Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Pectobacterium carotovorum |
Protein Variants | Comment | Organism |
---|---|---|
K443A | at pH 8.0, 6.33 and 9.33 the mutant enzyme shows no measurable activity | Pectobacterium carotovorum |
K443M | at pH 8.0, 6.33 and 9.33 the mutant enzyme shows no measurable activity | Pectobacterium carotovorum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pectobacterium carotovorum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
wild-type, K443A and K443M mutant enzymes | Pectobacterium carotovorum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + (2S,5S)-5-carboxymethylproline | a mechanism is proposed where the rate-limiting step is beta-lactam ring formation coupled to a protein conformational change. The role of K443 throughout the reaction is undercored | Pectobacterium carotovorum | AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CPS | - |
Pectobacterium carotovorum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Pectobacterium carotovorum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.36 | - |
(2S,5S)-5-carboxymethylproline | pH 8.0, 25°, wild-type enzyme | Pectobacterium carotovorum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Pectobacterium carotovorum |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.04 | - |
(2S,5S)-5-carboxymethylproline | pH 8.0, 25°, wild-type enzyme | Pectobacterium carotovorum |