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Information on EC 5.4.99.39 - beta-amyrin synthase
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EC Tree
5.4.99.39 beta-amyrin synthaseIUBMB Comments
Some organism possess a monofunctional beta-amyrin synthase [3,4,6-11], other have a multifunctional enzyme that also catalyses the synthesis of alpha-amyrin (EC 5.4.99.40) or lupeol (EC 5.4.99.41) .
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Word Map
- 5.4.99.39
-
triterpene
- oxidosqualene
- saponin
-
triterpenoids
- lupeol
- cyclases
- glycyrrhiza
- cycloartenol
-
oleanolic
- lanosterol
- uralensis
-
oleanane-type
- 2,3-oxidosqualene
-
oleanane
-
dammarenediol
-
soyasapogenol
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
beta-amyrin synthase, beta-as, mdosc1, gsas1, gsas2, esbas, cbbas, multifunctional osc, beta-amyrin cyclase, obas1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amyrin synthase
B-AS
bAS
BAS2
beta-AS
betaAS
OXA1
Oxidosqualene cyclase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3S)-2,3-epoxy-2,3-dihydrosqualene = beta-amyrin
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-
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(3S)-2,3-epoxy-2,3-dihydrosqualene = beta-amyrin
no scrambling of methyl groups is observed during beta-amyrin formation, the isopropyl group of the lupenyl cation intermediate must be held tightly during product formation
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(3S)-2,3-epoxy-2,3-dihydrosqualene = beta-amyrin
substrate is used in chair-chair-chair-boat conformation. Cyclization first generates the tetracyclic dammarenyl C20 cation with the 17beta-side chain
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(3S)-2,3-epoxy-2,3-dihydrosqualene = beta-amyrin
cyclization pathway of (3S)-2,3-oxidosqualene to generate beta-amyrin triterpene via bicyclic, malabaricanyl, dammarenyl, baccharenyl, lupanyl, and oleanyl cation intermediates, detailed mechanism overview
(3S)-2,3-epoxy-2,3-dihydrosqualene = beta-amyrin
cyclization pathway of (3S)-2,3-oxidosqualene to generate beta-amyrin triterpene. (3S)-2,3-oxidosqualene is folded into a chair-chair-chair-boat-boat conformation in the enzyme cavity, and the proton released from the DCTA amino acid motif attacks the epoxide ring, leading to sequential ring-forming reactions and the construction of 6,6,6,6,6-fused pentacyclic ring scaffold via several carbocationic intermediates. The oleanyl cation undergoes rearrangement reactions of 1,2-hydride shifts and deprotonation of axial-oriented H-12 to yield beta-amyrin
(3S)-2,3-epoxy-2,3-dihydrosqualene = beta-amyrin
molecular substrate docking and catalytic reaction mechanism analysis, overview. Residue Y560 is responsible for the high catalytic efficiency of enzyme GsAS2 compared to GsAS1
(3S)-2,3-epoxy-2,3-dihydrosqualene = beta-amyrin
the Phe416 residue is located near the D-ring formation site and works to position the oxidosqualene substrate correctly within the reaction cavity. On the other hand, the major catalysis-related function of the Tyr259 and Trp257 residues is to yield their Pi-electrons to the cationic intermediate
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, beta-amyrin-forming)
Some organism possess a monofunctional beta-amyrin synthase [3,4,6-11], other have a multifunctional enzyme that also catalyses the synthesis of alpha-amyrin (EC 5.4.99.40) [5] or lupeol (EC 5.4.99.41) [6].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3R)-2,2-dimethyl-3-[(3E,7E,11E)-3,7,12,16-tetramethylheptadeca-3,7,11,15-tetraen-1-yl]oxirane
(3alpha,9xi,10alpha)-4,4,14,20-tetramethylpregn-7-en-3-ol
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pre-chair-chair-chair-boat conformation of substrate
about 1% of the yield with substrate 24,30-bisnor-2,3-oxidosqualene
-
?
24,30-bisnor-2,3-oxidosqualene
29,30-bisnor-beta-amyrin + 29,30-bisnorgermanicol + 29,30-bisnor-delta-amyrin
(3S)-2,3-epoxy-2,3-dihydrosqualene
beta-amyrin
-
-
-
r
(3S)-2,3-epoxy-2,3-dihydrosqualene
beta-amyrin
-
isoform SITT1 produces 13% beta-amyrin
-
?
22,23-dihydro-2,3-oxidosqualene
euph-7-en-3beta-ol + bacchar-12-en-3beta-ol
-
-
about 10% of the yield with substrate 24,30-bisnor-2,3-oxidosqualene
-
?
22,23-dihydro-2,3-oxidosqualene
euph-7-en-3beta-ol + bacchar-12-en-3beta-ol
-
substrate is in a chair-chair-chair-boat conformation
4:1 mixture of euph-7-en-3beta-ol and bacchar-12-en-3beta-ol
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?
24,30-bisnor-2,3-oxidosqualene
29,30-bisnor-beta-amyrin + 29,30-bisnorgermanicol + 29,30-bisnor-delta-amyrin
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-
-
-
?
24,30-bisnor-2,3-oxidosqualene
29,30-bisnor-beta-amyrin + 29,30-bisnorgermanicol + 29,30-bisnor-delta-amyrin
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3:1:0.2 mixture of 29,30-bisnor-beta-amyrin, 29,30-bisnorgermanicol and 29,30-bisnor-delta-amyrin, 3:1:0.2 product ratio
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?
additional information
?
-
metabolite identification by GC/MS analysis
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-
?
additional information
?
-
-
metabolite identification by GC/MS analysis
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-
?
additional information
?
-
metabolite identification by GC-MS/MS analysis
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-
?
additional information
?
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GC-MS and NMR spectroscopic product and metabolites identification from reactions of wild-type and mutant enzymes, overview
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?
additional information
?
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product identification by EIMS and NMR spectral analyses
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?
additional information
?
-
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enzyme is involved in saponin biosynthesis
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?
additional information
?
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MdOSC1 is a mixed amyrin synthase, with a 5:1 ratio of alpha-amyrin to beta-amyrin. The alpha-amyrin to beta-amyrin to lupeol production ratio for MdOSC1 from (S)-2,3-oxidosqualene is 85:13:2
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-
?
additional information
?
