Methylumbelliferyl-acetate deacetylase
| methylumbelliferyl-acetate deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.1.56 | ||||||||
| CAS number | 83380-83-0 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a methylumbelliferyl-acetate deacetylase (EC 3.1.1.56, esterase D) is an enzyme that catalyzes the chemical reaction
- 4-methylumbelliferyl acetate + H2O 4-methylumbelliferone + acetate
Thus, the two substrates of this enzyme are 4-methylumbelliferyl acetate and H2O, whereas its two products are 4-methylumbelliferone and acetate.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 4-methylumbelliferyl-acetate acylhydrolase. This enzyme is also called esterase D.
References
- Hopkinson DA, Mestriner MA, Cortner J, Harris H (1973). "Esterase D: a new human polymorphism". Ann. Hum. Genet. 37 (2): 119–37. doi:10.1111/j.1469-1809.1973.tb01820.x. PMID 4768551.
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