EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.93 | full-length wild-type enzyme or the double mutant variant H296S/H309S are transformed in Escherichia coli BL21 | Pseudomonas sp. |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.5.1.93 | preliminary crystals of the double mutant can be grown from 4% PEG 8000, 100 mM Tris-HCl, pH 8.5, carried out by vapour diffusion using hanging-drop method at 17.85°C, 1.57 A resolution | Pseudomonas sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.93 | Pseudomonas sp. | - |
N176 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.1.93 | - |
Pseudomonas sp. |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.5.1.93 | additional information | - |
double mutant H296S/H309S exhibits 22fold enhanced specificity and reactivity for cephalosporin C over the natural substrate glutaryl-7-aminocephalosporanic acid | Pseudomonas sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.93 | cephalosporin C + H2O | double mutant H296S/H309S exhibits 22fold enhanced specificity and reactivity for cephalosporin C over the natural substrate glutaryl-7-aminocephalosporanic acid | Pseudomonas sp. | cephalosporanic acid + 2-amino-5-hydroxypentanoate | - |
? | |
3.5.1.93 | glutaryl-7-aminocephalosporanic acid + H2O | double mutant H296S/H309S exhibits 22fold enhanced specificity and reactivity for cephalosporin C over the natural substrate glutaryl-7-aminocephalosporanic acid | Pseudomonas sp. | 7-aminocephalosporanic acid + glutarate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.93 | cephalorin acylase | - |
Pseudomonas sp. |