Information on EC 1.14.13.89 - isoflavone 2-hydroxylase

for references in articles please use BRENDA:EC1.14.13.89
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.14.13.89
transferred to EC 1.14.14.90
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RECOMMENDED NAME
GeneOntology No.
isoflavone 2-hydroxylase
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Isoflavonoid biosynthesis
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Biosynthesis of secondary metabolites
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. mongolicus
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in isoflavonoid biosynthesis
physiological function
the enzyme promotes the accumulation of medicarpin malonyl glucoside
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
daidzein + NADPH + H+ + O2
2'-hydroxydaidzein + NADP+ + H2O
show the reaction diagram
Q2LAL0;
-
-
-
?
daidzein + NADPH + O2
2'-hydroxydaidzein + NADP+ + H2O
show the reaction diagram
Q2LAL0;
-
-
-
?
genistein + NADPH + H+ + O2
2'-hydroxygenistein + NADP+ + H2O
show the reaction diagram
Q2LAL0;
-
-
-
?
genistein + NADPH + O2
2'-hydroxygenistein + NADP+ + H2O
show the reaction diagram
Q2LAL0;
low activity
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-
?
moe
?
show the reaction diagram
Q2LAL0;
no activity with formononetin, cf. EC 1.14.13.53, 4'-methoxyisoflavone 2'-hydroxylase
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
daidzein + NADPH + H+ + O2
2'-hydroxydaidzein + NADP+ + H2O
show the reaction diagram
Q2LAL0
-
-
-
?
genistein + NADPH + H+ + O2
2'-hydroxygenistein + NADP+ + H2O
show the reaction diagram
Q2LAL0
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P-450
Q2LAL0;
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cytochrome P450
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heme
Q2LAL0;
;
NADPH
Q2LAL0;
;
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
protein CPR
Q2LAL0;
is an essential redox partner for functional expression of CYP; is an essential redox partner for functional expression of CYP
-
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
AmI2'H is expressed throughout the entire plant
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
transmembrane enzyme
Manually annotated by BRENDA team
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
secondary structure analysis of AmI2'H
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant truncated enzyme, lacking the N-terminal membrane binding motif, from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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; 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; 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; expression in Escherichia coli C41
Q2LAL0;
gene AmI2'H or CYP81E42, DNA and amino acid sequence determination and analysis, recombinant expression of truncated enzyme, lacking the N-terminal membrane binding motif, in Escherichia coli strain BL21(DE3). Expression of the enzyme without removal of the transmembrane domain or insertion of the hydrophilic peptide AKKTSSKGKL is unsuccessful
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the gene is upregulated during infection by Candidatus Leiberibacter asiaticus
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
modification of the gene sequence to facilitate protein expression and increase protein solubility, removal of the N-terminal membrane binding motif to enhance protein solubility
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.89)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)