The Enzyme Database

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Accepted name: UDP-N-acetylmuramate—L-alanine ligase
Reaction: ATP + UDP-N-acetyl-α-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-α-D-muramoyl-L-alanine
For diagram of peptidoglycan biosynthesis (part 1), click here
Other name(s): MurC synthetase; UDP-N-acetylmuramoyl-L-alanine synthetase; uridine diphospho-N-acetylmuramoylalanine synthetase; UDP-N-acetylmuramoylalanine synthetase; L-alanine-adding enzyme; UDP-acetylmuramyl-L-alanine synthetase; UDPMurNAc-L-alanine synthetase; L-Ala ligase; uridine diphosphate N-acetylmuramate:L-alanine ligase; uridine 5′-diphosphate-N-acetylmuramyl-L-alanine synthetase; uridine-diphosphate-N-acetylmuramate:L-alanine ligase; UDP-MurNAc:L-alanine ligase; alanine-adding enzyme; UDP-N-acetylmuramyl:L-alanine ligase; UDP-N-acetylmuramate:L-alanine ligase (ADP-forming)
Systematic name: UDP-N-acetyl-α-D-muramate:L-alanine ligase (ADP-forming)
Comments: Involved in the synthesis of a cell-wall peptide in bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-52-3
1.  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.
2.  Nathenson, S.G., Strominger, J.L. and Ito, E. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. IV. Purification and properties of D-glutamic acid-adding enzyme. J. Biol. Chem. 239 (1964) 1773–1776. [PMID: 14213349]
3.  van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883]
[EC created 1965, modified 2002]

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