EC 6.3.2.8 - UDP-N-acetylmuramate—L-alanine ligase

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IntEnz Enzyme Nomenclature
EC 6.3.2.8

Names

Accepted name:
UDP-N-acetylmuramate—L-alanine ligase
Other names:
L-Ala ligase
L-alanine-adding enzyme
MurC synthetase
UDP-N-acetylmuramoyl-L-alanine synthetase
UDP-N-acetylmuramoylalanine synthetase
UDP-N-acetylmuramyl:L-alanine ligase
UDP-MurNAc:L-alanine ligase
UDP-acetylmuramyl-L-alanine synthetase
UDPMurNAc-L-alanine synthetase
alanine-adding enzyme
uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase
uridine diphosphate N-acetylmuramate:L-alanine ligase
uridine diphospho-N-acetylmuramoylalanine synthetase
uridine-diphosphate-N-acetylmuramate:L-alanine ligase
UDP-N-acetylmuramate:L-alanine ligase (ADP-forming)
Systematic name:
UDP-N-acetyl-α-D-muramate:L-alanine ligase (ADP-forming)

Reaction

Comments:

Involved in the synthesis of a cell-wall peptide.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC50975
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008763
CAS Registry Number: 9023-52-3
UniProtKB/Swiss-Prot: (679) [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. 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: 1773-1776 (1964).
  3. van Heijenoort, J.
    Recent advances in the formation of the bacterial peptidoglycan monomer unit.
    Nat. Prod. Rep. 18: 503-519 (2001). [PMID: 11699883]

[EC 6.3.2.8 created 1965, modified 2002]