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Literature summary for 1.11.1.10 extracted from

  • Ayala, M.; Batista, C.V.; Vazquez-Duhalt, R.
    Heme destruction, the main molecular event during the peroxide-mediated inactivation of chloroperoxidase from Caldariomyces fumago (2011), J. Biol. Inorg. Chem., 16, 63-68.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
hydrogen peroxide the main process leading to peroxide-mediated enzyme inactivation is heme destruction (all tryptophan residues are partially oxidized in the inactive protein). 80000 molar equivalents of hydrogen peroxide are sufficient to reduce the activity of CPO to less than 5% Leptoxyphium fumago

Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
monochlorodimedone + Cl- + H2O2
-
Leptoxyphium fumago dichlorodimedone + H2O
-
?
additional information CPO is a peroxide-dependent chlorinating enzyme and it also catalyzes peroxidase-, catalase-, and cytochrome P450-type reactions of dehydrogenation, hydrogen peroxide decomposition, and oxygen insertion, respectively Leptoxyphium fumago ?
-
?

Synonyms

Synonyms Comment Organism
CPO
-
Leptoxyphium fumago

Cofactor

Cofactor Comment Organism Structure
heme
-
Leptoxyphium fumago