D00165
type: Enzyme
active site residues resources: P04063
active site residues resources: P00691
active site residues resources: P56271
active site residues resources: P10529
active site residues resources: P29957
active site residues resources: P56634
active site residues resources: P00690
active site residues resources: P04745
active site residues resources: P04746
cath: TIM Barrel
cath: Immunoglobulin-like
csa: 1amy
ec: https://purl.uniprot.org/enzyme/3.2.1.1
kegg cofactor: Calcium
kegg cofactor: Chloride
kegg enzyme: alpha-amylase
kegg pathway: Starch and sucrose metabolism
kegg product: Starch
kegg product: Dextrin
kegg substrate: Starch
kegg substrate: H2O
pdb: 1amyA01
pdb: 1avaA01
pdb: 1avaB01
pdb: 1bg9A01
pdb: 1bagA01
pdb: 2aaaA01
pdb: 2taaA01
pdb: 6taaA01
pdb: 7taaA01
pdb: 1aqhA01
pdb: 1aqmA01
pdb: 1b0iA01
pdb: 1clvA01
pdb: 1jaeA01
pdb: 1tmqA01
pdb: 1viwA01
pdb: 1bvnP01
pdb: 1dhkA01
pdb: 1jfhA01
pdb: 1oseA01
pdb: 1pifA01
pdb: 1pigA01
pdb: 1ppiA01
pdb: 1smdA01
pdb: 1bsiA01
pdb: 1cpuA01
pdb: 1hnyA01
pdb: 1amyA02
pdb: 1avaA02
pdb: 1avaB02
pdb: 1bg9A02
pdb: 1bagA02
pdb: 2aaaA02
pdb: 2taaA02
pdb: 6taaA02
pdb: 7taaA02
pdb: 1aqhA02
pdb: 1aqmA02
pdb: 1b0iA02
pdb: 1clvA02
pdb: 1jaeA02
pdb: 1tmqA02
pdb: 1viwA02
pdb: 1bvnP02
pdb: 1dhkA02
pdb: 1jfhA02
pdb: 1oseA02
pdb: 1pifA02
pdb: 1pigA02
pdb: 1ppiA02
pdb: 1smdA02
pdb: 1bsiA02
pdb: 1cpuA02
pdb: 1hnyA02
rlcp: p3
uniprot: P04063
uniprot: P00691
uniprot: P56271

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

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

Starch and sucrose metabolism
type: KeggPathway
references: KEGG:MAP00500

The three-dimensional structure of [alpha]-amylase from porcine pancreas at 5 A resolution - the active-site location.
type: BibliographicResource
authors:
  item: Payan F
  item: Haser R
  item: Pierrot M
  item: Frey M
  item: Astier JP
  item: Abadie B
  item: Duee B
  item: Buisson G
journal: Acta Crystallogr B
pages: 416-21
published year: 1980
volume: 36
references: P00690
comment: X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS)

Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus.
type: BibliographicResource
authors:
  item: Boel E
  item: Woldike HF
  item: Brady L
  item: Brzozowski AM
  item: Derewenda Z
  item: Dodson GG
  item: Jensen VJ
  item: Petersen SB
  item: Swift H
  item: Thim L
journal: Biochemistry
pages: 6244-9
published year: 1990
volume: 29
references: http://www.ncbi.nlm.nih.gov/pubmed/2207069
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P56271
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)

Structure and biosynthesis of the xylose-containing carbohydrate moiety of rice alpha-amylase.
type: BibliographicResource
authors:
  item: Hayashi M
  item: Tsuru A
  item: Mitsui T
  item: Takahashi N
  item: Hanzawa H
  item: Arata Y
  item: Akazawa T
journal: Eur J Biochem
pages: 287-95
published year: 1990
volume: 191
references: http://www.ncbi.nlm.nih.gov/pubmed/2143471

Structure and molecular model refinement of Aspergillus oryzae (TAKA) alpha-amylase: an application of the simulated-annealing method.
type: BibliographicResource
authors:
  item: Swift HJ
  item: Brady L
  item: Derewenda ZS
  item: Dodson EJ
  item: Dodson GG
  item: Turkenburg JP
  item: Wilkinson AJ
journal: Acta Crystallogr B
pages: 535-44
published year: 1991
volume: 47
references: http://www.ncbi.nlm.nih.gov/pubmed/1930835
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Biological variation in the catalytic concentration of pancreatic alpha-amylase and triacylglycerol lipase in serum.
type: BibliographicResource
authors:
  item: Huguet J
  item: Fuentes-Arderiu X
journal: Scand J Clin Lab Invest
pages: 735-8
published year: 1991
volume: 51
references: http://www.ncbi.nlm.nih.gov/pubmed/1806988

Alteration of bond-cleavage pattern in the hydrolysis catalyzed by Saccharomycopsis alpha-amylase altered by site-directed mutagenesis.
type: BibliographicResource
authors:
  item: Matsui I
  item: Ishikawa K
  item: Miyairi S
  item: Fukui S
  item: Honda K
journal: Biochemistry
pages: 5232-6
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1606147

Site-directed mutagenesis of active site residues in Bacillus subtilis alpha-amylase.
type: BibliographicResource
authors:
  item: Takase K
  item: Matsumoto T
  item: Mizuno H
  item: Yamane K
journal: Biochim Biophys Acta
pages: 281-8
published year: 1992
volume: 1120
references: http://www.ncbi.nlm.nih.gov/pubmed/1576155

