Reaction: ATP + UDP-N-acetyl-α-D-muramoyl-L-alanine + L-glutamate = ADP + phosphate + UDP-N-acetyl-α-D-muramoyl-L-alanyl-L-glutamate
Other name(s): murD2 (gene name); UDP-N-acetyl-α-D-muramoyl-L-alanyl-L-glutamate synthetase; UDP-MurNAc-L-Ala-L-Glu synthetase
Systematic name: UDP-N-acetylmuramoyl-L-alanineL-glutamate ligase (ADP-forming)
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 220.127.116.11, 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 18.104.22.168, glutamate racemase, and EC 22.214.171.124, UDP-N-acetylmuramoyl-L-alanineD-glutamate ligase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
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]