Protein Variants | Comment | Organism |
---|---|---|
additional information | the enzyme is mutated by PCR method to add a 3G3K tag to the C-terminal of the beta-subunit, the wild-type and mutated enzyme have nearly equal specific activity. The mutant enzyme has a 20% higher expressed activity than its wild-type counterpart. Immobilization of mutated and wild-type enzyme on glyoxyl agarose support via surface lysine or the poly-lysine tag, respectively | Pseudomonas sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics of free and immobilized wild-type and mutant enzymes, overview | Pseudomonas sp. | |
0.041 | - |
(7R)-7-(4-carboxybutanamido)cephalosporanate | pH 8.5, 37°C, free mutant enzyme | Pseudomonas sp. | |
0.043 | - |
(7R)-7-(4-carboxybutanamido)cephalosporanate | pH 8.5, 37°C, free wild-type enzyme | Pseudomonas sp. | |
0.0438 | - |
(7R)-7-(4-carboxybutanamido)cephalosporanate | pH 8.5, 37°C, immobilized mutant enzyme | Pseudomonas sp. | |
0.0484 | - |
(7R)-7-(4-carboxybutanamido)cephalosporanate | pH 8.5, 37°C, immobilized wild-type enzyme | Pseudomonas sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O | Pseudomonas sp. | - |
(7R)-7-aminocephalosporanate + glutarate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas sp. | P15557 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O | - |
Pseudomonas sp. | (7R)-7-aminocephalosporanate + glutarate | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterodimer | alphabeta structure, but not linked via disulfide bridge and not separable by SDS-PAGE | Pseudomonas sp. |
Synonyms | Comment | Organism |
---|---|---|
CCA | - |
Pseudomonas sp. |
cephalosporin C acylase | - |
Pseudomonas sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Pseudomonas sp. |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
free wild-type and mutant enzymes: pH 8.5, inactivation after 1 h, immobilized wild-type and mutant enzymes: pH 8.5, 30% and 10% activity remaing after 4 h | Pseudomonas sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
assay at | Pseudomonas sp. |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
the enzyme activities of both free and immobilized enzymes are greatly reduced at pH 5.5 | Pseudomonas sp. |
General Information | Comment | Organism |
---|---|---|
additional information | the protein structure of Pseudomonas SE83 CCA is obtained through the computational modeling with X-ray crystal structure of Pseudomonas N176 CCA (PDB accession code 4HST) as the template, three-dimensional structure, homology modeling, overview. The key residue of the enzyme, 1Ser of beta-subunit, is located in the active-site cavity, which is on the opposite side to the C-terminal of beta-subunit | Pseudomonas sp. |