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Chemical Compound Review:

Udp-murnac-ala (2R)-2-[[(2R)-2- [(3R,4R,5S,6R)-3-acetamido...

Synonyms: AC1NURKM, 1941-66-8, Udp-N-acetylmuramylalanine, Udp-N-acetylmuramyl-L-alanine

Doublet, P. et al., Marmor, S. et al., Ashiuchi, M. et al.

Ashiuchi, Kuwana, Yamamoto, Komatsu, Soda, Misono,

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Disease relevance of Udp-murnac-ala

Furthermore, we found that the DNA gyrase of E. coli was modulated by the glutamate racemase of E. coli in the presence of UDP-N-acetylmuramyl-l-alanine, which is a peptidoglycan precursor and functions as an absolute activator for the racemase [1].

High impact information on Udp-murnac-ala

The bacterial UDP-N-acetylmuramyl-L-alanine ligase (MurC) from Escherichia coli, an essential, cytoplasmic peptidoglycan biosynthetic enzyme, catalyzes the ATP-dependent ligation of L-alanine (Ala) and UDP-N-acetylmuramic acid (UNAM) to form UDP-N-acetylmuramyl-L-alanine (UNAM-Ala) [2].
While the other reported glutamate racemases from various (essentially gram-positive) bacterial species did not require any specific activator, the E. coli enzyme absolutely requires the presence of the peptidoglycan precursor UDP-N-acetylmuramyl-L-alanine to catalyze the interconversion of glutamic acid isomers [3].

References

Glutamate racemase is an endogenous DNA gyrase inhibitor. Ashiuchi, M., Kuwana, E., Yamamoto, T., Komatsu, K., Soda, K., Misono, H. J. Biol. Chem. (2002) [Pubmed]
Biochemical characterization of a phosphinate inhibitor of Escherichia coli MurC. Marmor, S., Petersen, C.P., Reck, F., Yang, W., Gao, N., Fisher, S.L. Biochemistry (2001) [Pubmed]
Regulation of the glutamate racemase of Escherichia coli investigated by site-directed mutagenesis. Doublet, P., van Heijenoort, J., Mengin-Lecreulx, D. Microb. Drug Resist. (1996) [Pubmed]

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