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Literature summary extracted from

  • Matsunaga, I.; Ueda, A.; Sumimoto, T.; Ichihara, K.; Ayata, M.; Ogura, H.
    Site-directed mutagenesis of the putative distal helix of peroxygenase cytochrome P450 (2001), Arch. Biochem. Biophys., 394, 45-53.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.2.4 expressed in Escherichia coli M15 (pREP4) cells Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
1.11.2.4 A246K the mutant shows a large decrease in activity and a roughly 19fold lower affinity for myristic acid than the wild type enzyme Bacillus subtilis
1.11.2.4 A246S the mutation decreases the catalytic activity, but does not affect affinity for myristic acid Bacillus subtilis
1.11.2.4 A246V the mutant shows slightly reduced activity and moderately reduced affinity for myristic acid Bacillus subtilis
1.11.2.4 F250K the mutant shows decreased specific activity compared to the wild type enzyme Bacillus subtilis
1.11.2.4 I244K the mutant shows decreased specific activity compared to the wild type enzyme Bacillus subtilis
1.11.2.4 I247K the mutant shows decreased specific activity compared to the wild type enzyme Bacillus subtilis
1.11.2.4 L237K the mutants shows specific activity similar to the wild type enzyme Bacillus subtilis
1.11.2.4 L241K the mutants shows specific activity similar to the wild type enzyme Bacillus subtilis
1.11.2.4 L251K the mutant shows decreased specific activity compared to the wild type enzyme Bacillus subtilis
1.11.2.4 P243A the mutant shows decreased specific activity compared to the wild type enzyme and gives an absorption spectrum that is not characteristic of a nitrogenous ligand-bound form of a ferric P450 Bacillus subtilis
1.11.2.4 P243H inactive, the mutant gives an absorption spectrum characteristic of a nitrogenous ligand-bound form of a ferric P450 Bacillus subtilis
1.11.2.4 P243K inactive, the mutant gives an absorption spectrum characteristic of a nitrogenous ligand-bound form of a ferric P450 Bacillus subtilis
1.11.2.4 P243S the mutant shows decreased specific activity compared to the wild type enzyme and gives an absorption spectrum that is not characteristic of a nitrogenous ligand-bound form of a ferric P450 Bacillus subtilis
1.11.2.4 R242A the mutant shows about a 5fold lower affinity than the wild type for myristic acid, if cumene hydroperoxide is used instead of H2o2, however, the Km value is not affected much by this substitution Bacillus subtilis
1.11.2.4 R242K the mutant shows a large decrease in activity for myristic acid and H2O2, if cumene hydroperoxide is used instead of H2o2, however, the Km value is not affected much by this substitution Bacillus subtilis
1.11.2.4 S248K the mutant shows decreased specific activity compared to the wild type enzyme Bacillus subtilis
1.11.2.4 V245K the mutant shows decreased specific activity compared to the wild type enzyme Bacillus subtilis
1.11.2.4 Y249K the mutant shows decreased specific activity compared to the wild type enzyme Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.2.4 0.021
-
 H2O2 wild type enzyme, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C Bacillus subtilis
1.11.2.4 0.11
-
 cumene hydroperoxide mutant enzyme R242A, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C Bacillus subtilis
1.11.2.4 0.2
-
 cumene hydroperoxide wild type enzyme, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C Bacillus subtilis
1.11.2.4 0.21
-
 H2O2 mutant enzyme R242K, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C Bacillus subtilis
1.11.2.4 0.24
-
 cumene hydroperoxide mutant enzyme R242K, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C Bacillus subtilis
1.11.2.4 4.4
-
 H2O2 mutant enzyme R242A, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C 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 CYP152A1 attacks the beta-carbon as well as the alpha-carbon of myristic acid ?
-
 ?

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 Ni-NTA agarose column chromatography, gel filtration Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.2.4 myristic acid + cumene hydroperoxide
-
 Bacillus subtilis ?
-
 ?
1.11.2.4 myristic acid + H2O2
-
 Bacillus subtilis ?
-
 ?
1.11.2.4 myristic acid + H2O2 CYP152A1 attacks the beta-carbon as well as the alpha-carbon of myristic acid Bacillus subtilis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.2.4 CYP152A1
-
 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