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MdOSC1 is a mixed amyrin synthase, with a 5:1 ratio of alpha-amyrin to beta-amyrin. The alpha-amyrin to beta-amyrin to lupeol production ratio for MdOSC1 from (S)-2,3-oxidosqualene is 85:13:2
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?
additional information
?
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GC-MS analysis metabolite identification
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme is involved in saponin biosynthesis
-
-
?
(3S)-2,3-epoxy-2,3-dihydrosqualene
beta-amyrin
-
-
-
r
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4-bromophenyl)[2-fluoro-4-([6-[methyl(prop-2-en-1-yl)amino]hexyl]oxy)phenyl]methanone
-
N,N-diethyl-2-[[(3beta)-17-methylideneandrost-5-en-3-yl]oxy]ethanamine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
[Inhibitory effects of antisense TGF beta1 on in vitro and in vivo proliferation of human bladder cancer cells]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.125
(3S)-2,2-dimethyl-3-[(3E,7E,11E,15E)-3,7,12,16,20-pentamethylhenicosa-3,7,11,15,19-pentaen-1-yl]oxirane
-
30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000698
(4-bromophenyl)[2-fluoro-4-([6-[methyl(prop-2-en-1-yl)amino]hexyl]oxy)phenyl]methanone
pH 7, 30°C
0.000102
N,N-diethyl-2-[[(3beta)-17-methylideneandrost-5-en-3-yl]oxy]ethanamine
pH 7, 30°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000107
(4-bromophenyl)[2-fluoro-4-([6-[methyl(prop-2-en-1-yl)amino]hexyl]oxy)phenyl]methanone
Euphorbia tirucalli
pH 7, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Conyza blinii, collected in 2014 from Panzhihua, Sichuan, China
UniProt
brenda
high expression of enzyme from day 4 to day 20 in medium inducing soyasaponin production, low level of expression after day 24 or in standard medium
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
the transcript level of OXA1 is very low in leaf during early vegetative stages as compared to early reproductive stages
brenda
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leaf epidermis is the preferred site of CrAS expression. CrAS is preferentialy expressed in younger leaves
brenda
highest enzyme level, very high GsAS2 activity in roots
brenda
in five-day old dark-grown seedling, enzyme expression is strongly induced by light, weakly induced by methyl jasmonate and low temperature, and not induced by elicitor or UV-B treatment
brenda
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
additional information
OXA1 is deficient in roots of early reproductive stage
brenda
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
additional information
H9NAL5
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
additional information
transcriptomics analysis of plant leaves, quantitative order of EsBAS mRNA accumulation is roots - stem barks - leaves in descending order
brenda
additional information
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transcriptomics analysis of plant leaves, quantitative order of EsBAS mRNA accumulation is roots - stem barks - leaves in descending order
brenda
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
additional information
GsAS1 transcript levels in roots are 2.3fold higher than the levels in either the leaves or stems. GsAS2 expression is 13.3fold higher than GsAS1 expression in roots and 1.6fold higher in stems
brenda
additional information
GsAS1 transcript levels in roots are 2.3fold higher than the levels in either the leaves or stems. GsAS2 expression is 13.3fold higher than GsAS1 expression in roots and 1.6fold higher in stems
brenda
additional information
-
GsAS1 transcript levels in roots are 2.3fold higher than the levels in either the leaves or stems. GsAS2 expression is 13.3fold higher than GsAS1 expression in roots and 1.6fold higher in stems
brenda
additional information
GsAS2 transcript levels in roots are 27.5fold greater compared to leaves and 18.6fold higher than in stems. GsAS2 expression is 13.3fold higher than GsAS1 expression in roots and 1.6fold higher in stems
brenda
additional information
GsAS2 transcript levels in roots are 27.5fold greater compared to leaves and 18.6fold higher than in stems. GsAS2 expression is 13.3fold higher than GsAS1 expression in roots and 1.6fold higher in stems
brenda
additional information
-
GsAS2 transcript levels in roots are 27.5fold greater compared to leaves and 18.6fold higher than in stems. GsAS2 expression is 13.3fold higher than GsAS1 expression in roots and 1.6fold higher in stems
brenda
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
additional information
about equal enzyme expression in the different tissues, quantitative tissue-specific real-time RT-PCR gene expression analysis
brenda
additional information
analysis of temporal and spatial specificity of the expression of beta-AS
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
beta-AS of Avena longiglumis is anchored to a specific site in the cytoplasmic matrix to perform the catalytic function
brenda
additional information
additional information
beta-AS of Panax japonicus does not cross the membrane
-
brenda
additional information
beta-AS of Panax quinquefolius does not cross the membrane
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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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)
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)
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)
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)
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)
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)
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)
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)
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)
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)
evolution
H9NAL5
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)
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)
evolution
PlgOSC1 not only contains a DCTAE motif that is implicated in substrate binding, but also has four repeats of the QXXXGXW motif, which is a typical feature of the triterpene synthase superfamily. PlgOSC1 has a Try residue in the MWCYCR motif that plays a role in the formation of beta-amyrin
evolution
residue F474 of Euphorbia tirucalli beta-amyrin cyclase is highly conserved in the superfamily of oxidosqualene cyclases
evolution
the enzyme is a member of the oxidosqualene cyclase (OSC) family
evolution
the sequence of the mature protein contains the highly conserved motifs (QXXXGXW/DCTAE) of OSCs and (MWCYCR) of beta-amyrin synthases
