Protein Variants | Comment | Organism |
---|---|---|
H69A | site-directed mutagenesis, the mutant does not bind FAD, the mutant is more sensitive to urea and unfolds at lower urea concentrations of 3 M compared to the wild-type enzyme at 5 M, the mutant also has a lower melting temperature | Brevibacterium sterolicum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Brevibacterium sterolicum | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
unfolding and folding after urea treatment of wild-type enzyme and mutant H69A, equilibrium unfolding study, kinetics | Brevibacterium sterolicum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cholesterol + O2 | - |
Brevibacterium sterolicum | cholest-4-en-3-one + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | structural determinants of the enzymes' stability | Brevibacterium sterolicum |
Synonyms | Comment | Organism |
---|---|---|
CO | - |
Brevibacterium sterolicum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Brevibacterium sterolicum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Brevibacterium sterolicum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | flavoenzyme, FAD is covalently linked to His69 | Brevibacterium sterolicum |