Purification and some properties of a Haim-sensitive alpha-amylase from newly isolated Bacillus sp. No. 195.
type: BibliographicResource
authors:
  item: Kawaguchi T
  item: Nagae H
  item: Murao S
  item: Arai M
journal: Biosci Biotechnol Biochem
pages: 1792-6
published year: 1992
volume: 56
references: http://www.ncbi.nlm.nih.gov/pubmed/1369074

Site-directed mutagenesis of catalytic active-site residues of Taka-amylase A.
type: BibliographicResource
authors:
  item: Nagashima T
  item: Tada S
  item: Kitamoto K
  item: Gomi K
  item: Kumagai C
  item: Toda H
journal: Biosci Biotechnol Biochem
pages: 207-10
published year: 1992
volume: 56
references: http://www.ncbi.nlm.nih.gov/pubmed/1377974

Mechanism of hydrolyses of phenyl alpha-maltosides catalyzed by taka-amylase A.
type: BibliographicResource
authors:
  item: Isoda Y
  item: Shimizu Y
  item: Hashimoto A
  item: Fujiwara H
  item: Nitta Y
  item: Kagemoto A
journal: J Biochem (Tokyo)
pages: 204-9
published year: 1992
volume: 111
references: http://www.ncbi.nlm.nih.gov/pubmed/1569044

Crystallization and preliminary X-ray crystallographic analysis of alpha-amylase from Bacillus subtilis.
type: BibliographicResource
authors:
  item: Chang C
  item: Kim KK
  item: Hwang KY
  item: Choi MU
  item: Suh SW
journal: J Mol Biol
pages: 235-8
published year: 1993
volume: 229
references: http://www.ncbi.nlm.nih.gov/pubmed/8421303

Molecular structure of taka-amylase A. I. Backbone chain folding at 3 A resolution.
type: BibliographicResource
authors:
  item: Matsuura Y
  item: Kusunoki M
  item: Harada W
  item: Tanaka N
  item: Iga Y
  item: Yasuoka N
  item: Toda H
  item: Narita K
  item: Kakudo M
journal: J Biochem (Tokyo)
pages: 1555-8
published year: 1980
volume: 87
references: http://www.ncbi.nlm.nih.gov/pubmed/6156152
references: P10529
comment: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS)

Crystallization and preliminary X-ray studies of wild type and catalytic-site mutant alpha-amylase from Bacillus subtilis.
type: BibliographicResource
authors:
  item: Mizuno H
  item: Morimoto Y
  item: Tsukihara T
  item: Matsumoto T
  item: Takase K
journal: J Mol Biol
pages: 1282-3
published year: 1993
volume: 234
references: http://www.ncbi.nlm.nih.gov/pubmed/8263932

Structure and molecular model refinement of pig pancreatic alpha-amylase at 2.1 A resolution.
type: BibliographicResource
authors:
  item: Qian M
  item: Haser R
  item: Payan F
journal: J Mol Biol
pages: 785-99
published year: 1993
volume: 231
references: http://www.ncbi.nlm.nih.gov/pubmed/8515451
references: P00690
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND REVISIONS

The catalytic mechanism of alpha-amylases based upon enzyme crystal structures and model building calculations.
type: BibliographicResource
authors:
  item: Mazur AK
  item: Haser R
  item: Payan F
journal: Biochem Biophys Res Commun
pages: 297-302
published year: 1994
volume: 204
references: http://www.ncbi.nlm.nih.gov/pubmed/7945374

The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution.
type: BibliographicResource
authors:
  item: Qian M
  item: Haser R
  item: Buisson G
  item: Duee E
  item: Payan F
journal: Biochemistry
pages: 6284-94
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8193143
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00690
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)

alpha-Amylases from Thermoactinomyces vulgaris: characteristics, primary structure and structure prediction.
type: BibliographicResource
authors:
  item: Hansen G
  item: Heese O
  item: Hohne WE
  item: Hofemeister B
journal: Int J Pept Protein Res
pages: 245-52
published year: 1994
volume: 44
references: http://www.ncbi.nlm.nih.gov/pubmed/7822101

Crystallization and preliminary X-ray diffraction studies of the alpha-amylase inhibitor coded 0.19 from wheat kernel.
type: BibliographicResource
authors:
  item: Miyazaki T
  item: Morimoto T
  item: Fukuyama K
  item: Matsubara H
journal: J Biochem (Tokyo)
pages: 179-81
published year: 1994
volume: 115
references: http://www.ncbi.nlm.nih.gov/pubmed/8206864

Crystal and molecular structure of barley alpha-amylase.
type: BibliographicResource
authors:
  item: Kadziola A
  item: Abe J
  item: Svensson B
  item: Haser R
journal: J Mol Biol
pages: 104-21
published year: 1994
volume: 239
references: http://www.ncbi.nlm.nih.gov/pubmed/8196040
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04063
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)

Refined molecular structure of pig pancreatic alpha-amylase at 2.1 A resolution.
type: BibliographicResource
authors:
  item: Larson SB
  item: Greenwood A
  item: Cascio D
  item: Day J
  item: McPherson A
journal: J Mol Biol
pages: 1560-84
published year: 1994
volume: 235
references: http://www.ncbi.nlm.nih.gov/pubmed/8107092

