Biology:N-formylglutamate deformylase
| N-formylglutamate deformylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.68 | ||||||||
| CAS number | 97286-12-9 | ||||||||
| 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 N-formylglutamate deformylase (EC 3.5.1.68) is an enzyme that catalyzes the chemical reaction
- N-formyl-L-glutamate + H2O formate + L-glutamate
Thus, the two substrates of this enzyme are N-formyl-L-glutamate and H2O, whereas its two products are formate 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-formyl-L-glutamate amidohydrolase. Other names in common use include beta-citryl-L-glutamate hydrolase, formylglutamate deformylase, N-formylglutamate hydrolase, beta-citrylglutamate amidase, beta-citryl-L-glutamate amidohydrolase, beta-citryl-L-glutamate amidase, beta-citrylglutamate amidase, and beta-citryl-L-glutamate-hydrolyzing enzyme. This enzyme participates in histidine metabolism and glyoxylate and dicarboxylate metabolism.
References
- "Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida". J. Bacteriol. 169 (10): 4696–702. 1987. PMID 3308850.
- "A beta-citryl-L-glutamate-hydrolysing enzyme in rat testes". Biochim. Biophys. Acta 760 (2): 206–14. 1983. doi:10.1016/0304-4165(83)90165-4. PMID 6414521.
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