EC 3.2.1.20 - α-glucosidase

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IntEnz Enzyme Nomenclature
EC 3.2.1.20

Names

Accepted name:
α-glucosidase
Other names:
α-1,4-glucosidase
α-D-glucosidase
α-glucopyranosidase
α-glucoside hydrolase
glucoinvertase
glucosidoinvertase
glucosidosucrase
maltase
maltase-glucoamylase
lysosomal α-glucosidase
acid maltase
Systematic name:
α-D-glucoside glucohydrolase

Reaction

Comments:

This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of 1,4-α-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-α-glucosidase and, more slowly, hydrolyses 1,6-α-D-glucose links.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00120 , PROSITE:PDOC01027
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004558 , GO:0090599 , GO:0032450
CAS Registry Number: 9001-42-7
UniProtKB/Swiss-Prot: (50) [show] [UniProt]

References

  1. Bruni, C.B., Sica, V., Auricchio, F. and Covelli, I.
    Further kinetic and structural characterization of the lysosomal α-D-glucoside glucohydrolase from cattle liver.
    Biochim. Biophys. Acta 212: 470-477 (1970). [PMID: 5466143]
  2. Flanagan, P.R. and Forstner, G.G.
    Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH.
    Biochem. J. 173: 553-563 (1978). [PMID: 29602]
  3. Larner, J.
    Other glucosidases.
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes, 2nd ed. vol. 4, Academic Press, New York, 1960, 369-378
  4. Sivikami, S. and Radhakrishnan, A.N.
    Purification of rabbit intestinal glucoamylase by affinity chromatography on Sephadex G-200.
    Indian J. Biochem. Biophys. 10: 283-284 (1973). [PMID: 4792946]
  5. Sørensen, S.H., Norén, O., Sjöström, H. and Danielsen, E.M.
    Amphiphilic pig intestinal microvillus maltase/glucoamylase. Structure and specificity.
    Eur. J. Biochem. 126: 559-568 (1982). [PMID: 6814909]

[EC 3.2.1.20 created 1961]