5.4.99.39: beta-amyrin synthase
This is an abbreviated version!
For detailed information about beta-amyrin synthase, go to the full flat file.
Word Map on EC 5.4.99.39
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5.4.99.39
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triterpene
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oxidosqualene
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saponin
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triterpenoids
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lupeol
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cyclases
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glycyrrhiza
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cycloartenol
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oleanolic
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lanosterol
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uralensis
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oleanane-type
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2,3-oxidosqualene
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oleanane
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dammarenediol
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soyasapogenol
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synthesis
- 5.4.99.39
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triterpene
- oxidosqualene
- saponin
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triterpenoids
- lupeol
- cyclases
- glycyrrhiza
- cycloartenol
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oleanolic
- lanosterol
- uralensis
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oleanane-type
- 2,3-oxidosqualene
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oleanane
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dammarenediol
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soyasapogenol
- synthesis
Reaction
Synonyms
AMS1, amyrin synthase, B-AS, bAS, BAS-like 2, BAS1, BAS2, beta-amyrin cyclase, beta-amyrin synthase, beta-AS, betaAS, BPY, CbbAS, CrAS, EsBAS, EtAS, GmAMS1, GsAS1, GsAS2, MdOSC1, MtAMY1, multifunctional OSC, ObAS1, OPSC 1, OSC, OSC1, OSC2, OXA1, Oxidosqualene cyclase, PBA, PlgOSC1, PNY, PSY, PtBS, SITTS1, SlTTS1, SvBS
ECTree
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Engineering
Engineering on EC 5.4.99.39 - beta-amyrin synthase
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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
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mutation in region responsible for product differentiation. Like wild-type, mutant produces beta-amyrin as sole product
M258I/W259L
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mutation in region responsible for product differentiation. Mutant produces 40.5% beta-amyrin, 53.4% lupeol, 3.6% butyrospermol and 2.5% germanicol
W259L
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mutation in region responsible for product differentiation. Mutant produces 30.3% beta-amyrin, 54.6% lupeol, 3.6% butyrospermol and 3.4% germanicol
Y261H
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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
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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
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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
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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
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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%
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RNAi-directed suppression of GsAS1 in Gentiana straminea decreasing oleonolic acid levels by 65.9%
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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
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RNAi-directed suppression of GsAS2 in Gentiana straminea decreasing oleonolic acid levels by 21.0%
additional information
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functional expression in Saccharomyces cerevisiae mutant lacking lanosterol synthase activity results in production of beta-amyrin
additional information
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functional expression in Saccharomyces cerevisiae results in production of beta-amyrin
additional information
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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
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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
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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
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functional expression in Saccharomyces cerevisiae mutant lacking lanosterol synthase activity results in production of beta-amyrin
additional information
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functional expression in Saccharomyces cerevisiae mutant lacking lanosterol synthase activity results in production of beta-amyrin