Characterization, crystallization and preliminary X-ray crystallographic analysis of the complex between barley alpha-amylase and the bifunctional alpha-amylase/subtilisin inhibitor from barley seeds.
type: BibliographicResource
authors:
  item: Vallee F
  item: Kadziola A
  item: Bourne Y
  item: Abe J
  item: Svensson B
  item: Haser R
journal: J Mol Biol
pages: 368-71
published year: 1994
volume: 236
references: http://www.ncbi.nlm.nih.gov/pubmed/8107117

The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat.
type: BibliographicResource
authors:
  item: Wiegand G
  item: Epp O
  item: Huber R
journal: J Mol Biol
pages: 99-110
published year: 1995
volume: 247
references: http://www.ncbi.nlm.nih.gov/pubmed/7897663
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00690
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH INHIBITOR

Subsite profile of the active center of porcine pancreatic alpha-amylase. Kinetic studies using maltooligosaccharides as substrates.
type: BibliographicResource
authors:
  item: Prodanov E
  item: Seigner C
  item: Marchis-Mouren G
journal: Biochem Biophys Res Commun
pages: 75-81
published year: 1984
volume: 122
references: http://www.ncbi.nlm.nih.gov/pubmed/6611158

The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes.
type: BibliographicResource
authors:
  item: Brayer GD
  item: Luo Y
  item: Withers SG
journal: Protein Sci
pages: 1730-42
published year: 1995
volume: 4
references: http://www.ncbi.nlm.nih.gov/pubmed/8528071
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04746
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)

Structure of Human Salivary [alpha]-Amylase at 1.6 A Resolution: Implications for its Role in the Oral Cavity.
type: BibliographicResource
authors:
  item: Ramasubbu N
  item: Paloth V
  item: Luo Y
  item: Brayer GD
  item: Levine MJ
journal: Acta Crystallogr D Biol Crystallogr
pages: 435-46
published year: 1996
volume: 52
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04745
comment: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)

Production and certification of an enzyme reference material for pancreatic alpha-amylase (CRM 476).
type: BibliographicResource
authors:
  item: Gubern G
  item: Lessinger JM
  item: Lorentz K
  item: Vassault A
  item: Canalias F
  item: Gella FJ
  item: Colinet E
  item: Profilis C
  item: Calam DH
  item: Ceriotti F
  item: Dufaux J
  item: Hadjivassiliou AG
journal: Clin Chim Acta
pages: 145-62
published year: 1996
volume: 251
references: http://www.ncbi.nlm.nih.gov/pubmed/8862470

Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose.
type: BibliographicResource
authors:
  item: Gilles C
  item: Astier JP
  item: Marchis-Mouren G
  item: Cambillau C
  item: Payan F
journal: Eur J Biochem
pages: 561-9
published year: 1996
volume: 238
references: http://www.ncbi.nlm.nih.gov/pubmed/8681972
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00690
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND REVISIONS

Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics.
type: BibliographicResource
authors:
  item: Machius M
  item: Vertesy L
  item: Huber R
  item: Wiegand G
journal: J Mol Biol
pages: 409-21
published year: 1996
volume: 260
references: http://www.ncbi.nlm.nih.gov/pubmed/8757803
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00690
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)

Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23.
type: BibliographicResource
authors:
  item: Aghajari N
  item: Feller G
  item: Gerday C
  item: Haser R
journal: Protein Sci
pages: 2128-9
published year: 1996
volume: 5
references: http://www.ncbi.nlm.nih.gov/pubmed/8897615

Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex.
type: BibliographicResource
authors:
  item: Bompard-Gilles C
  item: Rousseau P
  item: Rouge P
  item: Payan F
journal: Structure
pages: 1441-52
published year: 1996
volume: 4
references: http://www.ncbi.nlm.nih.gov/pubmed/8994970
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00690
comment: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF COMPLEX WITH INHIBITOR

Unequivocal identification of Asp-214 as the catalytic nucleophile of Saccharomyces cerevisiae alpha-glucosidase using 5-fluoro glycosyl fluorides.
type: BibliographicResource
authors:
  item: McCarter JD
  item: Withers SG
journal: J Biol Chem
pages: 6889-94
published year: 1996
volume: 271
references: http://www.ncbi.nlm.nih.gov/pubmed/8636115

Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0 A resolution.
type: BibliographicResource
authors:
  item: Brzozowski AM
  item: Davies GJ
journal: Biochemistry
pages: 10837-45
published year: 1997
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/9283074
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P10529
comment: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS)

Effect of pressure on the mechanism of hydrolysis of maltotetraose, maltopentaose, and maltohexose catalyzed by porcine pancreatic alpha-amylase.
type: BibliographicResource
authors:
  item: Matsumoto T
  item: Makimoto S
  item: Taniguchi Y
journal: Biochim Biophys Acta
pages: 243-50
published year: 1997
volume: 1343
references: http://www.ncbi.nlm.nih.gov/pubmed/9434115

Structure and possible catalytic residues of Taka-amylase A.
type: BibliographicResource
authors:
  item: Matsuura Y
  item: Kusunoki M
  item: Harada W
  item: Kakudo M
journal: J Biochem (Tokyo)
pages: 697-702
published year: 1984
volume: 95
references: http://www.ncbi.nlm.nih.gov/pubmed/6609921
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P10529
comment: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS)

