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Literature summary for 1.11.1.10 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
Search for more literature for 1.11.1.10

Cloned(Commentary)

Cloned (Comment) Organism
expression in Aspergillus niger Leptoxyphium fumago

Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Leptoxyphium fumago

Substrates and Products (Substrate)

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

pH Optimum

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

Cofactor

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