Long-chain-fatty-acyl-glutamate deacylase
Appearance
long-chain-fatty-acyl-glutamate deacylase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.1.55 | ||||||||
CAS no. | 82249-69-2 | ||||||||
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, a long-chain-fatty-acyl-glutamate deacylase (EC 3.5.1.55) is an enzyme that catalyzes the chemical reaction
- N-long-chain-fatty-acyl-L-glutamate + H2O a long-chain carboxylate + L-glutamate
Thus, the two substrates of this enzyme are N-long-chain-fatty-acyl-L-glutamate and H2O, whereas its two products are long-chain carboxylate and L-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-long-chain-fatty-acyl-L-glutamate amidohydrolase. Other names in common use include long-chain aminoacylase, long-chain-fatty-acyl-glutamate deacylase, long-chain acylglutamate amidase, and N-acyl-D-glutamate deacylase.
References
[edit]- Fukuda H, Iwade S, Kimura A (May 1982). "A new enzyme: long acyl aminoacylase from Pseudomonas diminuta". J. Biochem. 91 (5). Tokyo: 1731–8. PMID 7096313.