Enoylpyruvate transferase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Enoylpyruvate transferase''' (MurA) 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. | + | '''Enoylpyruvate transferase''' (MurA) 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>. |
== Relevance == | == Relevance == | ||
MurA is a target for antibiotics such as fosfomycin. | MurA is a target for antibiotics such as fosfomycin. | ||
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| + | == Structural highlights == | ||
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| + | MurA is composed of catalytic domain and C-terminal domain. The active site is located at the interface of the two domains.<ref>PMID:8994972</ref> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 17:24, 19 January 2016
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3D Structures of enoylpyruvate transferase
Updated on 19-January-2016
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
- ↑ 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
