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InterPro: IPR006425 Glucan 1,4-alpha-glucosidase

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UniProtKB
Matches:
32 proteins
AccessionHelp IPR006425 Glucan_glucosid
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR011613 Glycoside hydrolase 15-related
IPR014718 Glycoside hydrolase-type carbohydrate-binding, subgroup
IPR015220 Glucodextranase N
InterPro annotation
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AbstractHelp

Glucan 1,4-alpha-glucosidase catalyzes the hydrolysis of terminal 1,4-linked alpha-D-glucose residues from non-reducing ends of polysaccharides, releasing a beta-D-glucose monomer. Some forms of this enzyme can hydrolyze terminal 1,6- and 1,3-alpha-D-glucosidic bonds in polysaccharides as well [1].

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Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006425 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P29761 Glucoamylase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR012341 Six-hairpin glycosidase
IPR006425 Glucan 1,4-alpha-glucosidase
IPR008928 Six-hairpin glycosidase-like
IPR015220 Glucodextranase N
IPR014718 Glycoside hydrolase-type carbohydrate-binding, subgroup
IPR011613 Glycoside hydrolase 15-related
IPR000165 Glycoside hydrolase, family 15
IPR011013 Glycoside hydrolase-type carbohydrate-binding
SWISS-MODEL
ModBase

PublicationsHelp
1. Ohnishi H, Kitamura H, Minowa T, Sakai H, Ohta T.
Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme.
Eur. J. Biochem. 207 413-8 1992 [PubMed: 1633799]
http://dx.doi.org/10.1111/j.1432-1033.1992.tb17064.x

Additional ReadingHelp
Mizuno M, Tonozuka T, Suzuki S, Uotsu-Tomita R, Kamitori S, Nishikawa A, Sakano Y.
Structural insights into substrate specificity and function of glucodextranase.
J. Biol. Chem. 279 2004 10575-83 [PubMed: 14660574]
http://dx.doi.org/10.1074/jbc.M310771200
Aleshin AE, Feng PH, Honzatko RB, Reilly PJ.
Crystal structure and evolution of a prokaryotic glucoamylase.
J. Mol. Biol. 327 2003 61-73 [PubMed: 12614608]
http://dx.doi.org/10.1016/S0022-2836(03)00084-6
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InterPro 23.1