Crystallization (Comment) | Organism |
---|---|
crystallization of substrate-free enzyme, two-domain structure with an unusual fold, inside out alpha/beta barrel, which is built up from the 6fold repetititon of one folding unit, structure analysis | Enterobacter cloacae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine | Enterobacter cloacae | 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 |
---|---|---|---|
Enterobacter cloacae | - |
- |
- |
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 | Enterobacter cloacae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine | - |
Enterobacter cloacae | 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 | Enterobacter cloacae | phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
EPT | - |
Enterobacter cloacae |
UDP-N-acetylglucosamine enolpyruvyltransferase | - |
Enterobacter cloacae |