BRENDA - Enzyme Database show
show all sequences of 1.14.14.126

beta-Amyrin synthase (EsBAS) and beta-amyrin 28-oxidase (CYP716A244) in oleanane-type triterpene saponin biosynthesis in Eleutherococcus senticosus

Jo, H.J.; Han, J.Y.; Hwang, H.S.; Choi, Y.E.; Phytochemistry 135, 53-63 (2017)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
CYP716A244, DNA and amino acid sequence determination and analysis, phylogenetic analysis. quantitative RT-PCR enzyme expression analysis, transcriptomics analysis of plant leaves, recombinant expression in Saccharomyces cerevisiae, recombinant expression in trangsgenic Nicotiana tabacum, co-expression with beta-amyrin synthase, EsBAS; gene CYP716A244, phylogenetic tree, quantitative real-time PCR expression analysis, transient recombinant expression in Nicotiana benthamiana using the transformation method via Agrobacterium tumefaciens strain GV3101, and transient recombinant expression in Saccharomyces cerevisiae with coexpression of Arabidopsis thaliana NADPH-CYP reductase
Eleutherococcus senticosus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Eleutherococcus senticosus
16020
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
bound in heme
Eleutherococcus senticosus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
Eleutherococcus senticosus
overall reaction
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
Eleutherococcus senticosus
-
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
Eleutherococcus senticosus
-
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
additional information
Eleutherococcus senticosus
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Eleutherococcus senticosus
A0A1P8W705
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
transcriptome analysis
Eleutherococcus senticosus
-
root
-
Eleutherococcus senticosus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
beta-amyrin + 3 O2 + 3 NADPH + 3 H+
-
746004
Eleutherococcus senticosus
oleanolate + 3 NADP+ + 4 H2O
-
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
overall reaction
746004
Eleutherococcus senticosus
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
beta-amyrin + O2 + NADPH + H+
-
746004
Eleutherococcus senticosus
erythrodiol + NADP+ + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
-
746004
Eleutherococcus senticosus
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
-
746004
Eleutherococcus senticosus
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol
746004
Eleutherococcus senticosus
?
-
-
-
-
additional information
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol. The enzyme is a multifunctional oxidase enzymes with beta-amyrin 28-hydroxylase, alpha-amyrin 28-hydroxylase, and lupeol 28-hydroxylase activities
746004
Eleutherococcus senticosus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 54010, about, sequence calculation
Eleutherococcus senticosus
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Eleutherococcus senticosus
heme
-
Eleutherococcus senticosus
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._
Eleutherococcus senticosus
Cloned(Commentary) (protein specific)
Commentary
Organism
CYP716A244, DNA and amino acid sequence determination and analysis, phylogenetic analysis. quantitative RT-PCR enzyme expression analysis, transcriptomics analysis of plant leaves, recombinant expression in Saccharomyces cerevisiae, recombinant expression in trangsgenic Nicotiana tabacum, co-expression with beta-amyrin synthase, EsBAS; gene CYP716A244, phylogenetic tree, quantitative real-time PCR expression analysis, transient recombinant expression in Nicotiana benthamiana using the transformation method via Agrobacterium tumefaciens strain GV3101, and transient recombinant expression in Saccharomyces cerevisiae with coexpression of Arabidopsis thaliana NADPH-CYP reductase
Eleutherococcus senticosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Eleutherococcus senticosus
heme
-
Eleutherococcus senticosus
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._
Eleutherococcus senticosus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Eleutherococcus senticosus
16020
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
bound in heme
Eleutherococcus senticosus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
Eleutherococcus senticosus
overall reaction
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
Eleutherococcus senticosus
-
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
Eleutherococcus senticosus
-
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
additional information
Eleutherococcus senticosus
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
transcriptome analysis
Eleutherococcus senticosus
-
root
-
Eleutherococcus senticosus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
beta-amyrin + 3 O2 + 3 NADPH + 3 H+
-
746004
Eleutherococcus senticosus
oleanolate + 3 NADP+ + 4 H2O
-
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
overall reaction
746004
Eleutherococcus senticosus
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
beta-amyrin + O2 + NADPH + H+
-
746004
Eleutherococcus senticosus
erythrodiol + NADP+ + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
-
746004
Eleutherococcus senticosus
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
-
746004
Eleutherococcus senticosus
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol
746004
Eleutherococcus senticosus
?
