Cloned (Comment) | Organism |
---|---|
- |
Brevibacterium sterolicum |
Protein Variants | Comment | Organism |
---|---|---|
E311D | mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process | Brevibacterium sterolicum |
E311L | mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process | Brevibacterium sterolicum |
E311Q | mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process | Brevibacterium sterolicum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Brevibacterium sterolicum | - |
- |
- |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Brevibacterium sterolicum |