BRENDA - Enzyme Database show
show all sequences of 5.4.99.39

beta-Amyrin synthase, one of the most important key enzymes for triterpene skeleton formation in higher plants

Ma, Y.; Yang, R.; Zhou, S.; Yin, Y.; Zhang, X.; Liu, Y.; Pak. J. Bot. 50, 231-243 (2018)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene beta-AS, sequence comparisons and phylogenetic analysis
Artemisia annua
gene beta-AS, sequence comparisons and phylogenetic analysis
Avena longiglumis
gene beta-AS, sequence comparisons and phylogenetic analysis
Barbarea vurlgaris
gene beta-AS, sequence comparisons and phylogenetic analysis
Bupleurum chinense
gene beta-AS, sequence comparisons and phylogenetic analysis
Euphorbia tirucalli
gene beta-AS, sequence comparisons and phylogenetic analysis
Glycine max
gene beta-AS, sequence comparisons and phylogenetic analysis
Glycyrrhiza uralensis
gene beta-AS, sequence comparisons and phylogenetic analysis
Gypsophila vaccaria
gene beta-AS, sequence comparisons and phylogenetic analysis
Panax japonicus
gene beta-AS, sequence comparisons and phylogenetic analysis
Panax quinquefolius
gene beta-AS, sequence comparisons and phylogenetic analysis
Polygala tenuifolia
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
beta-AS of Avena longiglumis is anchored to a specific site in the cytoplasmic matrix to perform the catalytic function
Avena longiglumis
5737
-
additional information
beta-AS of Panax japonicus does not cross the membrane
Panax japonicus
-
-
additional information
beta-AS of Panax quinquefolius does not cross the membrane
Panax quinquefolius
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(3S)-2,3-epoxy-2,3-dihydrosqualene
Medicago truncatula
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Euphorbia tirucalli
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Glycine max
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Glycyrrhiza uralensis
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Avena longiglumis
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Artemisia annua
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Bupleurum chinense
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Panax quinquefolius
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Panax japonicus
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Gypsophila vaccaria
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Barbarea vurlgaris
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Polygala tenuifolia
-
beta-amyrin
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Artemisia annua
B1P7H3
-
-
Avena longiglumis
Q6IWA0
-
-
Barbarea vurlgaris
H9NAL5
-
-
Bupleurum chinense
B0ZSP3
-
-
Euphorbia tirucalli
Q401R6
-
-
Glycine max
Q8H2B0
-
-
Glycyrrhiza uralensis
D7P7W7
-
-
Gypsophila vaccaria
A3E7Y8
-
-
Medicago truncatula
-
-
-
Panax japonicus
A0A0H3YJP6
-
-
Panax quinquefolius
N0BQ25
-
-
Polygala tenuifolia
A1E4D1
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Medicago truncatula
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Artemisia annua
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Avena longiglumis
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Barbarea vurlgaris
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Bupleurum chinense
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Euphorbia tirucalli
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Glycine max
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Glycyrrhiza uralensis
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Gypsophila vaccaria
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Panax japonicus
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Panax quinquefolius
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Polygala tenuifolia
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Medicago truncatula
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Euphorbia tirucalli
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Glycine max
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Glycyrrhiza uralensis
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Avena longiglumis
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Artemisia annua
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Bupleurum chinense
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Panax quinquefolius
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Panax japonicus
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Gypsophila vaccaria
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Barbarea vurlgaris
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Polygala tenuifolia
beta-amyrin
-
-
-
r
Subunits
Subunits
Commentary
Organism
?
x * 87503, sequence calculation
Artemisia annua
?
x * 86859, sequence calculation
Avena longiglumis
?
x * 87503, sequence calculation
Barbarea vurlgaris
?
x * 87791, sequence calculation
Bupleurum chinense
?
x * 87590, sequence calculation
Euphorbia tirucalli
?
x * 84604, sequence calculation
Glycine max
?
x * 87073, sequence calculation
Glycyrrhiza uralensis
?
x * 87521, sequence calculation
Gypsophila vaccaria
?
x * 87900, sequence calculation
Panax japonicus
?
x * 87775, sequence calculation
Panax quinquefolius
?
