UDP-N-acetylmuramate—L-alanine ligase

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UDP-N-acetylmuramate-L-alanine ligase
EC number
CAS number 9023-52-3
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, an UDP-N-acetylmuramate—L-alanine ligase (EC is an enzyme that catalyzes the chemical reaction

ATP + UDP-N-acetylmuramate + L-alanine ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine

The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramate, and L-alanine, whereas its 3 products are ADP, phosphate, and UDP-N-acetylmuramoyl-L-alanine.

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is UDP-N-acetylmuramate:L-alanine ligase (ADP-forming). Other names in common use include 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, and UDP-N-acetylmuramyl:L-alanine ligase. This enzyme participates in d-glutamine and d-glutamate metabolism and peptidoglycan biosynthesis.

Structural studies[edit]

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1GQQ, 1GQY, 1J6U, 1P31, 1P3D, and 2F00.


  • Ito, E; Strominger JL (1962). "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: 2689–2695. 
  • Nathenson SG, Strominger JL, Ito, E (1964). "Enzymatic synthesis of the peptide in bacterial uridine nucleotides IV. Purification and properties of D-glutamic acid-adding enzyme". J. Biol. Chem. 239: 1773–1776. PMID 14213349. 
  • van Heijenoort J (2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Nat. Prod. Rep. 18 (5): 503–19. PMID 11699883. doi:10.1039/a804532a.