Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.21 extracted from

  • Jakopitsch, C.; Wanasinghe, A.; Jantschko, W.; Furtmueller, P.G.; Obinger, C.
    Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type synechocystis catalase-peroxidase and Y249F: proposal for the catalatic mechanism (2005), J. Biol. Chem., 280, 9037-9042.
    View publication on PubMed
Search for more literature for 1.11.1.21

Protein Variants

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

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

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Synonyms

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.