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Literature summary extracted from

  • Shoji, O.; Wiese, C.; Fujishiro, T.; Shirataki, C.; Wunsch, B.; Watanabe, Y.
    Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russig’s blue formation (2010), J. Biol. Inorg. Chem., 15, 1109-1115.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.11.2.4 V170F the hydroxylation activity of V170F for myristic acid is about one third of that of the wild type, but its catalytic activities for aromatic hydroxylation in the presence of octanoic acid or nonanoic acid are comparable to the catalytic activity of the wild type with pentanoic acid Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.2.4 myristic acid + H2O2 Bacillus subtilis
-
 ?
-
 ?
1.11.2.4 palmitic acid + H2O2 Bacillus subtilis
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.2.4 Bacillus subtilis O31440
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.2.4 1-methoxynaphthalene + H2O2 in the presence of heptanoic acid as a decoy molecule Bacillus subtilis 4-methoxy-1-naphthol + H2O
-
 ?
1.11.2.4 myristic acid + H2O2
-
 Bacillus subtilis ?
-
 ?
1.11.2.4 palmitic acid + H2O2
-
 Bacillus subtilis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.2.4 CYP152A1
-
 Bacillus subtilis
1.11.2.4 hydrogen peroxide-dependent cytochrome P450BSbeta
-
 Bacillus subtilis
1.11.2.4 P450 peroxygenase
-
 Bacillus subtilis