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. | ||
| - | == 3D Structures of | + | == 3D Structures of enoylpyruvate transferase == |
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Revision as of 10:18, 20 June 2013
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