Glucosylceramidase

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O-Glycosyl hydrolase family 30
Identifiers
Symbol	Glyco_hydro_30
Pfam	PF02055
InterPro	IPR001139
SCOP	1nof
OPM protein	1ogs
Available PDB structures: 1y7vA:40-533 1ogsA:40-533 1nofA:31-383

In enzymology, a glucosylceramidase (EC 3.2.1.45) is an enzyme that catalyzes the chemical reaction

D-glucosyl-N-acylsphingosine + H₂O $\rightleftharpoons$ D-glucose + N-acylsphingosine

Thus, the two substrates of this enzyme are D-glucosyl-N-acylsphingosine and H₂O, whereas its two products are D-glucose and N-acylsphingosine.

This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is D-glucosyl-N-acylsphingosine glucohydrolase. Other names in common use include psychosine hydrolase, glucosphingosine glucosylhydrolase, GlcCer-beta-glucosidase, beta-D-glucocerebrosidase, glucosylcerebrosidase, beta-glucosylceramidase, ceramide glucosidase, glucocerebrosidase, glucosylsphingosine beta-glucosidase, and glucosylsphingosine beta-D-glucosidase. This enzyme participates in sphingolipid metabolism and glycan structures - degradation.

1 Structural studies
2 Human proteins containing this domain
3 References
4 External links
- 4.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1OGS, 1Y7V, 2F61, 2J25, 2NSX, 2NT0, 2NT1, 2V3D, and 2V3E.

[edit] Human proteins containing this domain

GBA;

[edit] References

IUBMB entry for 3.2.1.45
BRENDA references for 3.2.1.45 (Recommended.)
PubMed references for 3.2.1.45
PubMed Central references for 3.2.1.45
Google Scholar references for 3.2.1.45
Brady RO, Kanfer JN and Shapiro D (1966). "The metabolism of glucocerebrosides. I. Preparation and properties of a glucocerebroside-cleaving enzyme from spleen tissue". J. Biol. Chem. 240: 39–43.
Vaccaro AM, Muscillo M, Suzuki K (1985). "Characterization of human glucosylsphingosine glucosyl hydrolase and comparison with glucosylceramidase". Eur. J. Biochem. 146: 315–21. PMID 3967661.