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alpha-amylase domain-containing protein
This entry represents a C-terminal domain associated with prokaryotic alpha-amylases, which adopt a secondary structure consisting of an eight-stranded antiparallel beta-sheet containing a Greek key motif. Their exact function has not, as yet, been determined [1]. [1]. 12482867. Differential regulation of a hyperthermophilic alpha-amylase. with a novel (Ca,Zn) two-metal center by zinc.. Linden A, Mayans O, Meyer-Klaucke W, Antranikian G, Wilmanns M;. J Biol Chem. 2003;278:9875-9884. (from Pfam)
alpha-amylase family glycosyl hydrolase
Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain. [1]. 8107092. Refined molecular structure of pig pancreatic alpha-amylase at. 2.1 A resolution.. Larson SB, Greenwood A, Cascio D, Day J, McPherson A;. J Mol Biol 1994;235:1560-1584.. [2]. 9600843. Crystal structure of yellow meal worm alpha-amylase at 1.64 A. resolution.. Strobl S, Maskos K, Betz M, Wiegand G, Huber R, Gomis-Ruth FX,. Glockshuber R;. J Mol Biol 1998;278:617-628. (from Pfam)
alpha-amylase
bacterial and fungal alpha amylase catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides.
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