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Literature summary 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

Activating Compound

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.90 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
1.14.14.90 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
1.14.14.90 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)

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.90 cytochrome P-450
-
 Glycine max
1.14.14.90 heme
-
 Glycine max
1.14.14.90 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