EC 6.3.2.53 - UDP-N-acetylmuramoyl-L-alanine—L-glutamate ligase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 6.3.2.53

Names

Accepted name:
UDP-N-acetylmuramoyl-L-alanine—L-glutamate ligase
Other names:
UDP-N-acetyl-α-D-muramoyl-L-alanyl-L-glutamate synthetase
UDP-MurNAc-L-Ala-L-Glu synthetase
Systematic name:
UDP-N-acetylmuramoyl-L-alanine—L-glutamate ligase (ADP-forming)

Reaction

Comments:

The enzyme, characterized from the bacterium Xanthomonas oryzae, catalyses the ligation of a terminal L-glutamate to UDP-N-acetyl-α-D-muramoyl-L-alanine. The combined activity of this enzyme and EC 5.1.1.23, UDP-N-acetyl-α-D-muramoyl-L-alanyl-L-glutamate epimerase, provides an alternative route for incorporating D-glutamate into peptidoglycan, replacing the more common combination of EC 5.1.1.3, glutamate racemase, and EC 6.3.2.9, UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (10) [show] [UniProt]

References

  1. Feng, R., Satoh, Y., Ogasawara, Y., Yoshimura, T., Dairi, T.
    A Glycopeptidyl-Glutamate Epimerase for Bacterial Peptidoglycan Biosynthesis.
    J. Am. Chem. Soc. 139: 4243-4245 (2017). [PMID: 28294606]

[EC 6.3.2.53 created 2018]