Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].

E.coli Aec37-like. Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family represented by Escherichia coli protein Aec37. The gene encoding Aec37 (aec-37) is located within a genomic island (AGI-3) isolated from the extraintestinal avian pathogenic Escherichia coli strain BEN2908. The function of Aec37 and its orthologs is unknown; however, deletion of a region of the genome that includes aec-37 affects the assimilation of seven carbohydrates, decreases growth rate of the strain in minimal medium containing galacturonate or trehalose, and attenuates the virulence of E. coli BEN2908 in chickens. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.

Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.

neutral alpha-glucosidase C, neutral alpha-glucosidase AB. This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.

glycosyl hydrolase family 31 (GH31). GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

Murineendoplasmic reticulum alpha-glucosidase II [Mus musculus],5H9O_A Complex of Murine endoplasmic reticulum alpha-glucosidase II with D-Glucose [Mus musculus],5H9O_C Complex of Murine endoplasmic reticulum alpha-glucosidase II with D-Glucose [Mus musculus],5HJO_A Murine endoplasmic reticulum alpha-glucosidase II with bound substrate analogue [Mus musculus],5HJO_C Murine endoplasmic reticulum alpha-glucosidase II with bound substrate analogue [Mus musculus],5HJR_A Murine endoplasmic reticulum alpha-glucosidase II with bound covalent intermediate [Mus musculus],5HJR_C Murine endoplasmic reticulum alpha-glucosidase II with bound covalent intermediate [Mus musculus]

Murineendoplasmic reticulum alpha-glucosidase II with N-butyl-1-deoxynojirimycin [Mus musculus]

Murineendoplasmic reticulum alpha-glucosidase II with N-9'-methoxynonyl-1-deoxynojirimycin [Mus musculus]

Murineendoplasmic reticulum alpha-glucosidase II with castanospermine [Mus musculus],5IEE_A Murine endoplasmic reticulum alpha-glucosidase II with 1-deoxynojirimycin [Mus musculus]

ChainA, Neutral alpha-glucosidase AB [Mus musculus],7KRY_C Chain C, Neutral alpha-glucosidase AB [Mus musculus]

Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1

Neutral alpha-glucosidase AB OS=Sus scrofa OX=9823 GN=GANAB PE=1 SV=1

Neutral alpha-glucosidase AB OS=Homo sapiens OX=9606 GN=GANAB PE=1 SV=3

Neutral alpha-glucosidase AB OS=Mus musculus OX=10090 GN=Ganab PE=1 SV=1

Neutral alpha-glucosidase AB OS=Macaca fascicularis OX=9541 GN=GANAB PE=2 SV=1