N-acetyldiaminopimelate deacetylase

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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.

[edit] References

IUBMB entry for 3.5.1.47
BRENDA references for 3.5.1.47 (Recommended.)
PubMed references for 3.5.1.47
PubMed Central references for 3.5.1.47
Google Scholar references for 3.5.1.47
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: 3983–4. PMID 4962540.