The alpha-amylase from the yellow meal worm: complete primary structure, crystallization and preliminary X-ray analysis.
type: BibliographicResource
authors:
  item: Strobl S
  item: Gomis-Ruth FX
  item: Maskos K
  item: Frank G
  item: Huber R
  item: Glockshuber R
journal: FEBS Lett
pages: 109-14
published year: 1997
volume: 409
references: http://www.ncbi.nlm.nih.gov/pubmed/9199514

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00165#41
type: BibliographicResource
title: Improved activity and modulated action pattern obtained by random mutagenesis at the fourth beta-alpha loop involved in substrate binding to the catalytic (beta/alpha)8-barrel domain of barley alpha-amylase 1.
authors:
  item: Matsui I
  item: Svensson B
journal: J Biol Chem
pages: 22456-63
published year: 1997
volume: 272
references: http://www.ncbi.nlm.nih.gov/pubmed/9278396

Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03 A resolution.
type: BibliographicResource
authors:
  item: Qian M
  item: Spinelli S
  item: Driguez H
  item: Payan F
journal: Protein Sci
pages: 2285-96
published year: 1997
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/9385631
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00690
comment: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS)

Structure, function and protein engineering of starch-degrading enzymes.
type: BibliographicResource
authors:
  item: Gottschalk TE
  item: Juge N
  item: McGuire KA
  item: Cottaz S
  item: Roepstorff P
  item: Driguez H
  item: Williamson G
  item: Svensson B
  item: Fierobe HP
  item: Mirgorodskaya E
  item: Clarke AJ
  item: Tull D
  item: Sigurskjold BW
  item: Christensen T
  item: Payre N
  item: Frandsen TP
journal: Biochem Soc Trans
pages: 198-204
published year: 1998
volume: 26
references: http://www.ncbi.nlm.nih.gov/pubmed/9649747

Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose.
type: BibliographicResource
authors:
  item: Fujimoto Z
  item: Takase K
  item: Doui N
  item: Momma M
  item: Matsumoto T
  item: Mizuno H
journal: J Mol Biol
pages: 393-407
published year: 1998
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/9514750
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00691
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 42-466

Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis.
type: BibliographicResource
authors:
  item: Kadziola A
  item: Sogaard M
  item: Svensson B
  item: Haser R
journal: J Mol Biol
pages: 205-17
published year: 1998
volume: 278
references: http://www.ncbi.nlm.nih.gov/pubmed/9571044
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structure of yellow meal worm alpha-amylase at 1.64 A resolution.
type: BibliographicResource
authors:
  item: Strobl S
  item: Maskos K
  item: Betz M
  item: Wiegand G
  item: Huber R
  item: Gomis-Ruth FX
  item: Glockshuber R
journal: J Mol Biol
pages: 617-28
published year: 1998
volume: 278
references: http://www.ncbi.nlm.nih.gov/pubmed/9600843
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P56634
comment: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS)

Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor.
type: BibliographicResource
authors:
  item: Aghajari N
  item: Feller G
  item: Gerday C
  item: Haser R
journal: Protein Sci
pages: 564-72
published year: 1998
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/9541387
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P29957
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-477

Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level.
type: BibliographicResource
authors:
  item: Aghajari N
  item: Feller G
  item: Gerday C
  item: Haser R
journal: Structure
pages: 1503-16
published year: 1998
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/9862804
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution.
type: BibliographicResource
authors:
  item: Strobl S
  item: Maskos K
  item: Wiegand G
  item: Huber R
  item: Gomis-Ruth FX
  item: Glockshuber R
journal: Structure
pages: 911-21
published year: 1998
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/9687373
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P56634
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00165#5
type: BibliographicResource
title: On porcine pancreatic alpha-amylase action: kinetic evidence for the binding of two maltooligosaccharide molecules (maltose, maltotriose and o-nitrophenylmaltoside) by inhibition studies. Correlation with the five-subsite energy profile.
authors:
  item: Seigner C
  item: Prodanov E
  item: Marchis-Mouren G
journal: Eur J Biochem
pages: 161-8
published year: 1985
volume: 148
references: http://www.ncbi.nlm.nih.gov/pubmed/3872211

Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution.
type: BibliographicResource
authors:
  item: Vallee F
  item: Kadziola A
  item: Bourne Y
  item: Juy M
  item: Rodenburg KW
  item: Svensson B
  item: Haser R
journal: Structure
pages: 649-59
published year: 1998
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/9634702
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04063
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH BASI

A plant-seed inhibitor of two classes of alpha-amylases: X-ray analysis of Tenebrio molitor larvae alpha-amylase in complex with the bean Phaseolus vulgaris inhibitor.
type: BibliographicResource
authors:
  item: Nahoum V
  item: Farisei F
  item: Le-Berre-Anton V
  item: Egloff MP
  item: Rouge P
  item: Poerio E
  item: Payan F
journal: Acta Crystallogr D Biol Crystallogr
pages: 360-2
published year: 1999
volume: 55
references: http://www.ncbi.nlm.nih.gov/pubmed/10089450
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Amylose chain behavior in an interacting context. III. Complete occupancy of the AMY2 barley alpha-amylase cleft and comparison with biochemical data.
type: BibliographicResource
authors:
  item: Andre G
  item: Buleon A
  item: Haser R
  item: Tran V
journal: Biopolymers
pages: 751-62
published year: 1999
volume: 50
references: http://www.ncbi.nlm.nih.gov/pubmed/10547530