-
-
-
-
additional information
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol. The enzyme is a multifunctional oxidase enzymes with beta-amyrin 28-hydroxylase, alpha-amyrin 28-hydroxylase, and lupeol 28-hydroxylase activities
746004
Eleutherococcus senticosus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 54010, about, sequence calculation
Eleutherococcus senticosus
Expression
Organism
Commentary
Expression
Eleutherococcus senticosus
methyl jasmonate treatment highly enhances CYP716A244 transcription at 12 h after methyl jasmonate treatment, and this enhancement declines as the culture time proceeds
up
General Information
General Information
Commentary
Organism
metabolism
oleanane-type triterpenes are the major saponin components in Eleutherococcus senticosus. The two enzymes, beta-amyrin synthase and beta-amyrin 28-oxidase, are essential for oleanane-type saponin biosynthesis from 2,3-oxidosqualene
Eleutherococcus senticosus
physiological function
CYP716A244 is a beta-amyrin 28-oxidase involved in saponin biosynthesis, beta-amyrin is the oleanane-type triterpene backbone. beta-Amyrin is oxidised at the C-28 position in a sequential three-step oxidation by the single cytochrome P450 enzyme to yield oleanolic acid through erythrodiol
Eleutherococcus senticosus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
oleanane-type triterpenes are the major saponin components in Eleutherococcus senticosus. The two enzymes, beta-amyrin synthase and beta-amyrin 28-oxidase, are essential for oleanane-type saponin biosynthesis from 2,3-oxidosqualene
Eleutherococcus senticosus
physiological function
CYP716A244 is a beta-amyrin 28-oxidase involved in saponin biosynthesis, beta-amyrin is the oleanane-type triterpene backbone. beta-Amyrin is oxidised at the C-28 position in a sequential three-step oxidation by the single cytochrome P450 enzyme to yield oleanolic acid through erythrodiol
Eleutherococcus senticosus
Expression (protein specific)
Organism
Commentary
Expression
Eleutherococcus senticosus
methyl jasmonate treatment highly enhances CYP716A244 transcription at 12 h after methyl jasmonate treatment, and this enhancement declines as the culture time proceeds
up
Other publictions for EC 1.14.14.126
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744248
Zhan
Cytochrome P450 CYP716A254 ca ...
Anemone flaccida
Biochem. Biophys. Res. Commun.
495
1271-1277
2018
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2
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745002
Yasumoto
Functional characterization o ...
Solanum lycopersicum
Front. Plant Sci.
8
21
2017
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2
4
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745906
Misra
Two CYP716A subfamily cytochr ...
Ocimum basilicum
New Phytol.
214
706-720
2017
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1
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3
1
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746004
Jo
beta-Amyrin synthase (EsBAS) ...
Eleutherococcus senticosus
Phytochemistry
135
53-63
2017
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1
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1
1
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7
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1
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3
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7
1
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1
2
2
1
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746048
Tamura
Cytochrome P450 monooxygenase ...
Platycodon grandiflorus
Plant Cell Physiol.
58
874-884
2017
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-
1
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4
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5
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4
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11
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4
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8
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11
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2
3
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746049
Han
Transcriptomic analysis of Ka ...
Kalopanax septemlobus
Plant Cell Physiol.
59
319-330
2017
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2
1
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1
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7
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2
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746060
Tamura
CYP716A179 functions as a tri ...
Glycyrrhiza uralensis, Glycyrrhiza uralensis 308-19
Plant Cell Rep.
36
437-445
2017
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1
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16
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6
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6
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18
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18
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748772
Andre
Multifunctional oxidosqualene ...
Malus domestica
New Phytol.
211
1279-1294
2016
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732623
Han
The involvement of beta-amyrin ...
Panax ginseng
Plant Cell Physiol.
54
2034-2046
2013
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732622
Fukushima
CYP716A subfamily members are ...
Medicago truncatula, Vitis vinifera
Plant Cell Physiol.
52
2050-2061
2011
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2
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732627
Carelli
Medicago truncatula CYP716A12 ...
Medicago truncatula
Plant Cell
23
3070-3081
2011
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