x * 87343, sequence calculation
Polygala tenuifolia
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Panax japonicus
sequence calculation
-
5.84
Artemisia annua
sequence calculation
-
5.87
Gypsophila vaccaria
sequence calculation
-
5.89
Panax quinquefolius
sequence calculation
-
5.92
Bupleurum chinense
sequence calculation
-
6.02
Glycine max
sequence calculation
-
6.1
Avena longiglumis
sequence calculation
-
6.12
Glycyrrhiza uralensis
sequence calculation
-
6.19
Polygala tenuifolia
sequence calculation
-
6.21
Barbarea vurlgaris
sequence calculation
-
6.29
Euphorbia tirucalli
sequence calculation
-
6.78
Cloned(Commentary) (protein specific)
Commentary
Organism
gene beta-AS, sequence comparisons and phylogenetic analysis
Artemisia annua
gene beta-AS, sequence comparisons and phylogenetic analysis
Avena longiglumis
gene beta-AS, sequence comparisons and phylogenetic analysis
Barbarea vurlgaris
gene beta-AS, sequence comparisons and phylogenetic analysis
Bupleurum chinense
gene beta-AS, sequence comparisons and phylogenetic analysis
Euphorbia tirucalli
gene beta-AS, sequence comparisons and phylogenetic analysis
Glycine max
gene beta-AS, sequence comparisons and phylogenetic analysis
Glycyrrhiza uralensis
gene beta-AS, sequence comparisons and phylogenetic analysis
Gypsophila vaccaria
gene beta-AS, sequence comparisons and phylogenetic analysis
Panax japonicus
gene beta-AS, sequence comparisons and phylogenetic analysis
Panax quinquefolius
gene beta-AS, sequence comparisons and phylogenetic analysis
Polygala tenuifolia
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
beta-AS of Avena longiglumis is anchored to a specific site in the cytoplasmic matrix to perform the catalytic function
Avena longiglumis
5737
-
additional information
beta-AS of Panax japonicus does not cross the membrane
Panax japonicus
-
-
additional information
beta-AS of Panax quinquefolius does not cross the membrane
Panax quinquefolius
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(3S)-2,3-epoxy-2,3-dihydrosqualene
Medicago truncatula
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Euphorbia tirucalli
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Glycine max
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Glycyrrhiza uralensis
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Avena longiglumis
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Artemisia annua
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Bupleurum chinense
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Panax quinquefolius
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Panax japonicus
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Gypsophila vaccaria
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Barbarea vurlgaris
-
beta-amyrin
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
Polygala tenuifolia
-
beta-amyrin
-
-
r
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Medicago truncatula
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Artemisia annua
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Avena longiglumis
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Barbarea vurlgaris
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Bupleurum chinense
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Euphorbia tirucalli
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Glycine max
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Glycyrrhiza uralensis
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Gypsophila vaccaria
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Panax japonicus
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Panax quinquefolius
-
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
Polygala tenuifolia
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Medicago truncatula
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Euphorbia tirucalli
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Glycine max
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Glycyrrhiza uralensis
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Avena longiglumis
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Artemisia annua
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Bupleurum chinense
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Panax quinquefolius
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Panax japonicus
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Gypsophila vaccaria
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Barbarea vurlgaris
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
-
748823
Polygala tenuifolia
beta-amyrin
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 87503, sequence calculation
Artemisia annua
?
x * 86859, sequence calculation
Avena longiglumis
?
x * 87503, sequence calculation
Barbarea vurlgaris
?
x * 87791, sequence calculation
Bupleurum chinense
?
x * 87590, sequence calculation
Euphorbia tirucalli
?
x * 84604, sequence calculation
Glycine max
?
x * 87073, sequence calculation
Glycyrrhiza uralensis
?
x * 87521, sequence calculation
Gypsophila vaccaria
?
x * 87900, sequence calculation
Panax japonicus
?
x * 87775, sequence calculation
Panax quinquefolius
?
