M00193
type: Enzyme
active site residues resources: Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family.
active site residues resources: Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
active site residues resources: The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.
active site residues resources: Q08751
active site residues resources: P38940
cath: Immunoglobulin-like
cath: TIM Barrel
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/1.-.-.-
csa: 1bvz
ec: https://purl.uniprot.org/enzyme/3.2.1.135
kegg cofactor: Calcium
kegg enzyme: neopullulanase
kegg product: Pullulan
kegg product: Panose
kegg substrate: Pullulan
kegg substrate: H2O
pdb: 1bvzA01
pdb: 1bvzB01
pdb: 1g1yA01
pdb: 1g1yB01
pdb: 1jf5A01
pdb: 1jf5B01
pdb: 1jf6A01
pdb: 1jf6B01
pdb: 1ji2A01
pdb: 1ji2B01
pdb: 1jibA01
pdb: 1jibB01
pdb: 1jl8A01
pdb: 1jl8B01
pdb: 1vb9A01
pdb: 1vb9B01
pdb: 1vfkA01
pdb: 1vfkB01
pdb: 1vfmA01
pdb: 1vfmB01
pdb: 1vfoA01
pdb: 1vfoB01
pdb: 1vfuA01
pdb: 1vfuB01
pdb: 1wzkA01
pdb: 1wzkB01
pdb: 1wzlA01
pdb: 1wzlB01
pdb: 1wzmA01
pdb: 1wzmB01
pdb: 1j0hA01
pdb: 1j0hB01
pdb: 1j0iA01
pdb: 1j0iB01
pdb: 1j0jA01
pdb: 1j0jB01
pdb: 1j0kA01
pdb: 1j0kB01
pdb: 1bvzA02
pdb: 1bvzB02
pdb: 1g1yA02
pdb: 1g1yB02
pdb: 1jf5A02
pdb: 1jf5B02
pdb: 1jf6A02
pdb: 1jf6B02
pdb: 1ji2A02
pdb: 1ji2B02
pdb: 1jibA02
pdb: 1jibB02
pdb: 1jl8A02
pdb: 1jl8B02
pdb: 1vb9A02
pdb: 1vb9B02
pdb: 1vfkA02
pdb: 1vfkB02
pdb: 1vfmA02
pdb: 1vfmB02
pdb: 1vfoA02
pdb: 1vfoB02
pdb: 1vfuA02
pdb: 1vfuB02

Analogue
compound: Pullulan
ligand het code: BCD
pdb: 1g1yA02

Analogue
compound: Pullulan
ligand het code: BCD
pdb: 1g1yB02

Analogue
compound: Pullulan
ligand het code: MTT
pdb: 1jibA02

Analogue
compound: Pullulan
ligand het code: MTT
pdb: 1jibB02

Analogue
compound: Pullulan
ligand het code: BCD
pdb: 1jl8A02

Analogue
compound: Pullulan
ligand het code: BCD
pdb: 1jl8B02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC
pdb: 1vb9A02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC
pdb: 1vb9B02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC
pdb: 1vfmA02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC
pdb: 1vfmB02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC-GLC
pdb: 1vfoA02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC-GLC
pdb: 1vfoB02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC-GLC-GLC
pdb: 1vfuA02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC-GLC-GLC-GLC-GLC
pdb: 1vfuB02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC-GLC
pdb: 1j0jA02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC-GLC
pdb: 1j0jB02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC
pdb: 1j0kA02

Analogue
compound: Pullulan
ligand het code: GLC-GLC-GLC
pdb: 1j0kB02

Analogue
compound: Pullulan
ligand het code: GLC-GLC
pdb: 1vfkA02

Analogue
compound: Pullulan
ligand het code: GLC-GLC
pdb: 1vfkB02

Analogue
compound: Panose
ligand het code: GLC
pdb: 1vfkA02

Analogue
compound: Panose
ligand het code: GLC
pdb: 1vfkB02

ReferenceForCatalyticMechanism
reference index: 5
reference section: p.146-150

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.2, p.170

ReferenceForCatalyticMechanism
reference index: 12
reference section: Fig.2

ReferenceForCatalyticMechanism
reference index: 22
reference section: FIG.5, p.31038

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

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

Action of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at alpha-(1----4)- and alpha-(1----6)-glucosidic linkages.
type: BibliographicResource
authors:
  item: Takata H
  item: Kuriki T
  item: Okada S
  item: Takesada Y
  item: Iizuka M
  item: Minamiura N
  item: Imanaka T
journal: J Biol Chem
pages: 18447-52
published year: 1992
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/1388153

