EC 6.3.2.9 - UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase

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IntEnz Enzyme Nomenclature
EC 6.3.2.9

Names

Accepted name:
UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase
Other names:
D-glutamate ligase
D-glutamate-adding enzyme
MurD synthetase
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
UDP-Mur-NAC-L-Ala:D-Glu ligase
uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase
UDP-N-acetylmuramoyl-L-alanine:glutamate ligase (ADP-forming)
UDP-N-acetylmuramoylalanine—D-glutamate ligase
UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (ADP-forming)
Systematic name:
UDP-N-acetyl-α-D-muramoyl-L-alanine:D-glutamate ligase (ADP-forming)

Reaction

Comments:

Involved in the synthesis of a cell-wall peptide in bacteria.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008764
CAS Registry Number: 9023-59-0
UniProtKB/Swiss-Prot: (483) [show] [UniProt]

References

  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 6.3.2.9 created 1965, modified 2002]