x * 87343, sequence calculation
Polygala tenuifolia
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Panax japonicus
sequence calculation
-
5.84
Artemisia annua
sequence calculation
-
5.87
Gypsophila vaccaria
sequence calculation
-
5.89
Panax quinquefolius
sequence calculation
-
5.92
Bupleurum chinense
sequence calculation
-
6.02
Glycine max
sequence calculation
-
6.1
Avena longiglumis
sequence calculation
-
6.12
Glycyrrhiza uralensis
sequence calculation
-
6.19
Polygala tenuifolia
sequence calculation
-
6.21
Barbarea vurlgaris
sequence calculation
-
6.29
Euphorbia tirucalli
sequence calculation
-
6.78
Expression
Organism
Commentary
Expression
Medicago truncatula
the enzyme is inducible by methyl jasmonate by 50fold in cell suspension cultures
up
General Information
General Information
Commentary
Organism
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Artemisia annua
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Avena longiglumis
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Barbarea vurlgaris
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Bupleurum chinense
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Euphorbia tirucalli
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Glycine max
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Glycyrrhiza uralensis
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Gypsophila vaccaria
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Medicago truncatula
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Panax japonicus
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Panax quinquefolius
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Polygala tenuifolia
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Artemisia annua
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Avena longiglumis
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Barbarea vurlgaris
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Bupleurum chinense
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Euphorbia tirucalli
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Glycine max
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Glycyrrhiza uralensis
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Gypsophila vaccaria
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Medicago truncatula
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Panax japonicus
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Panax quinquefolius
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Polygala tenuifolia
additional information
three-dimensional enzyme structure modeling
Avena longiglumis
additional information
beta-AS of Panax japonicus does not cross the membrane, three-dimensional enzyme structure modeling
Panax japonicus
additional information
beta-AS of Panax quinquefolius does not cross the membrane, three-dimensional enzyme structure modeling
Panax quinquefolius
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Artemisia annua
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Avena longiglumis
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Barbarea vurlgaris
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Bupleurum chinense
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Euphorbia tirucalli
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Glycine max
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Glycyrrhiza uralensis
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Gypsophila vaccaria
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Medicago truncatula
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Panax japonicus
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Panax quinquefolius
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Polygala tenuifolia
General Information (protein specific)
General Information
Commentary
Organism
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Artemisia annua
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Avena longiglumis
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Barbarea vurlgaris
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Bupleurum chinense
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Euphorbia tirucalli
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Glycine max
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Glycyrrhiza uralensis
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Gypsophila vaccaria
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Medicago truncatula
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Panax japonicus
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Panax quinquefolius
evolution
analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC)
Polygala tenuifolia
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Artemisia annua
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Avena longiglumis
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Barbarea vurlgaris
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Bupleurum chinense
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Euphorbia tirucalli
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Glycine max
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Glycyrrhiza uralensis
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Gypsophila vaccaria
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Medicago truncatula
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Panax japonicus
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Panax quinquefolius
metabolism
beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin
Polygala tenuifolia
additional information
three-dimensional enzyme structure modeling
Avena longiglumis
additional information
beta-AS of Panax japonicus does not cross the membrane, three-dimensional enzyme structure modeling
Panax japonicus
additional information
beta-AS of Panax quinquefolius does not cross the membrane, three-dimensional enzyme structure modeling
Panax quinquefolius
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Artemisia annua
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Avena longiglumis
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Barbarea vurlgaris
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Bupleurum chinense
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Euphorbia tirucalli
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Glycine max
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Glycyrrhiza uralensis
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Gypsophila vaccaria
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Medicago truncatula
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Panax japonicus
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Panax quinquefolius
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
Polygala tenuifolia
Expression (protein specific)
Organism
Commentary
Expression
Medicago truncatula
the enzyme is inducible by methyl jasmonate by 50fold in cell suspension cultures
up
Other publictions for EC 5.4.99.39
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)
748823
Ma
-
beta-Amyrin synthase, one of ...
Artemisia annua, Avena longiglumis, Barbarea vurlgaris, Bupleurum chinense, Euphorbia tirucalli, Glycine max, Glycyrrhiza uralensis, Gypsophila vaccaria, Medicago truncatula, Panax japonicus, Panax quinquefolius, Polygala tenuifolia
Pak. J. Bot.
50
231-243
2018
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39
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746004
Jo
beta-Amyrin synthase (EsBAS) ...
Eleutherococcus senticosus
Phytochemistry
135
53-63
2017
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2
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747546
Hoshino
Euphorbia tirucalli beta-amyr ...
Euphorbia tirucalli
ChemBioChem
18
2145-2155
2017
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1
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18
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18
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1
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1
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1
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2
2
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747786
Sun
beta-Amyrin synthase from Con ...
Eschenbachia blinii
FEBS open bio
7
1575-1585
2017
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1
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747921
Um
-
Functional characterization o ...
Platycodon grandiflorus
Hortic. Environ. Biotechnol.
58
613-619
2017
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1
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748812
Ito
beta-Amyrin synthase from Eup ...
Euphorbia tirucalli
Org. Biomol. Chem.
15
177-188
2017
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1
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15
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2
2
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748772
Andre
Multifunctional oxidosqualene ...
Malus domestica
New Phytol.
211
1279-1294
2016
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1
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1
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2
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3
3
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749323
Liu
An intronless beta-amyrin syn ...
Gentiana straminea
Sci. Rep.
6
33364
2016
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1
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5
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4
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2
4
8
4
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730595
Jin
Isolation and characterization ...
Polygala tenuifolia
Plant Cell Rep.
