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Literature summary for 1.14.14.1 extracted from

  • Zhang, J.; Li, A.; Xu, J.
    Improved expression of recombinant cytochrome P450 monooxygenase in Escherichia coli for asymmetric oxidation of sulfides (2010), Bioprocess Biosyst. Eng., 33, 1043-1049.
    View publication on PubMed
Search for more literature for 1.14.14.1

Cloned(Commentary)

Cloned (Comment) Organism
high level and functional expression of P450SMO in Escherichia coli strain BL21, method optimization and evaluation, overview Rhodococcus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ heme protein Rhodococcus sp.

Organism

Organism UniProt Comment Textmining
Rhodococcus sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-chlorothioanisole + [reduced NADPH-hemoprotein reductase] + O2 enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain Rhodococcus sp. 4-chlorothioanisole sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
4-fluorothioanisole + [reduced NADPH-hemoprotein reductase] + O2 enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain Rhodococcus sp. 4-fluorothioanisole sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
4-methoxythioanisole + [reduced NADPH-hemoprotein reductase] + O2 enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain Rhodococcus sp. 4-methoxythioanisole sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
4-tolylmethylsulfide + [reduced NADPH-hemoprotein reductase] + O2 enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain Rhodococcus sp. 4-tolylmethylsulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
ethyl methyl sulfide + [reduced NADPH-hemoprotein reductase] + O2 enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain Rhodococcus sp. ethyl methyl sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
phenyl methyl sulfide + [reduced NADPH-hemoprotein reductase] + O2 enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain Rhodococcus sp. phenyl methyl sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Synonyms

Synonyms Comment Organism
cytochrome P450 monooxygenase
-
 Rhodococcus sp.
More P450SMO belongs to class IV of P450 monooxygenase Rhodococcus sp.
P450SMO
-
 Rhodococcus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 whole cell assay Rhodococcus sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 50 recombinant Escherichia coli cell expressing the enzyme, at higher temperatures over 30°C, the activity decreases significantly, temperature profile, overview Rhodococcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 whole cell assay Rhodococcus sp.

pH Range

pH Minimum pH Maximum Comment Organism
5.5 8.5 recombinant Escherichia coli cell expressing the enzyme, below 7.0 or over 8.0 the enzyme activity decreases drastically, pH profile, overview Rhodococcus sp.

Cofactor

Cofactor Comment Organism Structure
heme
-
 Rhodococcus sp.
NADPH
-
 Rhodococcus sp.