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Links from Protein

Items: 5

1.

Alpha-amylase C-terminal domain

This is the C-terminal domain of alpha-amylase and related enzymes. This domain follows the catalytic beta/alpha domain. It folds into a beta-sandwich with a greek key topology. Paper describing PDB structure 1bvz. [1]. 10222200. Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution. Kamitori S, Kondo S, Okuyama K, Yokota T, Shimura Y, Tonozuka T, Sakano Y;. J Mol Biol 1999;287:907-921. Paper describing PDB structure 1g1y. [2]. 11226882. 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. Kondo S, Ohtaki A, Tonozuka T, Sakano Y, Kamitori S;. J Biochem. 2001;129:423-428. Paper describing PDB structure 1jf5. [3]. 11527532. 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. Ohtaki A, Kondo S, Shimura Y, Tonozuka T, Sakano Y, Kamitori S;. Carbohydr Res. 2001;334:309-313. Paper describing PDB structure 1jib. [4]. 11330677. Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues. Yokota T, Tonozuka T, Shimura Y, Ichikawa K, Kamitori S, Sakano Y;. Biosci Biotechnol Biochem. 2001;65:619-626. Paper describing PDB structure 1vfm. [5]. 15138257. Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and . TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-10-16
Family Accession:
NF046571.1
Method:
HMM
2.

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)

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Biological Process:
carbohydrate metabolic process (GO:0005975)
Date:
2024-10-16
Family Accession:
NF012356.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.

alpha-amylase family protein

alpha-amylase family protein similar to alpha amylase that catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides

Date:
2022-01-30
Family Accession:
10087997
Method:
Sparcle
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