malfunction
-
saponin biosynthesis in soybean seeds is suppressed through RNA interference-mediated beta-amyrin synthase gene silencing
malfunction
enzyme mutant F474A and F474G produces significantly larger amounts of the bicyclic products and a decreased amount of beta-amyrin compared to wild-type. The mutant variant F474A produces (9betaH)-polypoda-7,13,17,21-tetraen-3beta-ol and (9betaH)-polypoda-8(26),13,17,21-tetraen-3beta-ol, which are generated from a chair-boat folding conformation. Substitutions with aliphatic amino acids lacking Pi-electrons such as Val, Leu, and Met lead to a significantly decreased production of bicyclic compounds, and in turn exhibit a higher production of beta-amyrin
malfunction
RNAi-directed suppression of GsAS1 in Gentiana straminea decreases oleonolic acid levels by 65.9%
malfunction
RNAi-directed suppression of GsAS2 in Gentiana straminea decreasing oleonolic acid levels by 21.0%
malfunction
the Gly and Ala variants with a smaller bulk size at position 483, compared to wild-type Val483, predominantly afford monocyclic camelliol C, which suggests that the orientation of the (3S)-2,3-oxidosqualene substrate is not appropriately arranged in the reaction cavity as a result of the decreased bulk size, leading to failure of its normal folding into the chair-chair-chair-boat-boat conformation. The Ile variant, with a somewhat larger bulk, affords beta-amyrin as the dominant product. Various point mutants of Trp534 exhibit significantly decreased enzymatic activities and provide no aberrantly cyclized products, although the aromatic Phe and Tyr residues are incorporated and the steric sizes of the aliphatic residues are altered. Therefore, the Trp534 residue does not stabilize the transient cation through a cation-Pi interaction. Altering the steric bulk at the Met729 position afforded the pentacyclic skeletons
malfunction
the Y259F variant shows nearly equivalent activity to that of the wild type, but aliphatic mutants such as the Ala, Val, and Leu variants show significantly decreased activity and yield the tetracyclic dammarane scaffold. The aliphatic variants of Trp257 exhibit remarkably decreased enzymatic activity, and lupeol is produced in a high production ratio. The aromatic Phe and Tyr mutants exhibit high activities owing to their more increased Pi-electron density relative to that of the aliphatic mutants, but lupeol is produced in a significantly high yield besides beta-amyrin. The Trp residue is likely to be responsible for the robust binding of Me-30 through CH-Pi interaction. The decreased Pi-electron density of the Phe and Tyr mutants compared to that of Trp results in the high production of lupeol
metabolism
-
expression of PtBS in the triterpenoid synthase-deficient yeast mutant GIL77 leads to the production of beta-amyrin as sole product
metabolism
-
functional expression of ObAS1 in Saccharomyces cerevisiae leads to the production of beta-amyrin
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
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
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
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
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
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
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
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
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
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
metabolism
H9NAL5
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
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
metabolism
MdOSC1 and MdOSC5 are key genes in apple fruit triterpene biosynthesis, analysis of biosynthetic pathway of triterpenic acids in apple, overview. The gene expression of MdOSC1 is linked to the concentrations of ursolic and oleanolic acid
metabolism
the enzyme is involved in the putative saponin biosynthetic pathway from 2,3-oxidosqualene in Eleutherococcus senticosus, overview
metabolism
the enzyme plays a key role in the biosynthesis of triterpenoid saponins
metabolism
the enzyme synthesizes beta-amyrin, a central precursor in the platycoside biosynthesis pathway, overview. 69 platycosides are identified from Platycodon grandiflorum
physiological function
beta-amyrin in Eleutherococcus senticosus may play a key role in saponin biosynthesis
physiological function
-
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
H9NAL5
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants
physiological function
Conyza blinii is a widely used medicinal herb in southwestern China. The main pharmacological components of Conyza blinii are a class of oleanane-type pentacyclic triterpene glycosides, known as conyzasaponins, which are thought to be synthesized from beta-amyrin. The beta-amyrin synthase mediates cyclization of 2,3-oxidosqualene to yield beta-amyrin. The enzyme is an oxidosqualene cyclase (OSC) involved in conyzasaponin biosynthesis
physiological function
GsAS2 plays a more important role than GsAS1 in oleanolic acid biosynthesis in Gentiana straminea. Wild-type GsAS1 and mutant GsAS1 H560Y show 7-11% of wild-type GSAS2 activity
physiological function
the enzyme is involved in the biosynthesis of pentacyclic triterpenes, which, in apple, account for 32-70% of the epicuticular waxes, depending on the cultivar
physiological function
the enzyme plays a key role in the biosynthesis of triterpenoid saponins
additional information
analysis of triterpenes from apple fruits in a collection of 20 contrasting apple cultivars, expression patterns of triterpene-related genes in different apple cultivars, overview
additional information
-
analysis of triterpenes from apple fruits in a collection of 20 contrasting apple cultivars, expression patterns of triterpene-related genes in different apple cultivars, overview
additional information
beta-AS of Panax japonicus does not cross the membrane, three-dimensional enzyme structure modeling
additional information
beta-AS of Panax quinquefolius does not cross the membrane, three-dimensional enzyme structure modeling
additional information
catalytically important residue F474 residue is located near the B-ring formation site. The major role of Phe474 is not to stabilize the transient cation via cation-Pi interaction, but is to confer the appropriate steric bulk near the B-ring formation site, leading to the completion of the normal polycyclization pathway without accumulation of abortive cyclization products
additional information
