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Enoylpyruvate transferase

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== Function ==
== Function ==
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'''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. MurA is composed of catalytic domain and C-terminal domain<ref>PMID:7608103</ref>.
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'''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

Structure of enoylpyruvate transferase complex with PEP, UDP-N-acetylglucosamine, glycerol and sulfate (PDB entry 3swe)

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3D Structures of enoylpyruvate transferase

Updated on 19-January-2016

References

  1. ↑ 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
  2. ↑ 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

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Michal Harel, Alexander Berchansky

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