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Accepted name: UDP-
N-acetylmuramoyl- L-alanyl- D-glutamate— L-lysine ligase
Reaction: ATP + UDP-
N-acetyl-α- D-muramoyl- L-alanyl- D-glutamate + L-lysine = ADP + phosphate + UDP- N-acetyl-α- D-muramoyl- L-alanyl-γ- D-glutamyl- L-lysine
For diagram of peptidoglycan biosynthesis (part 1),
Other name(s): MurE synthetase; UDP-
N-acetylmuramoyl- L-alanyl- D-glutamyl- L-lysine synthetase; uridine diphospho- N-acetylmuramoylalanyl- D-glutamyllysine synthetase; UPD-MurNAc- L-Ala- D-Glu: L-Lys ligase; UDP- N-acetylmuramoyl- L-alanyl- D-glutamate: L-lysine γ-ligase (ADP-forming)
Systematic name: UDP-
N-acetyl-α- D-muramoyl- L-alanyl- D-glutamate: L-lysine γ-ligase (ADP-forming)
Comments: Involved in the synthesis of a cell-wall peptide in bacteria. This enzyme adds lysine in some Gram-positive organisms; in others and in Gram-negative organisms
EC 220.127.116.11 (UDP- N-acetylmuramoyl- L-alanyl- D-glutamate—2,6-diaminopimelate ligase) adds 2,6-diaminopimelate instead.
Links to other databases:
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9023-51-2
Ito, E. and Strominger, J.L. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. I. Enzymatic addition of
L-alanine, D-glutamic acid, and L-lysine. J. Biol. Chem. 237 (1962) 2689–2695.
van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit.
Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883]
[EC 18.104.22.168 created 1961, modified 2002]
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