33
511-519
2014
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1
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1
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1
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730640
Misra
Methyl jasmonate-elicited tran ...
Ocimum basilicum
Plant Physiol.
164
1028-1044
2014
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1
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747597
Liu
-
Cloning, prokaryotic expressi ...
Psammosilene tunicoides
Chin. Tradit. Herbal Drugs
45
1456-1460
2014
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1
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748805
Ito
beta-Amyrin synthase from Eup ...
Euphorbia tirucalli
Org. Biomol. Chem.
12
3836-3846
2014
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1
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9
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3
3
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729601
Ito
Effect of cation-pi interactio ...
Euphorbia tirucalli
Chemistry
19
17150-17158
2013
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6
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729707
Ito
Purification, kinetics, inhibi ...
Euphorbia tirucalli
FEBS J.
280
1267-1280
2013
1
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1
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4
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3
3
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1
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3
3
730571
Yu
Functional characterization of ...
Catharanthus roseus
Phytochemistry
91
122-127
2013
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711990
Brendolise
An unusual plant triterpene sy ...
Malus domestica
FEBS J.
278
2485-2499
2011
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715030
Sawai
Molecular characterization of ...
Aster tataricus
FEBS Lett.
585
1031-1036
2011
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716502
Takagi
Manipulation of saponin biosyn ...
Glycine max
Plant Cell Rep.
30
1835-1846
2011
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Wang
Two oxidosqualene cyclases res ...
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2
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716192
Yendo
Production of plant bioactive ...
Aster sedifolius, Centella asiatica, Gentiana straminea, Gypsophila vaccaria, Medicago truncatula, Panax ginseng
Mol. Biotechnol.
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14
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6
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2
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2
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716908
Shabani
-
Assessment of squalene synthas ...
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Russ. J. Plant Physiol.
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480-484
2010
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694622
Confalonieri
Enhanced triterpene saponin bi ...
Aster sedifolius
Plant Biotechnol. J.
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2009
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1
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694752
Shibuya
Identification of a product sp ...
Arabidopsis thaliana
Plant Physiol. Biochem.
47
26-30
2009
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1
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683463
Kirby
Engineering triterpene product ...
Artemisia annua
FEBS J.
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2008
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1
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694761
Cammareri
Molecular characterization of ...
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Plant Sci.
175
255-261
2008
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683462
Basyuni
Triterpene synthases from the ...
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FEBS J.
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683985
Meesapyodsuk
Saponin biosynthesis in Sapona ...
Gypsophila vaccaria
Plant Physiol.
143
959-969
2007
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1
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684059
Chung
-
Molecular characterization of ...
Glycine max
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54
518-523
2007
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682450
Sawai
Functional and structural anal ...
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247-257
2006
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683972
Kajikawa
Cloning and characterization o ...
Euphorbia tirucalli
Phytochemistry
66
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2005
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7
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1
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683583
Abe
Enzymatic cyclization of 22,23 ...
Pisum sativum
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126
3426-3427
2004
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683584
Abe
Mechanism and stereochemistry ...
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6880-6881
2004
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684074
Noma
-
Enzymatic formation of an unna ...
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Tetrahedron Lett.
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8299-8301
2004
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1
1
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683215
Zhang
Oxidosqualene cyclases from ce ...
Betula platyphylla
Biol. Pharm. Bull.
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642-650
2003
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683984
Iturbe-Ormaetxe
Molecular cloning and characte ...
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Plant Mol. Biol.
51
731-743
2003
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1
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5
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1
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683214
Hayashi
Cloning and characterization o ...
Glycyrrhiza glabra
Biol. Pharm. Bull.
24
912-916
2001
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1
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1
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4
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1
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1
1
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683422
Morita
Molecular cloning and function ...
Pisum sativum
Eur. J. Biochem.
267
3453-3460
2000
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1
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4
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1
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683581
Kushiro
-
Mutational studies on triterpe ...
Panax ginseng
J. Am. Chem. Soc.
122
6816-6824
2000
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4
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4
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1
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683580
Kushiro
-
Chimeric triterpene synthase. ...
Arabidopsis thaliana
J. Am. Chem. Soc.
121
1208-1216
1999
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1
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683420
Kushiro
beta-Amyrin synthase - cloning ...
Panax ginseng
Eur. J. Biochem.
256
238-244
1998
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1
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4
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1
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1
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1
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1
1
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-
683970
Taton
-
Inhibition of higher plant 2,3 ...
Pisum sativum
Phytochemistry
43
75-81
1996
-
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3
1
1
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1
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1
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3
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3
3
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1
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1
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