Protein Variants | Comment | Organism |
---|---|---|
Y249F | the bimolecular rate constants of dioxygen binding to ferrous Y249F is 1.3fold higher than the wild-type value. The dissociation constants of the ferrous-dioxygen is 1.5fold higher than wild-type value | Synechocystis sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe | dioxygen binding to ferrous KatG and Y249F is reversible and monophasic. Ferrous wild-type KatG is rapidly converted by hydrogen peroxide in a two-phasic reaction via compound II to compound III, the latter being also efficiently transformed to ferric KatG. Determination of bimolecular rate constant and dissociation constant | Synechocystis sp. | |
Fe2+ | dioxygen binding to ferrous KatG and Y249F is reversible and monophasic. Ferrous wild-type KatG is rapidly converted by hydrogen peroxide in a two-phasic reaction via compound II to compound III, the latter being also efficiently transformed to ferric KatG. Determination of bimolecular rate constant and dissociation constant | Synechocystis sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
catalase-peroxidase | bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7 | Synechocystis sp. |
KatG | bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7 | Synechocystis sp. |