Enoylpyruvate transferase
From Proteopedia
(Difference between revisions)
Line 2: | Line 2: | ||
== Function == | == Function == | ||
- | '''Enoylpyruvate transferase''' (MurA) or '''UDP-N-acetylglucosamine 1-carboxyvinyltransferase''' catalyzes the ligation of phosphoenolpyruvate (PEP) to UDP-N-acetylglucosamine (UNAG). The pyruvate moiety makes the linker between the glycan and peptide portion of peptidoglycans. Thus MurA is essential for the biosynthesis of bacterial cell walls.<ref>PMID:7608103</ref>. MurC or UDP-N-acetylmuramate-L-alanine ligase adds L-alanine in the biosynthesis of peptidoglycans which form part of the protective bacterial cell wall<ref>PMID:25114134</ref>. | + | '''Enoylpyruvate transferase''' (MurA) or '''UDP-N-acetylglucosamine 1-carboxyvinyltransferase''' catalyzes the ligation of phosphoenolpyruvate (PEP) to UDP-N-acetylglucosamine (UNAG). The pyruvate moiety makes the linker between the glycan and peptide portion of peptidoglycans. Thus MurA is essential for the biosynthesis of bacterial cell walls.<ref>PMID:7608103</ref>. '''MurC''' or '''UDP-N-acetylmuramate-L-alanine ligase''' adds L-alanine in the biosynthesis of peptidoglycans which form part of the protective bacterial cell wall<ref>PMID:25114134</ref>. |
== Relevance == | == Relevance == |
Revision as of 09:42, 15 July 2021
|
References
- ↑ Brown ED, Vivas EI, Walsh CT, Kolter R. MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli. J Bacteriol. 1995 Jul;177(14):4194-7. PMID:7608103
- ↑ Humnabadkar V, Prabhakar KR, Narayan A, Sharma S, Guptha S, Manjrekar P, Chinnapattu M, Ramachandran V, Hameed SP, Ravishankar S, Chatterji M. UDP-N-acetylmuramic acid l-alanine ligase (MurC) inhibition in a tolC mutant Escherichia coli strain leads to cell death. Antimicrob Agents Chemother. 2014 Oct;58(10):6165-71. doi: 10.1128/AAC.02890-14. , Epub 2014 Aug 11. PMID:25114134 doi:http://dx.doi.org/10.1128/AAC.02890-14
- ↑ Skarzynski T, Mistry A, Wonacott A, Hutchinson SE, Kelly VA, Duncan K. Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Structure. 1996 Dec 15;4(12):1465-74. PMID:8994972