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Literature summary extracted from

  • Conesa, A.; Van de Velde, F.; Van Rantwijk, F.; Sheldon, R.A.; Van den Hondel, C.A.M.J.J.; Punt, P.J.
    Expression of the Caldariomyces fumago chloroperoxidase in Aspergillus niger and characterization of the recombinant enzyme (2001), J. Biol. Chem., 276, 17635-17640.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.10 expression in Aspergillus niger Leptoxyphium fumago

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.10 Leptoxyphium fumago
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.10 recombinant enzyme Leptoxyphium fumago

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.10 indole + Cl- + H2O2
-
Leptoxyphium fumago oxindole + monochloroindole + H2O
-
?
1.11.1.10 indole + H2O2
-
Leptoxyphium fumago 2-oxindole + H2O
-
?
1.11.1.10 monochlorodimedon + Cl- + H2O2
-
Leptoxyphium fumago dichlorodimedon + H2O
-
?
1.11.1.10 additional information oxidation of substituted indoles and sulfides with H2O2 Leptoxyphium fumago ?
-
?
1.11.1.10 thioanisole + H2O2
-
Leptoxyphium fumago methyl-phenyl sulfoxide + ?
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.10 2.8
-
chlorination of monochlorodimedone Leptoxyphium fumago

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.10 heme the recombinant enzyme is only partly, 40%, occupied with heme Leptoxyphium fumago