the highly conserved aromatic residues Phe413, Tyr259 and Trp257 disclose the importance of the appropriate steric bulk, and cation-Pi and CH-Pi interactions for the efficient catalytic action of the polyolefin cyclization cascade, functional analysis, overview. Homology modeling of beta-amyrin synthase using the X-ray crystal structure of human lanosterol cyclase, PDB ID 1w6k, as template. Structure comparisons. The Tyr259 residue stabilizes the baccharenyl secondary cation via cation-Pi interaction, residue Trp257 stabilizes the oleanyl cation via cation-Pi interaction
additional information
the intronless beta-amyrin synthase gene GSAS2 is more efficient in oleanolic acid accumulation than its paralogue GsAS1 in Gentiana straminea. Both enzymes harbor two (alpha/alpha) barrel domains connected by loops, as well as three smaller beta structures
additional information
the intronless beta-amyrin synthase gene GSAS2 is more efficient in oleanolic acid accumulation than its paralogue GsAS1 in Gentiana straminea. Both enzymes harbor two (alpha/alpha) barrel domains connected by loops, as well as three smaller beta structures
additional information
-
the intronless beta-amyrin synthase gene GSAS2 is more efficient in oleanolic acid accumulation than its paralogue GsAS1 in Gentiana straminea. Both enzymes harbor two (alpha/alpha) barrel domains connected by loops, as well as three smaller beta structures
additional information
the Trp534 residue does not stabilize the transient cation through a cation-Pi interaction. the Trp residue, with the largest steric bulk among all natural amino acids, is essential for high enzymatic activity. Robust CH-Pi complexation between the Val483 and Trp534 residues is proposed. Met729 is positioned at the E-ring formation site. Homology modeling and structure-function analysis, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BAMS1_BARVU
762
1
87503
Swiss-Prot
other Location (Reliability: 2)
BAMS1_PANGI
763
0
87994
Swiss-Prot
other Location (Reliability: 2)
BAMS2_PANGI
761
0
87875
Swiss-Prot
other Location (Reliability: 4)
BAMS_BETPL
779
0
89558
Swiss-Prot
other Location (Reliability: 2)
BAMS_GLYGL
765
0
87516
Swiss-Prot
other Location (Reliability: 2)
BAMS_PEA
758
0
87244
Swiss-Prot
other Location (Reliability: 3)
BAMS_SOLLC
761
0
87248
Swiss-Prot
other Location (Reliability: 4)
DAMS_SOLLC
763
0
88036
Swiss-Prot
other Location (Reliability: 4)
ABAMS_PEA
764
0
88277
Swiss-Prot
other Location (Reliability: 2)
BASM1_KALSE
763
0
87385
Swiss-Prot
other Location (Reliability: 2)
BAS_BRUGY
759
0
87665
Swiss-Prot
other Location (Reliability: 2)
LUP1_ARATH
757
0
87352
Swiss-Prot
other Location (Reliability: 2)
LUP2_ARATH
763
0
87515
Swiss-Prot
other Location (Reliability: 2)
LUP4_ARATH
759
0
86953
Swiss-Prot
other Location (Reliability: 2)
A0A396GEY8_MEDTR
344
0
39890
TrEMBL
other Location (Reliability: 5)
A0A396GDK3_MEDTR
176
0
19885
TrEMBL
other Location (Reliability: 5)
A0A396GI72_MEDTR
136
0
15651
TrEMBL
other Location (Reliability: 3)
A0A2P1M9J5_9ASTR
63
0
7690
TrEMBL
other Location (Reliability: 3)
A0A396I5Y8_MEDTR
203
0
23102
TrEMBL
other Location (Reliability: 1)
A0A396GCV0_MEDTR
85
0
10101
TrEMBL
other Location (Reliability: 2)
A0A2P1M9J3_9ASTR
63
0
7690
TrEMBL
other Location (Reliability: 3)
A0A5B6ZVS7_DAVIN
188
0
21447
TrEMBL
other Location (Reliability: 2)
A0A396GFQ4_MEDTR
190
0
21704
TrEMBL
other Location (Reliability: 2)
A0A396I0H4_MEDTR
509
0
58536
TrEMBL
Mitochondrion (Reliability: 1)
A0A2I7YUC2_CICIN
193
0
22893
TrEMBL
other Location (Reliability: 3)
A0A2P6RZF4_ROSCH
250
0
28707
TrEMBL
other Location (Reliability: 2)
A0A2P6RZG4_ROSCH
434
0
49668
TrEMBL
other Location (Reliability: 3)
A0A396GKK7_MEDTR
522
0
60129
TrEMBL
Mitochondrion (Reliability: 5)
A0A072UUU3_MEDTR
87
0
10325
TrEMBL
other Location (Reliability: 2)
A0A5B7CDF0_DAVIN
333
0
37603
TrEMBL
other Location (Reliability: 2)
A0A2P6RZY3_ROSCH
470
0
54196
TrEMBL
other Location (Reliability: 1)
A0A2P1M9I9_ACHMI
104
0
12779
TrEMBL
Mitochondrion (Reliability: 1)
A0A396GCT1_MEDTR
120
0
13983
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6RZI8_ROSCH
399
0
45704
TrEMBL
other Location (Reliability: 3)
A0A2P6RZH6_ROSCH
263
1
31181
TrEMBL
Mitochondrion (Reliability: 3)
A0A2P6RZX4_ROSCH
129
0
14696
TrEMBL
other Location (Reliability: 5)
A0A396GGH1_MEDTR
209
0
23415
TrEMBL
other Location (Reliability: 2)
A3E7Y8_9CARY
760
0
87521
TrEMBL
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
87500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C486A
mutant shows 46% activity compared to wild-type (100%), Km similar to wild-type, kcat decreased
C564A
mutant shows 1.6% activity compared to wild-type (100%), Km increased compared to wild-type, kcat highly decreased
F413A
site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme
F413H
site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme
F413M
site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme
F413S
site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme
F413T
site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme
F413V
site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme
F413W
site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme
F413Y
site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme
F474A
site-directed mutagenesis, the mutant produces significantly larger amounts of the bicyclic products and a decreased amount of beta-amyrin compared to wild-type. The mutant variant produces (9betaH)-polypoda-7,13,17,21-tetraen-3beta-ol and (9betaH)-polypoda-8(26),13,17,21-tetraen-3beta-ol, which are generated from a chair-boat folding conformation
F474G
site-directed mutagenesis, the mutant produces significantly larger amounts of the bicyclic products and a decreased amount of beta-amyrin compared to wild-type
F474L
site-directed mutagenesis, the mutant shows a significantly decreased production of bicyclic compounds, and in turn exhibits a higher production of beta-amyrin compared to wild-type
F474M
site-directed mutagenesis, the mutant shows a significantly decreased production of bicyclic compounds, and in turn exhibits a higher production of beta-amyrin compared to wild-type
F474V
site-directed mutagenesis, the mutant shows a significantly decreased production of bicyclic compounds, and in turn exhibits a higher production of beta-amyrin compared to wild-type
M729A
site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio
M729F
site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio
M729G
site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio
M729L
site-directed mutagenesis, the mutant shows an unaltered enzymatic activity compared to wild-type and altered roduct distribution ratio
