Application | Comment | Organism |
---|---|---|
medicine | enzyme is a target for the antibiotic fosfomycin | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
crystallization of the enzyme complexed with UDP-N-acetylglucosamine and fosfomycin, two-domain structure with the active site located between them, structure and substrate binding analysis | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
fosfomycin | binds covalently to Cys115 | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine | Escherichia coli | enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan | phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
gene murA | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine | Cys115 is the active site nucleophile | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine | substrate binding structure | Escherichia coli | phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine | - |
? | |
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine | enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan | Escherichia coli | phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | two-domain structure with the active site located between them, substrate binding structure | Escherichia coli |