The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

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
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]
 
 


Data © 2001–2022 IUBMB
Web site © 2005–2022 Andrew McDonald