Glucosylceramidase
In enzymology, a glucosylceramidase (EC 3.2.1.45) is an enzyme that catalyzes the chemical reaction
- D-glucosyl-N-acylsphingosine + H2O D-glucose + N-acylsphingosine
| glucosylceramidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Glucosylceramidase tetramer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 3.2.1.45 | ||||||||
| CAS number | 37228-64-1 | ||||||||
| 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 | ||||||||
| |||||||||
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 degradation of glycan structures.
Human proteins containing this domain
- GBA belongs to Glycoside hydrolase family 30, GBA2 belongs to Glycoside hydrolase family 116.
References
Further reading
- Brady RO, Kanfer J, Shapiro D (1965). "The metabolism of glucocerebrosides: I. Purification and properties of a glucocerebroside-cleaving enzyme from spleen tissue". J. Biol. Chem. 240: 39–43. PMID 14253443.
- Vaccaro AM, Muscillo M, Suzuki K (1985). "Characterization of human glucosylsphingosine glucosyl hydrolase and comparison with glucosylceramidase". Eur. J. Biochem. 146 (2): 315–21. doi:10.1111/j.1432-1033.1985.tb08655.x. PMID 3967661.
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