Application | Comment | Organism |
---|---|---|
additional information | the Cyt P450 monooxygenases can be utilized in the bioremediation of pollutants, as these enzymes convert chemically inert compounds to more water-soluble, hydroxylated derivatives, which may be suitable substrates for many other enzymes | Rhodococcus ruber |
Cloned (Comment) | Organism |
---|---|
DNA sequence and genomic organization determination and analysis, usage of directional genome walking method, overexpression of His6-tagged enzyme in Escherichia coli starin BL21(DE3) | Rhodococcus ruber |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0034 | - |
NADPH | pH 7.4, 25°C | Rhodococcus ruber | |
0.126 | - |
NADH | pH 7.4, 25°C | Rhodococcus ruber |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | heme iron, a cytochrome P450 enzyme | Rhodococcus ruber |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
89000 | - |
x * 89000, recombinant His6-tagged enzyme, SDS-PAGE | Rhodococcus ruber |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus ruber | Q52TE7 | strain DSM 44319 | - |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography | Rhodococcus ruber |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2 | O-dealkylation | Rhodococcus ruber | 7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ? | - |
? | |
acenaphthene + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rhodococcus ruber | 1-acenaphthenol + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
cytochrome c + NADH + H+ + O2 | - |
Rhodococcus ruber | ? | - |
r | |
cytochrome c + O2 + NADH | - |
Rhodococcus ruber | ? | - |
r | |
ethylbenzene + [reduced NADPH-hemoprotein reductase] + O2 | recombinant enzyme | Rhodococcus ruber | 1-phenylethyl alcohol + 2-phenylethyl alcohol + [reduced NADPH-hemoprotein reductase] + O2 | - |
? | |
fluorene + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rhodococcus ruber | 9-fluorenol + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
indene + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rhodococcus ruber | indenol + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
m-xylene + [reduced NADPH-hemoprotein reductase] + O2 | recombinant enzyme | Rhodococcus ruber | 3-methylbenzyl alcohol + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
additional information | product identifications, no activity with alpha-pinene, terpeneol, ethoxyresorufin, and cyclohexane, a natural self-sufficient fusion protein consisting of ferredoxin, flavin-containing reductase, and P450 monooxygenase, substrate specificity: in the presence of NADPH, the enzyme shows hydroxylation activity towards polycyclic aromatic hydrocarbons naphthalene, indene, acenaphthene, toluene, fluorene, m-xylene, and ethyl benzene, the conversion of naphthalene, acenaphthene, and fluorene results in respective ring monohydroxylated metabolites, alkyl aromatics like toluene, m-xylene, and ethyl benzene are hydroxylated exclusively at the side chains | Rhodococcus ruber | ? | - |
? | |
naphthalene + [reduced NADPH-hemoprotein reductase] + O2 | regioselective oxidation | Rhodococcus ruber | 1-naphthol + H2O + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
toluene + O2 + NAD(P)H + cytochrome c | - |
Rhodococcus ruber | benzyl alcohol + H2O + NAD(P)+ + reduced cytochrome c | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 89000, recombinant His6-tagged enzyme, SDS-PAGE | Rhodococcus ruber |
Synonyms | Comment | Organism |
---|---|---|
class IV cytochrome P450 monooxygenase | - |
Rhodococcus ruber |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | 25 | assay at | Rhodococcus ruber |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
6 | - |
NADH | pH 7.4, 25°C | Rhodococcus ruber | |
12.75 | - |
NADPH | pH 7.4, 25°C | Rhodococcus ruber |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Rhodococcus ruber |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome c | - |
Rhodococcus ruber | |
Ferredoxin | bound | Rhodococcus ruber | |
FMN | bound, quantification of the molar ratio of FMN to protein of 1.1:1 | Rhodococcus ruber | |
NAD(P)H | NADPH is preferred to NADH giving twofold higher activity | Rhodococcus ruber |