IUBMB Enzyme Nomenclature

EC 5.1.1.23

Accepted name: UDP-N-acetyl-α-D-muramoyl-L-alanyl-L-glutamate epimerase

Reaction: ATP + UDP-N-acetyl-α-D-muramoyl-L-alanyl-L-glutamate + H2O = AMP + diphosphate + UDP-N-acetyl-α-D-muramoyl-L-alanyl-D-glutamate

Other name(s): murL (gene name); UDP-MurNAc-L-Ala-L-Glu epimerase

Systematic name: UDP-N-acetyl-α-D-muramoyl-L-alanyl-L-glutamate L-glutamate-epimerase

Comments: The enzyme, characterized from the bacterium Xanthomonas oryzae, catalyses epimerization of the terminal L-glutamate in UDP-N-acetyl-α-D-muramoyl-L-alanyl-L-glutamate. The reaction proceeds only in one direction and involves an adenylated intermediate. The combined activity of this enzyme and EC 6.3.2.53, UDP-N-acetylmuramoyl-L-alanine—L-glutamate ligase, 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: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Feng, R., Satoh, Y., Ogasawara, Y., Yoshimura, T. and Dairi, T. A glycopeptidyl-glutamate epimerase for bacterial peptidoglycan biosynthesis. J. Am. Chem. Soc. 139 (2017) 4243-4245. [PMID: 28294606]

[EC 5.1.1.23 created 2018]


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