For beta-glucuronidase, see Beta-glucuronidase
alpha-glucuronidase | |||||||||
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Identifiers | |||||||||
EC no. | 3.2.1.139 | ||||||||
CAS no. | 37259-81-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, an alpha-glucuronidase (EC 3.2.1.139) is an enzyme that catalyzes the chemical reaction
- an alpha-D-glucuronoside + H2O an alcohol + D-glucuronate
Thus, the two substrates of this enzyme are alpha-D-glucuronoside and H2O, whereas its two products are alcohol and D-glucuronate.
This enzyme belongs to the family of hydrolases, to be specific those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha-D-glucosiduronate glucuronohydrolase. This enzyme is also called alpha-glucosiduronase.
Structural studies
editAs of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes 1GQI, 1GQJ, 1GQK, 1GQL, 1H41, 1K9D, 1K9E, 1K9F, 1L8N, 1MQP, 1MQQ, 1MQR, and 1VJT.
See also
editReferences
edit- Visser, J., Kusters van Someren, M.A., Beldman, G. and Voragen, A.G.J. (Eds.), Xylans and Xylanases, Elsevier, Amsterdam, 1992, p. 213-224.
- Uchida H, Nanri T, Kawabata Y, Kusakabe I, Murakami K (1992). "Purification and characterization of intracellular alpha-glucuronidase from Aspergillus niger". Biosci. Biotechnol. Biochem. 56 (10): 1608–1615. doi:10.1271/bbb.56.1608.