Post-translational processing of two alpha-amylase inhibitors and an arcelin from the common bean, Phaseolus vulgaris.
type: BibliographicResource
authors:
  item: Young NM
  item: Thibault P
  item: Watson DC
  item: Chrispeels MJ
journal: FEBS Lett
medline id: 99198742
pages: 203-6
published year: 1999
volume: 446
references: http://www.ncbi.nlm.nih.gov/pubmed/10100643

Characterization of a thermostable alpha-amylase from a thermophilic Streptomyces megasporus strain SD12.
type: BibliographicResource
authors:
  item: Dey S
  item: Agarwal SO
journal: Indian J Biochem Biophys
pages: 150-7
published year: 1999
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/10650713

Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution.
type: BibliographicResource
authors:
  item: Kamitori S
  item: Kondo S
  item: Okuyama K
  item: Yokota T
  item: Shimura Y
  item: Tonozuka T
  item: Sakano Y
journal: J Mol Biol
pages: 907-21
published year: 1999
volume: 287
references: http://www.ncbi.nlm.nih.gov/pubmed/10222200

Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase.
type: BibliographicResource
authors:
  item: Hasegawa K
  item: Kubota M
  item: Matsuura Y
journal: Protein Eng
pages: 819-24
published year: 1999
volume: 12
references: http://www.ncbi.nlm.nih.gov/pubmed/10556241

Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris.
type: BibliographicResource
authors:
  item: Rydberg EH
  item: Brayer GD
  item: Withers SG
  item: Sidhu G
  item: Vo HC
  item: Hewitt J
  item: Cote HC
  item: Wang Y
  item: Numao S
  item: MacGillivray RT
  item: Overall CM
journal: Protein Sci
pages: 635-43
published year: 1999
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/10091666
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Specific inhibition of insect alpha-amylases: yellow meal worm alpha-amylase in complex with the amaranth alpha-amylase inhibitor at 2.0 A resolution.
type: BibliographicResource
authors:
  item: Pereira PJ
  item: Lozanov V
  item: Patthy A
  item: Huber R
  item: Bode W
  item: Pongor S
  item: Strobl S
journal: Structure Fold Des
pages: 1079-88
published year: 1999
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/10508777
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structures of human pancreatic alpha-amylase in complex with carbohydrate and proteinaceous inhibitors.
type: BibliographicResource
authors:
  item: Nahoum V
  item: Roux G
  item: Anton V
  item: Rouge P
  item: Puigserver A
  item: Bischoff H
  item: Henrissat B
  item: Payan F
journal: Biochem J
pages: 201-8
published year: 2000
volume: 346 Pt 1
references: http://www.ncbi.nlm.nih.gov/pubmed/10657258

Purification and characterization of alpha-amylase from rat pancreatic acinar carcinoma. Comparison with pancreatic alpha-amylase.
type: BibliographicResource
authors:
  item: Reddy MK
  item: Heda GD
  item: Reddy JK
journal: Biochem J
pages: 681-7
published year: 1987
volume: 242
references: http://www.ncbi.nlm.nih.gov/pubmed/3496084

New type of starch-binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no. 195 alpha-amylase contributes to starch binding and raw starch degrading.
type: BibliographicResource
authors:
  item: Sumitani J
  item: Tottori T
  item: Kawaguchi T
  item: Arai M
journal: Biochem J
pages: 477-84
published year: 2000
volume: 350 Pt 2
references: http://www.ncbi.nlm.nih.gov/pubmed/10947962

Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques.
type: BibliographicResource
authors:
  item: Brayer GD
  item: Sidhu G
  item: Maurus R
  item: Rydberg EH
  item: Braun C
  item: Wang Y
  item: Nguyen NT
  item: Overall CM
  item: Withers SG
journal: Biochemistry
pages: 4778-91
published year: 2000
volume: 39
references: http://www.ncbi.nlm.nih.gov/pubmed/10769135
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Protein engineering of bacterial alpha-amylases.
type: BibliographicResource
authors:
  item: Nielsen JE
  item: Borchert TV
journal: Biochim Biophys Acta
pages: 253-74
published year: 2000
volume: 1543
references: http://www.ncbi.nlm.nih.gov/pubmed/11150610

Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase.
type: BibliographicResource
authors:
  item: Fitter J
  item: Heberle J
journal: Biophys J
pages: 1629-36
published year: 2000
volume: 79
references: http://www.ncbi.nlm.nih.gov/pubmed/10969023

Analysis of catalytic residues of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) by site-directed mutagenesis.
type: BibliographicResource
authors:
  item: Ichikawa K
  item: Tonozuka T
  item: Yokota T
  item: Shimura Y
  item: Sakano Y
journal: Biosci Biotechnol Biochem
pages: 2692-5
published year: 2000
volume: 64
references: http://www.ncbi.nlm.nih.gov/pubmed/11210138

Structural similarities and evolutionary relationships in chloride-dependent alpha-amylases.
type: BibliographicResource
authors:
  item: D'Amico S
  item: Gerday C
  item: Feller G
journal: Gene
pages: 95-105
published year: 2000
volume: 253
references: http://www.ncbi.nlm.nih.gov/pubmed/10925206

A functional raw starch-binding domain of barley alpha-amylase expressed in Escherichia coli.
type: BibliographicResource
authors:
  item: Tibbot BK
  item: Wong DW
  item: Robertson GH
journal: J Protein Chem
pages: 663-9
published year: 2000
volume: 19
references: http://www.ncbi.nlm.nih.gov/pubmed/11307950

