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Literature summary for 1.14.14.1 extracted from

  • Zhang, J.D.; Li, A.T.; Yang, Y.; Xu, J.H.
    Sequence analysis and heterologous expression of a new cytochrome P450 monooxygenase from Rhodococcus sp. for asymmetric sulfoxidation (2010), Appl. Microbiol. Biotechnol., 85, 615-624.
    View publication on PubMed

Application

Application Comment Organism
biotechnology enzymatic activity of P450SMO makes it an attractive biocatalyst for asymmetric synthesis of enantiopure sulfoxides Rhodococcus sp.

Cloned(Commentary)

Cloned (Comment) Organism
into the pET28a (+) vector and expressed in Escherichia coli BL21 (DE3) Rhodococcus sp.

Inhibitors

Inhibitors Comment Organism Structure
imidazole at 20 mM, only half of P450SMO activity remains Rhodococcus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the C-terminal reductase portion of P450SMO comprises a [2Fe2S] ferredoxin center Rhodococcus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
87190
-
sequence analysis Rhodococcus sp.

Organism

Organism UniProt Comment Textmining
Rhodococcus sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
gel filtration Rhodococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7-ethoxycoumarin + NADPH + H+ + O2 mediates the O-dealkylation Rhodococcus sp. 7-hydroxycoumarin + NADP+ + H2O + ?
-
?
additional information no hydroxylation activity towards naphthalene, indene, ethyl benzene, and m-xylene Rhodococcus sp. ?
-
?
p-chlorothioanisole + [reduced NADPH-hemoprotein reductase] + O2
-
Rhodococcus sp. ?
-
?
p-fluorothioanisole + [reduced NADPH-hemoprotein reductase] + O2
-
Rhodococcus sp. ?
-
?
p-methoxythioanisole + [reduced NADPH-hemoprotein reductase] + O2
-
Rhodococcus sp. ?
-
?
p-tolyl methyl sulfide + [reduced NADPH-hemoprotein reductase] + O2
-
Rhodococcus sp. ?
-
?
phenyl ethyl sulfide + [reduced NADPH-hemoprotein reductase] + O2
-
Rhodococcus sp. ?
-
?

Synonyms

Synonyms Comment Organism
cytochrome P450 monooxygenase
-
Rhodococcus sp.
P450SMO
-
Rhodococcus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
toward p-chlorothioanisole Rhodococcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
toward p-chlorothioanisole Rhodococcus sp.

Cofactor

Cofactor Comment Organism Structure
FMN the C-terminal reductase portion of P450SMO comprises an FMN-binding Rhodococcus sp.
NADH the C-terminal reductase portion of P450SMO comprises an NADH-binding Rhodococcus sp.
NADPH
-
Rhodococcus sp.

pI Value

Organism Comment pI Value Maximum pI Value
Rhodococcus sp.
-
-
5.17