M729N
site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio
M729V
site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio
M729W
site-directed mutagenesis, the mutant with the bulky substitution is inactive
V483A
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type, and affords monocyclic camelliol C
V483G
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type, and affords monocyclic camelliol C
V483I
site-directed mutagenesis, the mutant shows unaltered substrate specificity compared to wild-type, and affords beta-amyrin as major product
W534A
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534F
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534H
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534I
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534M
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534V
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534Y
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
H560Y
site-directed mutagenesis, the mutation of the key residue of GsAS1 to that of GsAS2 results in 38% increased catalytic efficiency compared to wild-type GsAS1
Y560F
site-directed mutagenesis, the mutation of the key residue of GsAS2 results in 71.15% reduced catalytic efficiency compared to wild-type GsAS2
Y560H
site-directed mutagenesis, the mutation of the key residue of GsAS2 results in 41.3% reduced catalytic efficiency compared to wild-type GsAS2
C262S
-
mutation in region responsible for product differentiation. Like wild-type, mutant produces beta-amyrin as sole product
M258I/W259L
-
mutation in region responsible for product differentiation. Mutant produces 40.5% beta-amyrin, 53.4% lupeol, 3.6% butyrospermol and 2.5% germanicol
W259L
-
mutation in region responsible for product differentiation. Mutant produces 30.3% beta-amyrin, 54.6% lupeol, 3.6% butyrospermol and 3.4% germanicol
Y261H
-
mutation in region responsible for product differentiation. Mutant produces 2.4% lupeol, 13.6% germanicol and 84% of dammara-18(E),21-dien-3beta-ol, dammara-18(Z),21-dien-3beta-ol and dammara-18(28),21-dien-3beta-ol
additional information
additional information
-
construction of chimeric proteins using beta-amyrin synthase from Panax ginseng and lupeol synthase from Arabidopsis thaliana. Chimera with N-terminal half of beta-amyrin synthase and C-terminal half of lupeol synthase produces beta-amyrin and lupeol in ratio 3:1. Chimera with only the second quarter of the N-terminus from beta-amyrin synthase, produces beta-amyrin and lupeol in a 4:1 ratio, while another chimera created by mixed PCR produces beta-amyrin and lupeol in a 1:4 ratio
additional information
-
functional expression in Saccharomyces cerevisiae results in production of beta-amyrin
additional information
functional expression in Saccharomyces cerevisiae mutant lacking lanosterol synthase activity results in production of beta-amyrin
additional information
functional expression in Saccharomyces cerevisiae results in production of beta-amyrin
additional information
-
functional expression in Saccharomyces cerevisiae results in production of beta-amyrin
additional information
functional expression in Pichia pastoris results in production of beta-amyrin
additional information
-
functional expression in Pichia pastoris results in production of beta-amyrin
additional information
quantities of oleanane-type, 17-epi-dammarane-type, and dammarane-type triterpenes in cultures of wild-type and mutant strains differ significantly, overview
additional information
RNAi-directed suppression of GsAS1 in Gentiana straminea decreasing oleonolic acid levels by 65.9%
additional information
RNAi-directed suppression of GsAS1 in Gentiana straminea decreasing oleonolic acid levels by 65.9%
additional information
-
RNAi-directed suppression of GsAS1 in Gentiana straminea decreasing oleonolic acid levels by 65.9%
additional information
RNAi-directed suppression of GsAS2 in Gentiana straminea decreasing oleonolic acid levels by 21.0%
additional information
RNAi-directed suppression of GsAS2 in Gentiana straminea decreasing oleonolic acid levels by 21.0%
additional information
-
RNAi-directed suppression of GsAS2 in Gentiana straminea decreasing oleonolic acid levels by 21.0%
additional information
-
functional expression in Saccharomyces cerevisiae mutant lacking lanosterol synthase activity results in production of beta-amyrin
additional information
-
functional expression in Saccharomyces cerevisiae results in production of beta-amyrin
additional information
-
functional expression in Saccharomyces cerevisiae mutant with disruption in oxidosqualene cyclase gene results in production of beta-amyrin
additional information
transient expression of MdOSC1 and MdOSC5 together with CYP716A175 confirms the ratio between the different triterpene backbones observed after transient expression of MdOSC1 and MDOSC5 alone, overview
additional information
-
transient expression of MdOSC1 and MdOSC5 together with CYP716A175 confirms the ratio between the different triterpene backbones observed after transient expression of MdOSC1 and MDOSC5 alone, overview
additional information
functional expression in Saccharomyces cerevisiae results in production of beta-amyrin
additional information
-
functional expression in Saccharomyces cerevisiae results in production of beta-amyrin
additional information
functional expression in Saccharomyces cerevisiae mutant lacking lanosterol synthase activity results in production of beta-amyrin
additional information
-
functional expression in Saccharomyces cerevisiae mutant lacking lanosterol synthase activity results in production of beta-amyrin
additional information
-
functional expression in Saccharomyces cerevisiae mutant lacking lanosterol synthase activity results in production of beta-amyrin
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional recombinant enzyme from Escherichia coli strain BL21
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a polyhistidine-tagged protein in Saccharomyces cerevisiae GIL77, which lacks the lanosterol synthase gene. Expression yield: 5-7 mg
expressed in a lanosterol synthase deficient Saccharomyces cerevisiae strain
expression in Saccharomyces cerevisae
expression in Saccharomyces cerevisiae
expression of PtBS in the triterpenoid synthase-deficient yeast mutant GIL77 leads to the production of beta-amyrin as sole product
-
functional expression of ObAS1 in Saccharomyces cerevisiae leads to the production of beta-amyrin
-
