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Literature summary extracted from

  • Yi, X.; Conesa, A.; Punt, P.J.; Hager, L.P.
    Examining the role of glutamic acid 183 in chloroperoxidase catalysis (2003), J. Biol. Chem., 278, 13855-13859.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.10 expression of E183H in Escherichia coli Leptoxyphium fumago

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.10 E183H the mutation is detrimental to the chlorination and dismutation activity of chloroperoxidase, activities are reduced by 85% and 50% of the wild-type activity. Epoxidation activity of the mutant enzyme is significantly enhanced, about 2.5fold 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 partial Leptoxyphium fumago

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.10 H2O2 + methylene blue
-
 Leptoxyphium fumago oxidized methylene blue + H2O
-
 ?
1.11.1.10 monochlorodimedone + Cl- + H2O2
-
 Leptoxyphium fumago dichlorodimedone + H2O
-
 ?
1.11.1.10 p-nitrostyrene + H2O2
-
 Leptoxyphium fumago p-nitrostyrene oxide + H2O
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.10 2.7 5 wild-type enzyme, chlorination activity Leptoxyphium fumago
1.11.1.10 3
-
 mutant enzyme E183H, chlorination activity Leptoxyphium fumago