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Literature summary extracted from

  • Murataliev, M.B.; Feyereisen, R.
    Functional interactions in cytochrome P450BM3. Fatty acid substrate binding alters electron-transfer properties of the flavoprotein domain (1996), Biochemistry, 35, 15029-15037.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.6.2.4 CO stimulation Priestia megaterium
1.6.2.4 hexadecanol stimulation Priestia megaterium
1.6.2.4 laurate stimulation Priestia megaterium
1.6.2.4 laurate plus carbon monoxide, greater stimulation compared to laurate alone or carbon monoxide alone, decrease of stimulation in the presence of NADPH Priestia megaterium
1.6.2.4 palmitate stimulation Priestia megaterium
1.6.2.4 Tetradecanol stimulation Priestia megaterium

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.2.4 expression in Escherichia coli Priestia megaterium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.2.4 additional information Priestia megaterium part of the bacterial fusion protein P450BM3 composed of cytochrome P450 fatty acid hydroxylase and NADPH cytochrome P450 reductase ?
-
 ?
1.6.2.4 NADPH + ferricytochrome P450 Priestia megaterium during hydroxylation of fatty acids through the bacterial fusion protein P450BM3 ferrocytochrome P450 + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.6.2.4 Priestia megaterium
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.2.4 expressed in Escherichia coli, column chromatography on 2',5'-ADP-agarose Priestia megaterium

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.6.2.4 oxidation of the reduced P450BM3 by cytochrome c, ferricyanide or 2,6-dichlorophenolindophenol rapidly restores electron transfer and hydroxylase activity Priestia megaterium

Storage Stability

EC Number Storage Stability Organism
1.6.2.4 expressed in E. coli, -80°C Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.4 2 ferricytochrome c + NADPH additional electron acceptor: ferricyanide Priestia megaterium 2 ferrocytochrome c + NADP+ + H+
-
 ?
1.6.2.4 2 ferricytochrome c + NADPH additional electron acceptor: cytochrome P450 Priestia megaterium 2 ferrocytochrome c + NADP+ + H+
-
 ?
1.6.2.4 2 ferricytochrome c + NADPH additional electron acceptor: 2,6-dichlorophenolindophenol Priestia megaterium 2 ferrocytochrome c + NADP+ + H+
-
 ?
1.6.2.4 ferricytochrome c + NADPH + H+
-
 Priestia megaterium ferrocytochrome c + NADP+
-
 r
1.6.2.4 additional information simultaneous catalysis of reduction of cytochrome c and hydroxylation of laurate Priestia megaterium ?
-
 ?
1.6.2.4 additional information part of the bacterial fusion protein P450BM3 composed of cytochrome P450 fatty acid hydroxylase and NADPH cytochrome P450 reductase Priestia megaterium ?
-
 ?
1.6.2.4 NADPH + ferricytochrome P450 during hydroxylation of fatty acids through the bacterial fusion protein P450BM3 Priestia megaterium ferrocytochrome P450 + NADP+
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6.2.4 53.3
-
 ferricytochrome c
-
 Priestia megaterium
1.6.2.4 417
-
 ferricytochrome c in the presence of laurate and carbon monoxide Priestia megaterium

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.2.4 FAD
-
 Priestia megaterium
1.6.2.4 FMN
-
 Priestia megaterium
1.6.2.4 NADPH
-
 Priestia megaterium