gene BAS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional recombinant expressison in Saccharomyces cerevisiae strain INVSc1 under the control of GAL1 promoter yielding beta-amyrin, beta-amyrin biosynthesis pathway engineered in yeast, overview. Metabolite identification by GC-MS/MS analysis
gene bAS, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression in Saccharomyces cerevisiae strain GIL77, real-time RT-PCR enzyme expression analysis, MS analysis metabolite identification
gene beta-AS, sequence comparisons and phylogenetic analysis
gene EsBAS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, transcriptomics analysis of plant leaves, quantitative PCR enzyme expression analysis, recombinant expression of teh enzyme in Saccharomyces cerevisiae ERG7-deficient mutant strain. Functional recombinant coexpression of the gene encoding hygromycin phosphotransferase (HPT), gene CYP716A244 (EC 1.14.14.126), and gene EsBAS in transgenic tobacco plant leaves via Agrobacterium tumefaciens strain GV3101-mediated transformation. Metabolite identification by GC/MS analysis
gene EtAS, sequence comparisons, recombinant expression of wild-type and mutant enzymes in yeast
gene GsAS1, gene GsAS1 possesses introns, phylogenetic tree, recombinant expression in Pichia pastoris under the control of the methanol-inducible AOX1 promoter, heterologously expressed GsAS1 generates less beta-amyrin in yeast than does GsAS2, constitutive overexpression of GsAS2 results in a 3fold increase in oleanolic acid accumulation, quantitative RT-PCR expression analysis
gene GsAS2, DNA and amino acid sequence determination and analysis, the gene GsAS2 lacks introns, phylogenetic tree, recombinant expression in Pichia pastoris under the control of the methanol-inducible AOX1 promoter, heterologously expressed GsAS2 generates more beta-amyrin in yeast than does GsAS1, constitutive overexpression of GsAS2 results in a 5.7fold increase in oleanolic acid accumulation, quantitative RT-PCR expression analysis
gene OSC1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis of the enzyme in apple fruits, functional recombinant expression in Nicotiana benthamiana via transformation by Agrobacterium tumefaciens strain GV3101 resulting in production of alpha-amyrin, beta-amyrin, and lupeol. MdOSC1 produces predominantly alpha-amyrin, beta-amyrin to a lesser extent, and small amounts of lupeol
gene PBA, DNA and amino acid sequence determination and analysis, functional recombinant expression in Escherichia coli strain BL21
recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain GIL77
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after 24 h of elicitation, beta-amyrin synthase transcripts are increased at 0.1, 1, and 2 mM of methyl jasmonate, and they are increased at 0.1 and 1 mM salicylic acid
CrAS is preferentially expressed in leaf epidermis, in younger leaves and during the earlier stages of seedling development in Catharanthus roseus
-
GsAS1 transcription is 9.8fold induced by methyl jasmonate (MeJA) treatment with increased oleanolic acid content, while salicylic acid has no effect
GsAS2 transcription is 12.2fold induced by methyl jasmonate (MeJA) treatment with increased oleanolic acid content, while salicylic acid has no effect
RNAi-directed suppression of GsAS1 in Gentiana straminea decreases oleonolic acid levels by 65.9%
RNAi-directed suppression of GsAS2 in Gentiana straminea decreases oleonolic acid levels by 21.0%
the enzyme is induced by methyl jasmonate (MeJA). The transcription of EsBAS is clearly enhanced at 12 and 24 h after MeJA treatment and reduced to the level of the control (without MeJA treatment) at 72 h after MeJA treatment
the enzyme is inducible by methyl jasmonate by 50fold in cell suspension cultures
-
the transcription of gene CbbAS is upregulated 4-24 h after treatment of seedlings with methyl jasmonate
the treatment with 0.1 mM methyl jasmonate yields greater accumulation of beta-amyrin as well as B-AS activity
the treatment with 0.1 mM methyl jasmonate yields greater accumulation of beta-amyrin as well as B-AS activity
-
the treatment with 0.1 mM methyl jasmonate yields greater accumulation of beta-amyrin as well as B-AS activity
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
engineering of the sterol pathway in Saccharomyces cerevisiae for production of beta-amyrin. Expression of enzyme gene plus manipulation of 3-hydroxy-3-methylglutaryl-CoA reductase and lanosterol synthase in Saccharomyces cerevisiae leads to levels of 6 mg beta-amyrin per l of culture
synthesis
-
use of enzyme for production of unnatural tetracyclic sesterterpenes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sawai, S.; Shindo, T.; Sato, S.; Kaneko, T.; Tabata, S.; Ayabe, S.; Aoki, T.
Functional and structural analysis of genes encoding oxidosqualene cyclases of Lotus japonicus
Plant Sci.
170
247-257
2006
Lotus japonicus
brenda
Hayashi, H.; Huang, P.; Kirakosyan, A.; Inoue, K.; Hiraoka, N.; Ikeshiro, Y.; Kushiro, T.; Shibuya, M.; Ebizuka, Y.
Cloning and characterization of a cDNA encoding beta-amyrin synthase involved in glycyrrhizin and soyasaponin biosyntheses in licorice
Biol. Pharm. Bull.
24
912-916
2001
Glycyrrhiza glabra
brenda
Zhang, H.; Shibuya, M.; Yokota, S.; Ebizuka, Y.
Oxidosqualene cyclases from cell suspension cultures of Betula platyphylla var. japonica: molecular evolution of oxidosqualene cyclases in higher plants
Biol. Pharm. Bull.
26
642-650
2003
Betula platyphylla (Q8W3Z1)
brenda
Kushiro, T.; Shibuya, M.; Ebizuka, Y.
beta-Amyrin synthase - cloning of oxidosqualene cyclase that catalyzes the formation of the most popular triterpene among higher plants
Eur. J. Biochem.
256
238-244
1998
Panax ginseng (O82140), Panax ginseng
brenda
Morita, M.; Shibuya, M.; Kushiro, T.; Masuda, K.; Ebizuka, Y.
Molecular cloning and functional expression of triterpene synthases from pea (Pisum sativum) new alpha-amyrin-producing enzyme is a multifunctional triterpene synthase
Eur. J. Biochem.
267
3453-3460
2000
Pisum sativum
brenda
Basyuni, M.; Oku, H.; Tsujimoto, E.; Kinjo, K.; Baba, S.; Takara, K.
Triterpene synthases from the Okinawan mangrove tribe, Rhizophoraceae
FEBS J.
274
5028-5042
2007
Bruguiera gymnorhiza (A8CDT2), Bruguiera gymnorhiza
brenda
Kirby, J.; Romanini, D.W.; Paradise, E.M.; Keasling, J.D.
Engineering triterpene production in Saccharomyces cerevisiae-beta-amyrin synthase from Artemisia annua
FEBS J.
275
1852-1859
2008
Artemisia annua
brenda
Kushiro, T.; Shibuya, M.; Ebizuka, Y.
Chimeric triterpene synthase. A possible model for multifunctional triterpene synthase
J. Am. Chem. Soc.
121
1208-1216
1999
Arabidopsis thaliana
-
brenda
Kushiro, T.; Shibuya, M.; Masuda, K.; Ebizuka, Y.
