N-acetyldiaminopimelate deacetylase

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
Search PMC articles PubMed articles NCBI proteins

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 ${\displaystyle \rightleftharpoons }$ 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.