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

Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.
type: BibliographicResource
authors:
  item: Yokota T
  item: Tonozuka T
  item: Shimura Y
  item: Ichikawa K
  item: Kamitori S
  item: Sakano Y
journal: Biosci Biotechnol Biochem
pages: 619-26
published year: 2001
volume: 65
references: http://www.ncbi.nlm.nih.gov/pubmed/11330677
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

http://ezcatdb.cbrc.jp/EzCatDB/reference/M00193#14
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
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

http://ezcatdb.cbrc.jp/EzCatDB/reference/M00193#15
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
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Catalytic activities of intracellular dimeric neopullulanase on cyclodextrin, acarbose and maltose.
type: BibliographicResource
authors:
  item: Cheong KA
  item: Kim TJ
  item: Yoon JW
  item: Park CS
  item: Lee TS
  item: Kim YB
  item: Park KH
  item: Kim JW
journal: Biotechnol Appl Biochem
pages: 27-34
published year: 2002
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/11834127

Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other.
type: BibliographicResource
authors:
  item: Lee HS
  item: Park KH
  item: Kim MS
  item: Cho HS
  item: Kim JI
  item: Kim TJ
  item: Choi JH
  item: Park C
  item: Oh BH
journal: J Biol Chem
pages: 21891-7
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/11923309

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
medline id: 22047855
pages: 443-53
published year: 2002
volume: 318
references: http://www.ncbi.nlm.nih.gov/pubmed/12051850
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q08751
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Mutual conversion of substrate specificities of Thermoactinomyces vulgaris R-47 alpha-amylases TVAI and TVAII by site-directed mutagenesis.
type: BibliographicResource
authors:
  item: Ohtaki A
  item: Iguchi A
  item: Mizuno M
  item: Tonozuka T
  item: Sakano Y
  item: Kamitori S
journal: Carbohydr Res
pages: 1553-8
published year: 2003
volume: 338
references: http://www.ncbi.nlm.nih.gov/pubmed/12860426

Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes.
type: BibliographicResource
authors:
  item: Jespersen HM
  item: MacGregor EA
  item: Henrissat B
  item: Sierks MR
  item: Svensson B
journal: J Protein Chem
pages: 791-805
published year: 1993
volume: 12
references: http://www.ncbi.nlm.nih.gov/pubmed/8136030

Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase.
type: BibliographicResource
authors:
  item: Hondoh H
  item: Kuriki T
  item: Matsuura Y
journal: J Mol Biol
pages: 177-88
published year: 2003
volume: 326
references: http://www.ncbi.nlm.nih.gov/pubmed/12547200
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P38940
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.
type: BibliographicResource
authors:
  item: Ohtaki A
  item: Mizuno M
  item: Tonozuka T
  item: Sakano Y
  item: Kamitori S
journal: J Biol Chem
pages: 31033-40
published year: 2004
volume: 279
references: http://www.ncbi.nlm.nih.gov/pubmed/15138257
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

A convenient enzymatic synthesis of 4(2)-alpha-isomaltosylisomaltose using Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II).
type: BibliographicResource
authors:
  item: Tonozuka T
  item: Sakai H
  item: Ohta T
  item: Sakano Y
journal: Carbohydr Res
pages: 157-62
published year: 1994
volume: 261
references: http://www.ncbi.nlm.nih.gov/pubmed/8087809

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

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

Structural consequences of neopullulanase mutations.
type: BibliographicResource
authors:
  item: Lamminmaki U
  item: Vihinen M
journal: Biochim Biophys Acta
pages: 195-200
published year: 1996
volume: 1295
references: http://www.ncbi.nlm.nih.gov/pubmed/8695646

Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center.
type: BibliographicResource
authors:
  item: Kuriki T
  item: Kaneko H
  item: Yanase M
  item: Takata H
  item: Shimada J
  item: Handa S
  item: Takada T
  item: Umeyama H
  item: Okada S
journal: J Biol Chem
pages: 17321-9
published year: 1996
volume: 271
references: http://www.ncbi.nlm.nih.gov/pubmed/8663322

Introducing transglycosylation activity in a liquefying alpha-amylase.
type: BibliographicResource
authors:
  item: Saab-Rincon G
  item: del-Rio G
  item: Santamaria RI
  item: Lopez-Munguia A
  item: Soberon X
journal: FEBS Lett
pages: 100-6
published year: 1999
volume: 453
references: http://www.ncbi.nlm.nih.gov/pubmed/10403384

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
medline id: 99241045
pages: 907-21
published year: 1999
volume: 287
references: http://www.ncbi.nlm.nih.gov/pubmed/10222200
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q08751
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family.
type: BibliographicResource
authors:
  item: Park KH
  item: Kim TJ
  item: Cheong TK
  item: Kim JW
  item: Oh BH
  item: Svensson B
journal: Biochim Biophys Acta
pages: 165-85
published year: 2000
volume: 1478
references: http://www.ncbi.nlm.nih.gov/pubmed/10825529

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

The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.
type: BibliographicResource
authors:
  item: Mizuno M
  item: Tonozuka T
  item: Uechi A
  item: Ohtaki A
  item: Ichikawa K
  item: Kamitori S
  item: Nishikawa A
  item: Sakano Y
journal: Eur J Biochem
pages: 2530-8
published year: 2004
volume: 271
references: http://www.ncbi.nlm.nih.gov/pubmed/15182368
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