Mutational studies on triterpene synthases: engineering lupeol synthase into beta-amyrin synthase
J. Am. Chem. Soc.
122
6816-6824
2000
Panax ginseng
-
brenda
Abe, I.; Sakano, Y.; Tanaka, H.; Lou, W.; Noguchi, H.; Shibuya, M.; Ebizuka, Y.
Enzymatic cyclization of 22,23-dihydro-2,3-oxidosqualene into euph-7-en-3beta-ol and bacchar-12-en-3beta-ol by recombinant beta-amyrin synthase
J. Am. Chem. Soc.
126
3426-3427
2004
Pisum sativum
brenda
Abe, I.; Sakano, Y.; Sodeyama, M.; Tanaka, H.; Noguchi, H.; Shibuya, M.; Ebizuka, Y.
Mechanism and stereochemistry of enzymatic cyclization of 24,30-bisnor-2,3-oxidosqualene by recombinant beta-amyrin synthase
J. Am. Chem. Soc.
126
6880-6881
2004
Pisum sativum
brenda
Taton, M.; Ceruti, M.; Cattel, L.; Rahier, A.
Inhibition of higher plant 2,3-oxidosqualene cyclases by nitrogen-containing oxidosqualene analogs
Phytochemistry
43
75-81
1996
Pisum sativum
-
brenda
Kajikawa, M.; Yamato, K.T.; Fukuzawa, H.; Sakai, Y.; Uchida, H.; Ohyama, K.
Cloning and characterization of a cDNA encoding beta-amyrin synthase from petroleum plant Euphorbia tirucalli L.
Phytochemistry
66
1759-1766
2005
Euphorbia tirucalli (Q401R6), Euphorbia tirucalli
brenda
Iturbe-Ormaetxe, I.; Haralampidis, K.; Papadopoulou, K.; Osbourn, A.E.
Molecular cloning and characterization of triterpene synthases from Medicago truncatula and Lotus japonicus
Plant Mol. Biol.
51
731-743
2003
Medicago truncatula (Q84PE3), Medicago truncatula
brenda
Meesapyodsuk, D.; Balsevich, J.; Reed, D.W.; Covello, P.S.
Saponin biosynthesis in Saponaria vaccaria. cDNAs encoding beta-amyrin synthase and a triterpene carboxylic acid glucosyltransferase
Plant Physiol.
143
959-969
2007
Gypsophila vaccaria
brenda
Chung, E.; Cho, C.W.; Kim, K.Y.; Chung, J.; Kim, J.I.; Chung, Y.S.; Fukui, K.; Lee, J.H.
Molecular characterization of the GmAMS1 gene encoding beta -amyrin synthase in soybean plants
Russ. J. Plant Physiol.
54
518-523
2007
Glycine max (Q8H2B0)
-
brenda
Noma, H.; Tanaka, H.; Noguchi, H.; Shibuya, M.; Ebizuka, Y.; Abe, I.
Enzymatic formation of an unnatural novel tetracyclic sesterterpene by beta-amyrin synthase
Tetrahedron Lett.
45
8299-8301
2004
Pisum sativum
-
brenda
Confalonieri, M.; Cammareri, M.; Biazzi, E.; Pecchia, P.; Fevereiro, M.P.; Balestrazzi, A.; Tava, A.; Conicella, C.
Enhanced triterpene saponin biosynthesis and root nodulation in transgenic barrel medic (Medicago truncatula Gaertn.) expressing a novel beta-amyrin synthase (AsOXA1) gene
Plant Biotechnol. J.
7
172-182
2009
Aster sedifolius
brenda
Shibuya, M.; Katsube, Y.; Otsuka, M.; Zhang, H.; Tansakul, P.; Xiang, T.; Ebizuka, Y.
Identification of a product specific beta-amyrin synthase from Arabidopsis thaliana
Plant Physiol. Biochem.
47
26-30
2009
Arabidopsis thaliana (B6EXY6), Arabidopsis thaliana
brenda
Cammareri, M.; Consiglio, M.F.; Pecchia, P.; Corea, G.; Lanzotti, V.; Ibeas, J.I.; Tava, A.; Conicella, C.
Molecular characterization of ?-amyrin synthase from Aster sedifolius L. and triterpenoid saponin analysis
Plant Sci.
175
255-261
2008
Aster sedifolius (Q5D7Q8)
brenda
Brendolise, C.; Yauk, Y.K.; Eberhard, E.D.; Wang, M.; Chagne, D.; Andre, C.; Greenwood, D.R.; Beuning, L.L.
An unusual plant triterpene synthase with predominant alpha-amyrin-producing activity identified by characterizing oxidosqualene cyclases from Malus domestica
FEBS J.
278
2485-2499
2011
Malus domestica (C7SCX1), Malus domestica
brenda
Sawai, S.; Uchiyama, H.; Mizuno, S.; Aoki, T.; Akashi, T.; Ayabe, S.; Takahashi, T.
Molecular characterization of an oxidosqualene cyclase that yields shionone, a unique tetracyclic triterpene ketone of Aster tataricus
FEBS Lett.
585
1031-1036
2011
Aster tataricus
brenda
Yendo, A.C.; de Costa, F.; Gosmann, G.; Fett-Neto, A.G.
Production of plant bioactive triterpenoid saponins: elicitation strategies and target genes to improve yields
Mol. Biotechnol.
46
94-104
2010
Aster sedifolius, Centella asiatica, Gentiana straminea, Gypsophila vaccaria, Medicago truncatula, Panax ginseng
brenda
Takagi, K.; Nishizawa, K.; Hirose, A.; Kita, A.; Ishimoto, M.
Manipulation of saponin biosynthesis by RNA interference-mediated silencing of beta-amyrin synthase gene expression in soybean
Plant Cell Rep.
30
1835-1846
2011
Glycine max
brenda
Wang, Z.; Guhling, O.; Yao, R.; Li, F.; Yeats, T.H.; Rose, J.K.; Jetter, R.
Two oxidosqualene cyclases responsible for biosynthesis of tomato fruit cuticular triterpenoids
Plant Physiol.
155
540-552
2011
Solanum lycopersicum, Solanum lycopersicum (E7DN63)
brenda
Shabani, L.; Ehsanpour, A.; Esmaeili, A.
