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Literature summary extracted from

  • Matsunaga, I.; Sumimoto, T.; Ayata, M.; Ogura, H.
    Functional modulation of a peroxygenase cytochrome P450: novel insight into the mechanisms of peroxygenase and peroxidase enzymes (2002), FEBS Lett., 528, 90-94.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.2.4
-
 Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
1.11.2.4 R242K the mutant enzyme bound with deuterated myristic acid shows greatly increased rate of 3,5,3',5'-tetramethylbenzidine oxidation Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.2.4 3,5,3',5'-tetramethylbenzidine 3,5,3',5'-tetramethylbenzidine as an additional substrate intercepts the hydroxylation of myristic acid Bacillus subtilis
1.11.2.4 myristic acid myristic acid hydroxylation is inhibited by 3,5,3',5'-tetramethylbenzidine oxidation in a 3,5,3',5'-tetramethylbenzidine concentration-dependent manner Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.2.4 0.026
-
 myristic acid pH and temperature not specified in the publication Bacillus subtilis
1.11.2.4 0.026
-
 3,5,3',5'-tetramethylbenzidine pH and temperature not specified in the publication Bacillus subtilis
1.11.2.4 0.035
-
 H2O2 pH and temperature not specified in the publication 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 3,5,3',5'-tetramethylbenzidine + H2O2 Bacillus subtilis a myristic acid-dependent reaction, when deuterated myristic acid is used as a substrate to decrease hydroxylation activity, the rate of 3,5,3',5'-tetramethylbenzidine oxidation increases ?
-
 ?
1.11.2.4 additional information Bacillus subtilis a reductase and NAD(P)H are not required for activity ?
-
 ?
1.11.2.4 myristic acid + H2O2 Bacillus subtilis
-
 ?
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.2.4
-
 Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.2.4 3,5,3',5'-tetramethylbenzidine + H2O2 a myristic acid-dependent reaction, when deuterated myristic acid is used as a substrate to decrease hydroxylation activity, the rate of 3,5,3',5'-tetramethylbenzidine oxidation increases Bacillus subtilis ?
-
 ?
1.11.2.4 additional information a reductase and NAD(P)H are not required for activity Bacillus subtilis ?
-
 ?
1.11.2.4 myristic acid + H2O2
-
 Bacillus subtilis ?
-
 ?

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.2.4 heme
-
 Bacillus subtilis