N-acetyldiaminopimelate deacetylase
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| N-acetyldiaminopimelate deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.47 | ||||||||
| CAS no. | 99193-93-8 | ||||||||
| 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 N-acetyldiaminopimelate deacetylase (EC 3.5.1.47) is an enzyme that catalyzes the chemical reaction
- N-acetyl-LL-2,6-diaminoheptanedioate + H2O acetate + LL-2,6-diaminoheptanedioate
Thus, the two substrates of this enzyme are N-acetyl-LL-2,6-diaminoheptanedioate and H2O, whereas its two products are acetate 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 N6-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase. Other names in common use include N-acetyl-L-diaminopimelic acid deacylase, N-acetyl-LL-diaminopimelate deacylase, and 6-N-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase. This enzyme participates in lysine biosynthesis.
References
- Bartlett ATM; White PJ (1985). "Species of Bacillus that make a vegetative peptidoglycan containing lysine lack diaminopimelate epimerase but have diaminopimelate dehydrogenase". J. Gen. Microbiol. 131: 2145–2152. doi:10.1099/00221287-131-9-2145.
- Saleh F; White PJ (1979). "Metabolism of DD-2,6-diaminopimelic acid by a diaminopimelate-requiring mutant of Bacillus megaterium". J. Gen. Microbiol. 115: 95–100. doi:10.1099/00221287-115-1-95.
- Sundharadas G, Gilvarg C (1967). "Biosynthesis of alpha,epsilon-diaminopimelic acid in Bacillus megaterium". J. Biol. Chem. 242 (17): 3983–4. PMID 4962540.
