A cytosolic heme-thiolate protein with sequence homology to P-450 monooxygenases. Unlike the latter, it needs neither NAD(P)H, dioxygen nor specific reductases for function. Enzymes of this type are produced by bacteria (e.g. Sphingomonas paucimobilis, Bacillus subtilis). Catalytic turnover rates are high compared with those of monooxygenation reactions as well as peroxide shunt reactions catalysed by the common P-450s. A model substrate is myristate, but other saturated and unsaturated fatty acids are also hydroxylated. Oxidizes the peroxidase substrate 3,3',5,5'-tetramethylbenzidine (TMB) and peroxygenates aromatic substrates in a fatty-acid-dependent reaction.
A cytosolic heme-thiolate protein with sequence homology to P-450 monooxygenases. Unlike the latter, it needs neither NAD(P)H, dioxygen nor specific reductases for function. Enzymes of this type are produced by bacteria (e.g. Sphingomonas paucimobilis, Bacillus subtilis). Catalytic turnover rates are high compared with those of monooxygenation reactions as well as peroxide shunt reactions catalysed by the common P-450s. A model substrate is myristate, but other saturated and unsaturated fatty acids are also hydroxylated. Oxidizes the peroxidase substrate 3,3',5,5'-tetramethylbenzidine (TMB) and peroxygenates aromatic substrates in a fatty-acid-dependent reaction.
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
P450BSbeta produces both the beta-OH (60%) and the alpha-OH (40%) fatty acids. Ferredoxin, ferredoxin reductase, and P450 reductase systems do not appear to function in P450BSbeta reactions. P450BSbeta does not require any electrons and protons for catalytic activity, because it utilizes H2O2 as an oxidant instead of O2/2e-/2H+. This enzyme requires neither a reductase nor a proton delivery system
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
P450BSbeta produces both the beta-OH (60%) and the alpha-OH (40%) fatty acids. Ferredoxin, ferredoxin reductase, and P450 reductase systems do not appear to function in P450BSbeta reactions. P450BSbeta does not require any electrons and protons for catalytic activity, because it utilizes H2O2 as an oxidant instead of O2/2e-/2H+. This enzyme requires neither a reductase nor a proton delivery system
myristic acid hydroxylation is inhibited by 3,5,3',5'-tetramethylbenzidine oxidation in a 3,5,3',5'-tetramethylbenzidine concentration-dependent manner
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ferric P450BSbeta in the substrate-bound form, sitting drop vapor diffusion method, using 10% (w/v) polyethylene glycol 3350 and 50 mM MES at pH 6.8, at 20°C
sitting drop vapor diffusion method, using 10% (w/v) PEG 4000 and 50 mM MES (pH 6.8) or 10% (w/v) PEG 4000, 0.15 mM magnesium acetate and 50 mM MES (pH 6.5) in the presence of 2 mM myristic acid
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
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
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
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
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
Lee, D.-S.; Yamada, A.; Sugimoto, H.; Matsunaga, I.; Ogura, H.; Ichihara, K.; Adachi, S.-i.; Park, S.-Y.; Shiro, Y.
Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis: Crystallographic, spectroscopic, and mutational studies
Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russigs blue formation