Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutants in Escherichia coli | Enterobacter cloacae |
Protein Variants | Comment | Organism |
---|---|---|
D305A | site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity, fosfomycin is not covalently attached to Cys115 | Enterobacter cloacae |
D305C | site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity | Enterobacter cloacae |
D305E | site-directed mutagenesis, weaker binding of UDP-GlcNAc, 0.1% activity compared to the wild-type | Enterobacter cloacae |
D305H | site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity, fosfomycin is not covalently attached to Cys115 | Enterobacter cloacae |
N23A | site-directed mutagenesis, reduced activity, 20fold higher apparent dissociation constant for fosfomycin compared to wild-type | Enterobacter cloacae |
N23S | site-directed mutagenesis, reduced activity, 200fold higher apparent dissociation constant for fosfomycin compared to wild-type | Enterobacter cloacae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Enterobacter cloacae | - |
MurA | - |
Enterobacter cloacae | - |
recombinant purified enzyme | - |
Enterobacter cloacae DSM 30054 | - |
MurA | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine | mechanism | Enterobacter cloacae | |
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine | D305 has a dual role as a general base and an essential binding partner to UDP-GlcNAc | Enterobacter cloacae | |
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine | N23 is responsible for stabilization of transition states | Enterobacter cloacae | |
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine | Asn23 and Asp305 are essential in the active site | Enterobacter cloacae | |
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine | enyme exhibits an open conformation when substrate-free, and a closed, tightly-packed conformation upon substrate binding | 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 | - |
r | |
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine | - |
Enterobacter cloacae DSM 30054 | phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine | - |
r |