EC - UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase

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IntEnz Enzyme Nomenclature


Accepted name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase
Other names:
MurE synthetase
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine synthetase
UPD-MurNAc-L-Ala-D-Glu:L-Lys ligase
uridine diphospho-N-acetylmuramoylalanyl-D-glutamyllysine synthetase
L-lysine-adding enzyme
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)



Involved in the synthesis of a cell-wall peptide. This enzyme adds lysine in some Gram-positive organisms; in others and in Gram-negative organisms EC (UDP-N-acetylmuramoylalanyl-D-glutamate—2,6-diaminopimelate ligase) adds 2,6-diaminopimelate instead.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047482
CAS Registry Number: 9023-51-2
UniProtKB/Swiss-Prot: (38) [show] [UniProt]


  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: 2689-2695 (1962).
  2. van Heijenoort, J.
    Recent advances in the formation of the bacterial peptidoglycan monomer unit.
    Nat. Prod. Rep. 18: 503-519 (2001). [PMID: 11699883]

[EC created 1961, modified 2002]