Analysis of structural and physico-chemical parameters involved in the specificity of binding between alpha-amylases and their inhibitors.
type: BibliographicResource
authors:
  item: Da Silva MC
  item: de Sa MF
  item: Chrispeels MJ
  item: Togawa RC
  item: Neshich G
journal: Protein Eng
pages: 167-77
published year: 2000
volume: 13
references: http://www.ncbi.nlm.nih.gov/pubmed/10775658

Specificity modulation of barley alpha-amylase through biased random mutagenesis involving a conserved tripeptide in beta --> alpha loop 7 of the catalytic (beta/alpha)(8)-barrel domain.
type: BibliographicResource
authors:
  item: Gottschalk TE
  item: Tull D
  item: Aghajari N
  item: Haser R
  item: Svensson B
journal: Biochemistry
pages: 12844-54
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11669621

Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex.
type: BibliographicResource
authors:
  item: Qian M
  item: Nahoum V
  item: Bonicel J
  item: Bischoff H
  item: Henrissat B
  item: Payan F
journal: Biochemistry
pages: 7700-9
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11412124

Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity.
type: BibliographicResource
authors:
  item: Buisson G
  item: Duee E
  item: Haser R
  item: Payan F
journal: EMBO J
pages: 3909-16
published year: 1987
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/3502087
references: P00690
comment: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS)

Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
type: BibliographicResource
authors:
  item: MacGregor EA
  item: Janecek S
  item: Svensson B
journal: Biochim Biophys Acta
pages: 1-20
published year: 2001
volume: 1546
references: http://www.ncbi.nlm.nih.gov/pubmed/11257505

An investigation of the action of porcine pancreatic alpha-amylase on native and gelatinised starches.
type: BibliographicResource
authors:
  item: Slaughter SL
  item: Ellis PR
  item: Butterworth PJ
journal: Biochim Biophys Acta
pages: 29-36
published year: 2001
volume: 1525
references: http://www.ncbi.nlm.nih.gov/pubmed/11342250

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00165#72
type: BibliographicResource
title: Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs.
authors:
  item: Ohtaki A
  item: Kondo S
  item: Shimura Y
  item: Tonozuka T
  item: Sakano Y
  item: Kamitori S
journal: Carbohydr Res
pages: 309-13
published year: 2001
volume: 334
references: http://www.ncbi.nlm.nih.gov/pubmed/11527532

Amylolytic enzymes: molecular aspects of their properties.
type: BibliographicResource
authors:
  item: Horvathova V
  item: Janecek S
  item: Sturdik E
journal: Gen Physiol Biophys
pages: 7-32
published year: 2001
volume: 20
references: http://www.ncbi.nlm.nih.gov/pubmed/11508823

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00165#74
type: BibliographicResource
title: Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structure of the mutant E354A complexed with beta-cyclodextrin, and kinetic analyses on cyclodextrins.
authors:
  item: Kondo S
  item: Ohtaki A
  item: Tonozuka T
  item: Sakano Y
  item: Kamitori S
journal: J Biochem (Tokyo)
pages: 423-8
published year: 2001
volume: 129
references: http://www.ncbi.nlm.nih.gov/pubmed/11226882

The determinants of alpha-amylase pH-activity profiles.
type: BibliographicResource
authors:
  item: Nielsen JE
  item: Borchert TV
  item: Vriend G
journal: Protein Eng
pages: 505-12
published year: 2001
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/11522925

Deletion analysis of the C-terminal region of the alpha-amylase of Bacillus sp. strain TS-23.
type: BibliographicResource
authors:
  item: Lo HF
  item: Lin LL
  item: Chiang WY
  item: Chie MC
  item: Hsu WH
  item: Chang CT
journal: Arch Microbiol
pages: 115-23
published year: 2002
volume: 178
references: http://www.ncbi.nlm.nih.gov/pubmed/12115056

Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase.
type: BibliographicResource
authors:
  item: Aghajari N
  item: Roth M
  item: Haser R
journal: Biochemistry
pages: 4273-80
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/11914073

Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids.
type: BibliographicResource
authors:
  item: Rydberg EH
  item: Li C
  item: Maurus R
  item: Overall CM
  item: Brayer GD
  item: Withers SG
journal: Biochemistry
pages: 4492-502
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/11914097

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00165#79
type: BibliographicResource
title: Barley alpha-amylase Met53 situated at the high-affinity subsite -2 belongs to a substrate binding motif in the beta-->alpha loop 2 of the catalytic (beta/alpha)8-barrel and is critical for activity and substrate specificity.
authors:
  item: Mori H
  item: Bak-Jensen KS
  item: Svensson B
journal: Eur J Biochem
pages: 5377-90
published year: 2002
volume: 269
references: http://www.ncbi.nlm.nih.gov/pubmed/12423336

Alpha-amylase structure and activity.
type: BibliographicResource
authors:
  item: MacGregor EA
journal: J Protein Chem
pages: 399-415
published year: 1988
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/3267138

Functional mimicry between anti-Tendamistat antibodies and alpha-amylase.
type: BibliographicResource
authors:
  item: Goncalves O
  item: Dintinger T
  item: Blanchard D
  item: Tellier C
journal: J Immunol Methods
pages: 29-37
published year: 2002
volume: 269
references: http://www.ncbi.nlm.nih.gov/pubmed/12379350

Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution.
type: BibliographicResource
authors:
  item: Kamitori S
  item: Abe A
  item: Ohtaki A
  item: Kaji A
  item: Tonozuka T
  item: Sakano Y
journal: J Mol Biol
pages: 443-53
published year: 2002
volume: 318
references: http://www.ncbi.nlm.nih.gov/pubmed/12051850

Kinetics and energetics of the binding between barley alpha-amylase/subtilisin inhibitor and barley alpha-amylase 2 analyzed by surface plasmon resonance and isothermal titration calorimetry.
type: BibliographicResource
authors:
  item: Nielsen PK
  item: Bonsager BC
  item: Berland CR
  item: Sigurskjold BW
  item: Svensson B
journal: Biochemistry
pages: 1478-87
published year: 2003
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/12578360

Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain.
type: BibliographicResource
authors:
  item: Janecek S
  item: Svensson B
  item: MacGregor EA
journal: Eur J Biochem
pages: 635-45
published year: 2003
volume: 270
references: http://www.ncbi.nlm.nih.gov/pubmed/12581203

Detection of a covalent intermediate in the mechanism of action of porcine pancreatic alpha-amylase by using 13C nuclear magnetic resonance.
type: BibliographicResource
authors:
  item: Tao BY
  item: Reilly PJ
  item: Robyt JF
journal: Biochim Biophys Acta
pages: 214-20
published year: 1989
volume: 995
references: http://www.ncbi.nlm.nih.gov/pubmed/2784982

1aqhA01
type: Pdb
catalytic residue: ASP 174;GLU 200;ASP 264
cofactor binding residue: ASN 88;GLN 135;ASP 144;HIS 178(Calcium binding);ARG 172;ASN 262;LYS 300(Chloride binding)
references: 1aqh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqh

1aqmA01
type: Pdb
catalytic residue: ASP 174;GLU 200;ASP 264
cofactor binding residue: ASN 88;GLN 135;ASP 144;HIS 178(Calcium binding);ARG 172;ASN 262;LYS 300(Chloride binding)
references: 1aqm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqm

1b0iA01
type: Pdb
catalytic residue: ASP 174;GLU 200;ASP 264
cofactor binding residue: ASN 88;GLN 135;ASP 144;HIS 178(Calcium binding);ARG 172;ASN 262;LYS 300(Chloride binding)
references: 1b0i
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b0i

1bagA01
type: Pdb
catalytic residue: ASP 176; ;ASP 269
cofactor binding residue: ASN 101;THR 137;ASP 146;HIS 180(Calcium binding);GLY 169;ASP 171(2nd calcium)
references: 1bag
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bag
comment: mutant E208Q

1bsiA01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
references: 1bsi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bsi

1bvnP01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
references: 1bvn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvn

1clvA01
type: Pdb
catalytic residue: ASP 185;GLU 222;ASP 287
cofactor binding residue: ASN 98;ARG 146;ASP 155;HIS 189(Calcium binding);ARG 183;ASN 285;ARG 321(Chloride binding)
references: 1clv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1clv

1cpuA01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
references: 1cpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cpu

1dhkA01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
references: 1dhk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dhk

1hnyA01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
references: 1hny
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hny

1jaeA01
type: Pdb
catalytic residue: ASP 185;GLU 222;ASP 287
cofactor binding residue: ASN 98;ARG 146;ASP 155;HIS 189(Calcium binding);ARG 183;ASN 285;ARG 321(Chloride binding)
references: 1jae
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jae

1jfhA01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
references: 1jfh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jfh

1oseA01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
references: 1ose
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ose

1pifA01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
references: 1pif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pif

1pigA01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
references: 1pig
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pig

1ppiA01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
references: 1ppi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ppi

1smdA01
type: Pdb
catalytic residue: ASP 197;GLU 233;ASP 300
cofactor binding residue: ASN 100;ARG 158;ASP 167;HIS 201(Calcium binding);ARG 195;ASN 298;ARG 337(Chloride binding)
modified residue: ASN 350(Deamidation)
references: 1smd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1smd

1tmqA01
type: Pdb
catalytic residue: ASP 185;GLU 222;ASP 287
cofactor binding residue: ASN 98;ARG 146;ASP 155;HIS 189(Calcium binding);ARG 183;ASN 285;ARG 321(Chloride binding)
references: 1tmq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tmq

1viwA01
type: Pdb
catalytic residue: ASP 185;GLU 222;ASP 287
cofactor binding residue: ASN 98;ARG 146;ASP 155;HIS 189(Calcium binding);ARG 183;ASN 285;ARG 321(Chloride binding)
references: 1viw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1viw

1amyA01
type: Pdb
catalytic residue: ASP 179;GLU 204;ASP 289
cofactor binding residue: ASN 91;PHE 143;ASP 148;ASP 142(Calcium binding);GLU 108;THR 111;ASP 113;ASP 117(2nd calcium);ASP 127;ASP 138;ALA 141;ALA 146(3rd calcium)
references: 1amy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1amy

1avaA01
type: Pdb
catalytic residue: ASP 179;GLU 204;ASP 289
cofactor binding residue: ASN 91;PHE 143;ASP 148;ASP 142(Calcium binding);GLU 108;THR 111;ASP 113;ASP 117(2nd calcium);ASP 127;ASP 138;ALA 141;ALA 146(3rd calcium)
references: 1ava
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ava

