EzCatDB: T00062

DB codeT00062
RLCP classification1.30.36000.3
CATH domainDomain 13.20.20.80Catalytic domain
Domain 23.90.400.10
Domain 32.60.40.1180
E.C.3.2.1.10
CSA1uok
MACiEM0285

CATH domainRelated DB codes (homologues)
2.60.40.1180M00113,T00307,D00165,D00176,D00664,D00665,D00863,D00864,M00112,M00193,M00314,T00057,T00067
3.20.20.80S00202,S00210,S00748,S00906,S00907,S00911,S00912,S00915,M00134,M00160,D00479,S00204,S00205,S00206,S00207,S00203,S00208,S00209,S00211,S00213,S00214,M00113,T00307,D00165,D00166,D00169,D00176,D00501,D00502,D00503,D00844,D00861,D00864,M00026,M00112,M00193,M00346,T00057,T00063,T00066,T00067

Enzyme Name
Swiss-protKEGG

P21332
Protein nameOligo-1,6-glucosidaseoligo-1,6-glucosidase
limit dextrinase (erroneous)
isomaltase
sucrase-isomaltase
exo-oligo-1,6-glucosidase
dextrin 6alpha-glucanohydrolase
alpha-limit dextrinase
dextrin 6-glucanohydrolase
oligosaccharide alpha-1,6-glucohydrolase
SynonymsEC 3.2.1.10
Oligosaccharide alpha-1,6-glucosidase
Sucrase-isomaltase
Isomaltase
Dextrin 6-alpha-D-glucanohydrolase

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

Swiss-prot:Accession NumberP21332
Entry nameO16G_BACCE
ActivityHydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Subunit
Subcellular locationCytoplasm.
Cofactor


SubstratesProducts
KEGG-idC00252C00001C00031
CompoundIsomaltoseH2OD-Glucose
TypepolysaccharideH2Ocarbohydrate
1uokA01Unbound
Unbound
1uokA02Unbound
Unbound
1uokA03Unbound
Unbound

Active-site residues
resource
Swiss-prot;P21332 & literature [4], [9]
pdbCatalytic residues
1uokA01ASP 199;GLU 255;ASP 329
1uokA02
1uokA03

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.678-679
[7]p.145-146
[8]Fig. 2, p.4

references
[1]
PubMed ID1915879
JournalFEBS Lett
Year1991
Volume290
Pages221-3
AuthorsWatanabe K, Kitamura K, Hata Y, Katsube Y, Suzuki Y
TitleOverproduction, purification and crystallization of Bacillus cereus oligo-1,6-glucosidase.
[2]
PubMed ID1761534
JournalJ Biol Chem
Year1991
Volume266
Pages24287-94
AuthorsWatanabe K, Chishiro K, Kitamura K, Suzuki Y
TitleProline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006.
[3]
PubMed ID1555585
JournalEur J Biochem
Year1992
Volume205
Pages249-56
AuthorsSuzuki Y, Yonezawa K, Hattori M, Takii Y
TitleAssignment of Bacillus thermoamyloliquefaciens KP1071 alpha-glucosidase I to an exo-alpha-1,4-glucosidase, and its striking similarity to bacillary oligo-1,6-glucosidases in N-terminal sequence and in structural parameters calculated from the amino acid composition.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID93380886
PubMed ID8370659
JournalJ Biochem (Tokyo)
Year1993
Volume113
Pages646-9
AuthorsKizaki H, Hata Y, Watanabe K, Katsube Y, Suzuki Y
TitlePolypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis.
Related Swiss-protP21332
[5]
PubMed ID8001545
JournalEur J Biochem
Year1994
Volume226
Pages277-83
AuthorsWatanabe K, Masuda T, Ohashi H, Mihara H, Suzuki Y
TitleMultiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule.
[6]
PubMed ID8787404
JournalAppl Environ Microbiol
Year1996
Volume62
Pages2066-73
AuthorsWatanabe K, Kitamura K, Suzuki Y
TitleAnalysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID97336211
PubMed ID9193006
JournalJ Mol Biol
Year1997
Volume269
Pages142-53
AuthorsWatanabe K, Hata Y, Kizaki H, Katsube Y, Suzuki Y
TitleThe refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization.
Related PDB1uok
Related Swiss-protP21332
[8]
PubMed ID11257505
JournalBiochim Biophys Acta
Year2001
Volume1546
Pages1-20
AuthorsMacGregor EA, Janecek S, Svensson B
TitleRelationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
[9]
PubMed ID11676021
JournalBiosci Biotechnol Biochem
Year2001
Volume65
Pages2058-64
AuthorsWatanabe K, Miyake K, Suzuki Y
TitleIdentification of catalytic and substrate-binding site residues in Bacillus cereus ATCC7064 oligo-1,6-glucosidase.

comments
This enzyme belongs to glycosyl hydrolase family-13.
This enzyme must adopt a similar mechanism to that of alpha-amylase (D00165 in the EzCatDB).

createdupdated
2005-04-142009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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