Alpha-glucosidase | |||||||||
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Alpha-glucosidase hexamer, Sulfolobus solfataricus
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Identifiers | |||||||||
EC number | 3.2.1.20 | ||||||||
CAS number | 9001-42-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Search | |
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PMC | articles |
PubMed | articles |
NCBI | proteins |
Alpha-glucosidase (EC 3.2.1.20, maltase, glucoinvertase, glucosidosucrase, maltase-glucoamylase, alpha-glucopyranosidase, glucosidoinvertase, alpha-D-glucosidase, alpha-glucoside hydrolase, alpha-1,4-glucosidase, alpha-D-glucoside glucohydrolase) is a glucosidase located in the brush border of the small intestine that acts upon α(1→4) bonds. This is in contrast to beta-glucosidase. Alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent.
Other glucosidases include:
Alpha-glucosidase hydrolyzes terminal non-reducing (1→4)-linked alpha-glucose residues to release a single alpha-glucose molecule. Alpha-glucosidase is a carbohydrate-hydrolase that releases alpha-glucose as opposed to beta-glucose. Beta-glucose residues can be released by glucoamylase, a functionally similar enzyme. The substrate selectivity of alpha-glucosidase is due to subsite affinities of the enzyme’s active site. Two proposed mechanisms include a nucleophilic displacement and an oxocarbenium ion intermediate.
Alpha-glucosidases can potentially be split, according to primary structure, into two families. The gene coding for human lysosomal alpha-glucosidase is about 20 kb long and its structure has been cloned and confirmed.