Glycoside hydrolase family 13
Alpha amylase, N-terminal ig-like domain |
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crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase 1 (tvai) mutant d356n/e396q complexed with p2, a pullulan model oligosaccharide |
Identifiers |
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Symbol |
Alpha-amylase_N |
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Pfam |
PF02903 |
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InterPro |
IPR004185 |
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SCOP |
1sma |
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SUPERFAMILY |
1sma |
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In molecular biology, glycoside hydrolase family 13 is a family of glycoside hydrolases.
Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[5]
Enzymes containing this domain belong to family 13 (CAZY GH_13) of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme which catalyses hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains in the conversion of starch to maltose. Other enzymes in this family include neopullulanase, which hydrolyses pullulan to panose, and cyclomaltodextrinase, which hydrolyses cyclodextrins.
References
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