Enoylpyruvate transferase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | MurA is composed of <scene name='55/551189/Cv/3'>catalytic domain</scene> and <scene name='55/551189/Cv/5'>C-terminal domain</scene>. The active site is located at the interface of the two domains and binds the fosfomycin and UDP-GlcNAc.<ref>PMID:8994972</ref> | + | MurA is composed of <scene name='55/551189/Cv/3'>catalytic domain</scene> and <scene name='55/551189/Cv/5'>C-terminal domain</scene>. The active site is located at the interface of the two domains and binds the <scene name='55/551189/Cv/8'>fosfomycin</scene> and <scene name='55/551189/Cv/7'>UDP-GlcNAc</scene>.<ref>PMID:8994972</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 16:07, 21 January 2016
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3D Structures of enoylpyruvate transferase
Updated on 21-January-2016
References
- ↑ 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
- ↑ 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