1j0hA02
type: Pdb
catalytic residue: ASP 328;GLU 357;ASP 424
cofactor binding residue: ASN 147;ASN 149; ;SER 153;GLY 172;ASP 174(Calcium binding)
references: 1j0h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j0h

1j0hB02
type: Pdb
catalytic residue: ASP 328;GLU 357;ASP 424
cofactor binding residue: ASN 147;ASN 149; ;SER 153;GLY 172;ASP 174(Calcium binding)
references: 1j0h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j0h

1j0iA02
type: Pdb
catalytic residue: ASP 328;GLU 357;ASP 424
cofactor binding residue: ASN 147;ASN 149; ;SER 153;GLY 172;ASP 174(Calcium binding)
references: 1j0i
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j0i

1j0iB02
type: Pdb
catalytic residue: ASP 328;GLU 357;ASP 424
cofactor binding residue: ASN 147;ASN 149; ;SER 153;GLY 172;ASP 174(Calcium binding)
references: 1j0i
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j0i

1jf5A02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1jf5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jf5
comment: mutant F286A

1jf5B02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1jf5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jf5
comment: mutant F286A

1jf6A02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1jf6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jf6
comment: mutant F286Y

1jf6B02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1jf6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jf6
comment: mutant F286Y

1ji2A02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1ji2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ji2

1ji2B02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1ji2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ji2

1vb9A02
type: Pdb
catalytic residue: ;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1vb9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vb9
comment: mutant D325N

1vb9B02
type: Pdb
catalytic residue: ;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1vb9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vb9
comment: mutant D325N

1vfkA02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1vfk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vfk

1vfkB02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1vfk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vfk

1vfmA02
type: Pdb
catalytic residue: ;GLU 354;
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1vfm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vfm
comment: mutant D325N, D421N

1vfmB02
type: Pdb
catalytic residue: ;GLU 354;
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1vfm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vfm
comment: mutant D325N, D421N

1vfoA02
type: Pdb
catalytic residue: ;GLU 354;
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1vfo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vfo
comment: mutant D325N, D421N

1vfoB02
type: Pdb
catalytic residue: ;GLU 354;
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1vfo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vfo
comment: mutant D325N, D421N

1vfuA02
type: Pdb
catalytic residue: ;GLU 354;
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1vfu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vfu
comment: mutant D325N, D421N

1vfuB02
type: Pdb
catalytic residue: ;GLU 354;
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1vfu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vfu
comment: mutant D325N, D421N

1wzkA02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1wzk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wzk
comment: mutant D465N

1wzkB02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1wzk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wzk
comment: mutant D465N

1wzlA02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1wzl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wzl
comment: mutant R469L

1wzlB02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1wzl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wzl
comment: mutant R469L

1wzmA02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1wzm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wzm
comment: mutant R469K

1wzmB02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1wzm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wzm
comment: mutant R469K

1bvzA02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1bvz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvz

1bvzB02
type: Pdb
catalytic residue: ASP 325;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1bvz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvz

1g1yA02
type: Pdb
catalytic residue: ASP 325; ;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1g1y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g1y
comment: mutant E354A

1g1yB02
type: Pdb
catalytic residue: ASP 325; ;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1g1y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g1y
comment: mutant E354A

1j0jA02
type: Pdb
catalytic residue: ASP 328; ;ASP 424
cofactor binding residue: ASN 147;ASN 149; ;SER 153;GLY 172;ASP 174(Calcium binding)
references: 1j0j
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j0j
comment: mutantE357Q

1j0jB02
type: Pdb
catalytic residue: ASP 328; ;ASP 424
cofactor binding residue: ASN 147;ASN 149; ;SER 153;GLY 172;ASP 174(Calcium binding)
references: 1j0j
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j0j
comment: mutantE357Q

1j0kA02
type: Pdb
catalytic residue: ASP 328; ;ASP 424
cofactor binding residue: ASN 147;ASN 149; ;SER 153;GLY 172;ASP 174(Calcium binding)
references: 1j0k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j0k
comment: mutantE357Q

1j0kB02
type: Pdb
catalytic residue: ASP 328; ;ASP 424
cofactor binding residue: ASN 147;ASN 149; ;SER 153;GLY 172;ASP 174(Calcium binding)
references: 1j0k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j0k
comment: mutantE357Q

1jibA02
type: Pdb
catalytic residue: ;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1jib
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jib
comment: mutant D325N

1jibB02
type: Pdb
catalytic residue: ;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1jib
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jib
comment: mutant D325N

1jl8A02
type: Pdb
catalytic residue: ;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1jl8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jl8
comment: mutant D325N

1jl8B02
type: Pdb
catalytic residue: ;GLU 354;ASP 421
cofactor binding residue: ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
references: 1jl8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jl8
comment: mutant D325N

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

Panose
type: KeggProduct
compound type: polysaccharide
references: KEGG:C00713
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pullulan
type: KeggSubstrate
type: KeggProduct
compound type: polysaccharide
references: KEGG:C00480

pullulanase II
type: KeggEnzyme