Enoylpyruvate transferase

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<StructureSection load='3swe' size='350' side='right' caption='Structure of enoylpyruvate transferase complex with PEP and UDP-N-acetylglucosamine (PDB entry [[3swe]])' scene=''>
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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=''>
'''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.
'''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.

Revision as of 10:22, 20 June 2013

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

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Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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