Enoylpyruvate transferase

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<StructureSection load='3swe' size='350' side='right' caption='Structure of enoylpyruvate transferase complex with PEP, UDP-N-acetylglucosamine, glycerol and sulfate (PDB entry [[3swe]])' scene=''>
<StructureSection load='3swe' size='350' side='right' caption='Structure of enoylpyruvate transferase complex with PEP, UDP-N-acetylglucosamine, glycerol and sulfate (PDB entry [[3swe]])' scene=''>
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== 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 and is a target for antibiotics. MurA is composed of catalytic domain and C-terminal domain.
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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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== Relevance ==
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MurA is a target for antibiotics such as fosfomycin.
</StructureSection>
</StructureSection>
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**[[3swg]] – AaMurA + UNAG + PEP<BR />
**[[3swg]] – AaMurA + UNAG + PEP<BR />
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}}
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== References ==
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<references/>
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[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 17:03, 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

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Michal Harel, Alexander Berchansky

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