| succinyl-diaminopimelate desuccinylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.18 | ||||||||
| CAS no. | 9024-94-6 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a succinyl-diaminopimelate desuccinylase (EC 3.5.1.18) is an enzyme that catalyzes the chemical reaction
- N-succinyl-LL-2,6-diaminoheptanedioate + H2O succinate + LL-2,6-diaminoheptanedioate
Thus, the two substrates of this enzyme are N-succinyl-LL-2,6-diaminoheptanedioate and H2O, whereas its two products are succinate and LL-2,6-diaminoheptanedioate.
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-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase. This enzyme is also called N-succinyl-L-alpha,epsilon-diaminopimelic acid deacylase. This enzyme participates in lysine biosynthesis.
References[edit]
- Kindler SH, Gilvarg C (December 1960). "N-Succinyl-L-2,6-diaminopimelic acid deacylase". The Journal of Biological Chemistry. 235: 3532–5. PMID 13756049.
