Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.13.155 extracted from

  • Luan, Z.; Yin, Y.; Li, A.; Yu, H.; Xu, J.
    Monoterpene hydroxylation with an artificial self-sufficient P450 utilizing a P450SMO reductase domain for the electron transfer (2015), J. Mol. Catal. B, 116, 78-82 .
No PubMed abstract available
Search for more literature for 1.14.13.155

Protein Variants

Protein Variants Comment Organism
additional information construction of an artificial self-sufficient P450-type monoterpene hydroxylase by fusing the wild-type P450SMO reductase domain and the P450cam(Y96F/V247L) domain to a linker region (G4S)4. The resultant chimeric P450 enzyme, chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4, catalyzes the hydroxylation of (-)-limonene and (-)-alpha-pinene as well as camphor, which are all inactive for the wild-type enzyme P450SMO Rhodococcus sp. ECU0066
Y96F/V247L mutant P450cam, shows altered substrate specificity compared to the wild-type enzyme Rhodococcus sp. ECU0066

Inhibitors

Inhibitors Comment Organism Structure
(1R,4S,6S)-1-methyl-4-(prop-1-en-2-yl)-7-oxabicyclo[4.1.0]heptane
-
 Rhodococcus sp. ECU0066
(1S,5R)-2-methyl-5-(prop-1-en-2-yl)cyclohex-2-en-1-ol
-
 Rhodococcus sp. ECU0066
(1S,6R)-3-methyl-6-(prop-1-en-2-yl)cyclohex-2-en-1-ol
-
 Rhodococcus sp. ECU0066
1,7,7-trimethylbicyclo[2.2.1]heptane-2,5-dione
-
 Rhodococcus sp. ECU0066
4,6,6-trimethylbicyclo[3.1.1]hept-3-en-2-ol
-
 Rhodococcus sp. ECU0066
4,6,6-trimethylbicyclo[3.1.1]hept-3-en-2-one
-
 Rhodococcus sp. ECU0066
5-hydroxy-1,7,7-trimethylbicyclo[2.2.1]heptan-2-one
-
 Rhodococcus sp. ECU0066

Organism

Organism UniProt Comment Textmining
Rhodococcus sp. ECU0066
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(-)-alpha-pinene + NADH + H+ + O2 substrate enzyme mutant chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4 Rhodococcus sp. ECU0066 alpha-pinene oxide + NAD+ + H2O
-
 ?
(-)-limonene + NADH + H+ + O2 substrate of enzyme mutant chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4 Rhodococcus sp. ECU0066 (1S,6R)-isopiperitenol + (4R,6S)-carveol + (R)-1,2-epoxy-limonene
-
 ?
camphor + NADH + H+ + O2 substrate of enzyme mutant P450Cam (Y96F/V247L) and enzyme mutant chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4 Rhodococcus sp. ECU0066 5-exo-hydroxycamphor + NAD+ + H2O
-
 ?
additional information usage of artificial substrates by chimeric P450 mutants, the wild-type P450SMO reductase shows no activity with substrates camphor, (-)-alpha-pinene, and (-)-limonene Rhodococcus sp. ECU0066 ?
-
 ?

Subunits

Subunits Comment Organism
More the cytochrome P450 enzyme consists of a heme domain, a flavin-reductase domain containing FMN and NADPH binding sites, and a[Fe2S2] ferredoxin domain Rhodococcus sp. ECU0066

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25 30 assay at Rhodococcus sp. ECU0066

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Rhodococcus sp. ECU0066

Cofactor

Cofactor Comment Organism Structure
cytochrome P450
-
 Rhodococcus sp. ECU0066