dijA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1dij
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dij
comment: mutant Y195F

1dtuA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1dtu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dtu
comment: mutant Y89D, S146P

1eo5A01
type: Pdb
catalytic residue: ; ;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1eo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eo5
comment: mutant D229A, E257A

1eo7A01
type: Pdb
catalytic residue: ; ;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1eo7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eo7
comment: mutant D229A, E257A

1i75A01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1i75
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i75

1i75B01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1i75
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i75

1kckA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1kck
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kck
comment: mutant N193G

1kclA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1kcl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kcl
comment: mutant G179L

1ot1A01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1ot1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ot1
comment: mutant D135A

1ot2A01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1ot2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ot2
comment: mutant D135N

1pamA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1pam
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pam

1pamB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1pam
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pam

1pezA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1pez
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pez
comment: mutant A230V

1tcmA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1tcm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tcm
comment: mutant W616A

1tcmB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1tcm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tcm
comment: mutant W616A

1ukqA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1ukq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ukq

1ukqB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1ukq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ukq

1uksA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1uks
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1uks
comment: mutant F183L, F259L

1uksB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1uks
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1uks
comment: mutant F183L, F259L

1uktA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1ukt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ukt
comment: mutant Y100L

1uktB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1ukt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ukt
comment: mutant Y100L

1v3jA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1v3j
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v3j
comment: mutant F283L

1v3jB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1v3j
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v3j
comment: mutant F283L

1v3kA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1v3k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v3k
comment: mutant F283Y

1v3kB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1v3k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v3k
comment: mutant F283Y

1v3lA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1v3l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v3l
comment: mutant F283L

1v3lB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1v3l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v3l
comment: mutant F283L

1v3mA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1v3m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v3m
comment: mutant F283Y

1v3mB01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 1v3m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v3m
comment: mutant F283Y

2cxgA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 2cxg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cxg

2dijA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 2dij
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2dij
comment: mutant Y195F

4cgtA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 4cgt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4cgt
comment: mutant deletion 145-150, F151D

6cgtA01
type: Pdb
catalytic residue: ASP 229;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 6cgt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6cgt
comment: mutant L194T

7cgtA01
type: Pdb
catalytic residue: ;GLU 257;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 7cgt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7cgt
comment: mutant D229A

8cgtA01
type: Pdb
catalytic residue: ASP 229; ;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 8cgt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8cgt
comment: mutant E257A

9cgtA01
type: Pdb
catalytic residue: ASP 229; ;HIS 327;ASP 328
cofactor binding residue: ASP 27;ASN 29;ASN 32;ASN 33;GLY 51;ASP 53(Calcium-1);ASN 139;ILE 190;ASP 199;HIS 233(Calcium-2)
references: 9cgt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9cgt
comment: mutant E257A

Calcium
type: KeggCofactor
compound type: divalent metal (Ca2+, Mg2+)
references: KEGG:C00076
references: CHEBI:29108
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Cyclomaltodextrin
type: KeggProduct
compound type: polysaccharide
references: KEGG:C00973
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Starch
type: KeggSubstrate
compound type: polysaccharide
references: KEGG:C00369

Maltodextrin
type: KeggSubstrate
type: KeggProduct
compound type: polysaccharide
references: KEGG:C01935

Bacillus macerans amylase
type: KeggEnzyme

cyclodextrin glucanotransferase
type: KeggEnzyme

alpha-cyclodextrin glucanotransferase
type: KeggEnzyme

alpha-cyclodextrin glycosyltransferase
type: KeggEnzyme

beta-cyclodextrin glucanotransferase
type: KeggEnzyme

beta-cyclodextrin glycosyltransferase
type: KeggEnzyme

gamma-cyclodextrin glycosyltransferase
type: KeggEnzyme

cyclodextrin glycosyltransferase
type: KeggEnzyme

cyclomaltodextrin glucotransferase
type: KeggEnzyme

cyclomaltodextrin glycosyltransferase
type: KeggEnzyme

konchizaimu
type: KeggEnzyme

alpha-1,4-glucan 4-glycosyltransferase, cyclizing
type: KeggEnzyme

BMA
type: KeggEnzyme

CGTase
type: KeggEnzyme

neutral-cyclodextrin glycosyltransferase
type: KeggEnzyme

1,4-alpha-D-glucan 4-alpha-D-(1,4-alpha-D-glucano)-transferase(cyclizing)
type: KeggEnzyme