Enoylpyruvate transferase
From Proteopedia
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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. | '''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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== 3D Structures of enoylpyruvate transferase == | == 3D Structures of enoylpyruvate transferase == | ||
Revision as of 11:21, 24 November 2014
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3D Structures of enoylpyruvate transferase
Updated on 24-November-2014