1avaB01
type: Pdb
catalytic residue: ASP 179;GLU 204;ASP 289
cofactor binding residue: ASN 91;PHE 143;ASP 148;ASP 142(Calcium binding);GLU 108;THR 111;ASP 113;ASP 117(2nd calcium);ASP 127;ASP 138;ALA 141;ALA 146(3rd calcium)
references: 1ava
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ava

1bg9A01
type: Pdb
catalytic residue: ASP 179;GLU 204;ASP 289
cofactor binding residue: ASN 91;ASP 142;PHE 143;ASP 148(Calcium binding);GLU 108;THR 111;ASP 113;ASP 117(2nd calcium);ASP 127;ASP 138;ALA 141;ALA 146(3rd calcium)
references: 1bg9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bg9

2aaaA01
type: Pdb
catalytic residue: ASP 206;GLU 230;ASP 297
cofactor binding residue: ASP 121;GLU 162;ASP 175;GLU 210(Calcium binding);ASP 206;GLU 230(Inhibitory calcium binding)
references: 2aaa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2aaa

2taaA01
type: Pdb
catalytic residue: ASP 206;GLU 230;ASP 297
cofactor binding residue: ASN 121;GLU 162;ASP 175;HIS 210(Calcium binding);ASP 206;GLU 230(Inhibitory calcium binding)
references: 2taa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2taa

6taaA01
type: Pdb
catalytic residue: ASP 206;GLU 230;ASP 297
cofactor binding residue: ASN 121;GLU 162;ASP 175;HIS 210(Calcium binding);ASP 206;GLU 230(Inhibitory calcium binding)
references: 6taa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6taa

7taaA01
type: Pdb
catalytic residue: ASP 206;GLU 230;ASP 297
cofactor binding residue: ASN 121;GLU 162;ASP 175;HIS 210(Calcium binding);ASP 206;GLU 230(Inhibitory calcium binding)
references: 7taa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7taa

1smdA02
type: Pdb
modified residue: ASN 412;ASN 459(Deamidation)
references: 1smd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1smd

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

Chloride
type: KeggCofactor
compound type: halide
references: KEGG:C00115

Dextrin
type: KeggProduct
compound type: polysaccharide
references: KEGG:C00721

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

glycogenase
type: KeggEnzyme

alpha amylase, alpha-amylase
type: KeggEnzyme

endoamylase
type: KeggEnzyme

Taka-amylase A
type: KeggEnzyme

1,4-alpha-D-glucan glucanohydrolase
type: KeggEnzyme

Analogue
compound: Starch
ligand het code: MA2-MA3
pdb: 1jfhA01

Analogue
compound: Dextrin
ligand het code: MAN-MA1
pdb: 1jfhA01

TransitionStateAnalogue
ligand het code: DAF-GLC
pdb: 1bg9A01

TransitionStateAnalogue
ligand het code: ABC
pdb: 7taaA01

TransitionStateAnalogue
ligand het code: AC1-GLC-AC1-GLC
pdb: 1oseA01

TransitionStateAnalogue
ligand het code: AGL-GLC-HMC-AGL-GLC-GLC
pdb: 1pigA01

TransitionStateAnalogue
ligand het code: GLC-GLC-DAF-GLC
pdb: 1ppiA01

TransitionStateAnalogue
ligand het code: GLC-GLC-HMC-AGL-GLC
pdb: 1cpuA01

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.699-700

ReferenceForCatalyticMechanism
reference index: 9
reference section: Fig. 1, Fig. 2, p.215, p.219-220
reference step: 3

ReferenceForCatalyticMechanism
reference index: 18
reference section: Fig. 6, p.207-208
reference step: 3

ReferenceForCatalyticMechanism
reference index: 22
reference section: Fig. 2, p.298-301
reference step: 5

ReferenceForCatalyticMechanism
reference index: 23
reference section: p.6292-6293

ReferenceForCatalyticMechanism
reference index: 27
reference section: p.1580-1582

ReferenceForCatalyticMechanism
reference index: 37
reference section: Scheme 2
reference step: 4

ReferenceForCatalyticMechanism
reference index: 38
reference section: Fig. 2, p.10843-10845
reference step: 4

ReferenceForCatalyticMechanism
reference index: 43
reference section: Fig. 1, p.201-203
reference step: 2

ReferenceForCatalyticMechanism
reference index: 44
reference section: p.403-404

ReferenceForCatalyticMechanism
reference index: 45
reference section: p.211-214

ReferenceForCatalyticMechanism
reference index: 46
reference section: p.620-622

ReferenceForCatalyticMechanism
reference index: 47
reference section: p.565-568

ReferenceForCatalyticMechanism
reference index: 61
reference section: Fig. 2, p.4785-4789
reference step: 10

ReferenceForCatalyticMechanism
reference index: 62
reference section: Fig. 5, p.261-264
reference step: 2

ReferenceForCatalyticMechanism
reference index: 69
reference section: Fig. 2, Fig. 8A, p.7707
reference step: 4

ReferenceForCatalyticMechanism
reference index: 70
reference section: Fig. 2, p.4-5
reference step: 8

ReferenceForCatalyticMechanism
reference index: 77
reference section: Fig. 3, p.4277-4278
reference step: 8

ReferenceForCatalyticMechanism
reference index: 78
reference section: Scheme 1, p.4500-4502
reference step: 10

ReferenceForCatalyticMechanism
reference index: 79
reference section: Fig. 3
reference step: 4