We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
Enoylpyruvate transferase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
<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=''> | ||
| + | == Function == | ||
| - | '''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 | + | '''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>. |
| + | |||
| + | == Relevance == | ||
| + | |||
| + | MurA is a target for antibiotics such as fosfomycin. | ||
</StructureSection> | </StructureSection> | ||
| Line 53: | Line 58: | ||
**[[3swg]] – AaMurA + UNAG + PEP<BR /> | **[[3swg]] – AaMurA + UNAG + PEP<BR /> | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
| + | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 17:03, 19 January 2016
| |||||||||||
3D Structures of enoylpyruvate transferase
Updated on 19-January-2016
