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Α-Glucosidase

class of enzymes

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Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionJul 14, 2026
Entity authorityQ2839456
Source-derived summary

α-Glucosidase (EC 3.2.1.20, (systematic name α-D-glucoside glucohydrolase) is a glucosidase located in the brush border of the small intestine that acts upon α(1→4) bonds:

Hydrolysis of terminal, non-reducing (1→4)-linked α-D-glucose residues with release of D-glucose

This is in contrast to EC 3.2.1.21 β-glucosidase.

Terminology

GO:0090599, the broad sense

The Gene Ontology entry GO:0090599 represents the broad sense of "alpha-glucosidase". It is defined as "catalysis of the hydrolysis of terminal, non-reducing alpha-linked alpha-D-glucose residue with release of alpha-D-glucose." In this sense, "alpha-glucosidase" can encompass a wide range of enzyme activities, differing by the linkage of their terminal (1→3, 1→4, or 1→6), the specific identity of their substrate (sucrose, maltose, or starch), among other aspects.

EC 3.2.1.20, the narrow sense

The definition associated with Enzyme Commission number 3.2.1.20 is narrower. It requires the linkage to be 1→4, and the preferred substrate to be smaller oligosaccharides (as opposed to larger polysaccharides like starch: alpha-amylase would otherwise be included). Human genes that produce enzymes with activities specified by this EC number include:

MGAM is the "maltase-glucoamylase", found on the intestine brush border.

GAA is the "acid alpha-glucosidase", found in the lysosome.

GANC, "neutral alpha-glucosidase C".

Synonyms mentioned by the Commission include maltase, glucoinvertase, glucosidosucrase, maltase-glucoamylase, α-glucopyranosidase, glucosidoinvertase, α-D-glucosidase, α-glucoside hydrolase, α-1,4-glucosidase, α-D-glucoside glucohydrolase. These names are not recommended because they may only refer to a specific activity of the enzyme, or a specific protein having this acvitity.

Editorial summary

Begin with the source’s own compact description: “Α-Glucosidase” is class of enzymes. The dossier treats that line as a proposition to test through Α-Glucosidase, class and enzymes, not as a finished interpretation.

Editorial reviewA dependable orientation record for establishing vocabulary, names and a first evidence trail. The current 233-word lead offers orientation but no explicit four-digit date, so chronology should not be assumed. The selected authority fields contribute no independent date. For this dossier, Α-Glucosidase, class and enzymes is the immediate research focus.
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Source & attribution

This entry incorporates text from Α-Glucosidase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.