UDP-N-acetylglucosamine enolpyruvyl transferase
UDP-N-acetylglucosamine enolpyruvyl transferase (or MurA) is an enzyme[1] that catalyzes the first committed step in peptidoglycan biosynthesis, namely the ligation of phosphoenolpyruvate (PEP) to the 3'-hydroxyl group of UDP-N-acetylglucosamine. This pyruvate moiety provides the linker that bridges the glycan and peptide portion of peptidoglycan.[2]
The enzyme is inhibited by the antibiotic fosfomycin, which covalently modifies an active site cysteine residue.[3]
References
- ↑ "Enolpyruvate transferase, EPT family". Retrieved 2008-11-23.
- ↑ Brown ED, Vivas EI, Walsh CT, Kolter R (July 1995). "MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli". J. Bacteriol. 177 (14): 4194–7. PMC 177162. PMID 7608103.
- ↑ King, Michael B. (2005). Lange Q & A. New York: McGraw-Hill, Medical Pub. Division. p. 298. ISBN 0-07-144578-1.
|
This article is issued from Wikipedia - version of the Sunday, January 10, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.