Assessment of squalene synthase and beta-amyrin synthase gene expression in licorice roots treated with methyl jasmonate and salicylic acid using real-time qPCR
Russ. J. Plant Physiol.
57
480-484
2010
Glycyrrhiza glabra (Q9MB42)
-
brenda
Ito, R.; Hashimoto, I.; Masukawa, Y.; Hoshino, T.
Effect of cation-pi interactions and steric bulk on the catalytic action of oxidosqualene cyclase: a case study of Phe728 of beta-amyrin synthase from Euphorbia tirucalli L
Chemistry
19
17150-17158
2013
Euphorbia tirucalli (Q401R6)
brenda
Ito, R.; Masukawa, Y.; Hoshino, T.
Purification, kinetics, inhibitors and CD for recombinant beta-amyrin synthase from Euphorbia tirucalli L and functional analysis of the DCTA motif, which is highly conserved among oxidosqualene cyclases
FEBS J.
280
1267-1280
2013
Euphorbia tirucalli (Q401R6)
brenda
Yu, F.; Thamm, A.M.; Reed, D.; Villa-Ruano, N.; Quesada, A.L.; Gloria, E.L.; Covello, P.; De Luca, V.
Functional characterization of amyrin synthase involved in ursolic acid biosynthesis in Catharanthus roseus leaf epidermis
Phytochemistry
91
122-127
2013
Catharanthus roseus
brenda
Jin, M.L.; Lee, D.Y.; Um, Y.; Lee, J.H.; Park, C.G.; Jetter, R.; Kim, O.T.
Isolation and characterization of an oxidosqualene cyclase gene encoding a beta-amyrin synthase involved in Polygala tenuifolia Willd. saponin biosynthesis
Plant Cell Rep.
33
511-519
2014
Polygala tenuifolia
brenda
Misra, R.C.; Maiti, P.; Chanotiya, C.S.; Shanker, K.; Ghosh, S.
Methyl jasmonate-elicited transcriptional responses and pentacyclic triterpene biosynthesis in sweet basil
Plant Physiol.
164
1028-1044
2014
Ocimum basilicum
brenda
Jo, H.J.; Han, J.Y.; Hwang, H.S.; Choi, Y.E.
beta-Amyrin synthase (EsBAS) and beta-amyrin 28-oxidase (CYP716A244) in oleanane-type triterpene saponin biosynthesis in Eleutherococcus senticosus
Phytochemistry
135
53-63
2017
Eleutherococcus senticosus (A0A1P8W708), Eleutherococcus senticosus
brenda
Hoshino, T.; Nakagawa, K.; Aiba, Y.; Itoh, D.; Nakada, C.; Masukawa, Y.
Euphorbia tirucalli beta-amyrin synthase critical roles of steric sizes at Val483 and Met729 and the CH-Pi interaction between Val483 and Trp534 for catalytic action
ChemBioChem
18
2145-2155
2017
Euphorbia tirucalli (Q401R6)
brenda
Liu, J.; Xie, H.; Chen, H.; Qian, Z.
Cloning, prokaryotic expression, and functional identification of beta-amyrin synthase cDNA of Psammosilene tunicoides
Chin. Tradit. Herbal Drugs
45
1456-1460
2014
Psammosilene tunicoides (A5A5F1)
-
brenda
Sun, R.; Liu, S.; Tang, Z.Z.; Zheng, T.R.; Wang, T.; Chen, H.; Li, C.L.; Wu, Q.
beta-Amyrin synthase from Conyza blinii expressed in Saccharomyces cerevisiae
FEBS open bio
7
1575-1585
2017
Eschenbachia blinii (A0A2P0VE73)
brenda
Um, Y.; Jin, M.; Lee, D.; Kim, C.; Hong, C.; Lee, Y.; Kim, O.
Functional characterization of the beta-amyrin synthase gene involved in platycoside biosynthesis in Platycodon grandiflorum
Hortic. Environ. Biotechnol.
58
613-619
2017
Platycodon grandiflorus (A0A1Z2WUZ5)
-
brenda
Andre, C.; Legay, S.; Deleruelle, A.; Nieuwenhuizen, N.; Punter, M.; Brendolise, C.; Cooney, J.; Lateur, M.; Hausman, J.; Larondelle, Y.; Laing, W.
Multifunctional oxidosqualene cyclases and cytochrome P450 involved in the biosynthesis of apple fruit triterpenic acids
New Phytol.
211
1279-1294
2016
Malus domestica (C7SCX0), Malus domestica
brenda
Ito, R.; Masukawa, Y.; Nakada, C.; Amari, K.; Nakano, C.; Hoshino, T.
beta-Amyrin synthase from Euphorbia tirucalli. Steric bulk, not the Pi-electrons of Phe, at position 474 has a key role in affording the correct folding of the substrate to complete the normal polycyclization cascade
Org. Biomol. Chem.
12
3836-3846
2014
Euphorbia tirucalli (Q401R6)
brenda
Ito, R.; Nakada, C.; Hoshino, T.
beta-Amyrin synthase from Euphorbia tirucalli L. functional analyses of the highly conserved aromatic residues Phe413, Tyr259 and Trp257 disclose the importance of the appropriate steric bulk, and cation-Pi and CH-Pi interactions for the efficient catalytic
Org. Biomol. Chem.
15
177-188
2017
Euphorbia tirucalli (Q401R6)
brenda
Ma, Y.; Yang, R.; Zhou, S.; Yin, Y.; Zhang, X.; Liu, Y.
beta-Amyrin synthase, one of the most important key enzymes for triterpene skeleton formation in higher plants
Pak. J. Bot.
50
231-243
2018
Artemisia annua (B1P7H3), Avena longiglumis (Q6IWA0), Barbarea vulgaris (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)
-
brenda
Liu, Y.; Zhao, Z.; Xue, Z.; Wang, L.; Cai, Y.; Wang, P.; Wei, T.; Gong, J.; Liu, Z.; Li, J.; Li, S.; Xiang, F.
An intronless beta-amyrin synthase gene is more efficient in oleanolic acid accumulation than its paralog in Gentiana straminea
Sci. Rep.
6
33364
2016
Gentiana straminea (A0A023U990), Gentiana straminea (C1K2M2), Gentiana straminea
brenda
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