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Literature summary for 1.14.14.90 extracted from

  • Uchida, K.; Akashi, T.; Aoki, T.
    Functional expression of cytochrome P450 in Escherichia coli An approach to functional analysis of uncharacterized enzymes for flavonoid biosynthesis (2015), Plant Biotechnol., 32, 205-213 .
No PubMed abstract available
Search for more literature for 1.14.14.90

Activating Compound

Activating Compound Comment Organism Structure
protein CPR is an essential redox partner for functional expression of CYP Glycine max

Cloned(Commentary)

Cloned (Comment) Organism
dual plasmid method development for functional expression of plant CYPs in Escherichia coli, method and culture conditions optimization, overview. Gene CYP81E11, DNA and amino acid sequence determination and analysis, recombinant expression of the transmembrane-domain truncated CYP enzyme in Escherichia coli strain C41(DE3) and coexpression with CPR from Lotus japonicus as a discrete polypeptide. The optimal temperature is 25°C, addition of the heme precursor 5-aminolevulinic acid is essential for functional expression of CYP81E11 Glycine max
dual plasmid method development for functional expression of plant CYPs in Escherichia coli, method and culture conditions optimiztaion, overview. Gene CYP81E12, DNA and amino acid sequence determination and analysis, recombinant expression of the transmembrane-domain truncated CYP enzyme in Escherichia coli strain C41(DE3) and coexpression with CPR from Lotus japonicus as a discrete polypeptide. The optimal temperature is 25°C, addition of the heme precursor 5-aminolevulinic acid is essential for functional expression of CYP81E12 Glycine max
dual plasmid method development for functional expression of plant CYPs in Escherichia coli, method and culture conditions optimiztaion, overview. Gene CYP81E13, DNA and amino acid sequence determination and analysis, recombinant expression of the transmembrane-domain truncated CYP enzyme in Escherichia coli strain C41(DE3) and coexpression with CPR from Lotus japonicus as a discrete polypeptide. The optimal temperature is 25°C, addition of the heme precursor 5-aminolevulinic acid is essential for functional expression of CYP81E13 Glycine max

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
daidzein + [reduced NADPH-hemoprotein reductase] + O2 Glycine max
-
 2'-hydroxydaidzein + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
genistein + [reduced NADPH-hemoprotein reductase] + O2 Glycine max
-
 2'-hydroxygenistein + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Glycine max
-
 cv. Tamba Kurodaizu
-
Glycine max Q2LAL0 cv. Tamba Kurodaizu
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
daidzein + [reduced NADPH-hemoprotein reductase] + O2
-
 Glycine max 2'-hydroxydaidzein + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
genistein + [reduced NADPH-hemoprotein reductase] + O2
-
 Glycine max 2'-hydroxygenistein + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
additional information no activity with formononetin, cf. EC 1.14.13.53, 4'-methoxyisoflavone 2'-hydroxylase Glycine max ?
-
 ?

Synonyms

Synonyms Comment Organism
CYP81E
-
 Glycine max
CYP81E11
-
 Glycine max
CYP81E12
-
 Glycine max
CYP81E13
-
 Glycine max
I2'H
-
 Glycine max

Cofactor

Cofactor Comment Organism Structure
cytochrome P-450
-
 Glycine max
heme
-
 Glycine max
NADPH-hemoprotein reductase A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._ Glycine max