N-acetyldiaminopimelate deacetylase

N-acetyldiaminopimelate deacetylase
Identifiers
EC number 3.5.1.47
CAS number 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 / EGO

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 \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 and 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. 
  • Saleh F and White PJ (1979). "Metabolism of DD-2,6-diaminopimelic acid by a diaminopimelate-requiring mutant of Bacillus megaterium". J. Gen. Microbiol. 115: 95–100. 
  • Sundharadas G, Gilvarg C (1967). "Biosynthesis of alpha,epsilon-diaminopimelic acid in Bacillus megaterium". J. Biol. Chem. 242 (17): 3983–4. PMID 4962540.