5.4.99.39 C262S mutation in region responsible for product differentiation. Like wild-type, mutant produces beta-amyrin as sole product 683581 5.4.99.39 C486A mutant shows 46% activity compared to wild-type (100%), Km similar to wild-type, kcat decreased 729707 5.4.99.39 C564A mutant shows 1.6% activity compared to wild-type (100%), Km increased compared to wild-type, kcat highly decreased 729707 5.4.99.39 D485E mutant shows no activity 729707 5.4.99.39 D485N mutant shows no activity 729707 5.4.99.39 F413A site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme 748812 5.4.99.39 F413H site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme 748812 5.4.99.39 F413M site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme 748812 5.4.99.39 F413S site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme 748812 5.4.99.39 F413T site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme 748812 5.4.99.39 F413V site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme 748812 5.4.99.39 F413W site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme 748812 5.4.99.39 F413Y site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme 748812 5.4.99.39 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 748805 5.4.99.39 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 748805 5.4.99.39 F474H site-directed mutagenesis 748805 5.4.99.39 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 748805 5.4.99.39 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 748805 5.4.99.39 F474T site-directed mutagenesis 748805 5.4.99.39 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 748805 5.4.99.39 F474W site-directed mutagenesis 748805 5.4.99.39 F474Y site-directed mutagenesis 748805 5.4.99.39 F728A highly reduced activity compared to wild-type 729601 5.4.99.39 F728H highly reduced activity compared to wild-type 729601 5.4.99.39 F728I highly reduced activity compared to wild-type 729601 5.4.99.39 F728M highly reduced activity compared to wild-type 729601 5.4.99.39 F728W highly reduced activity compared to wild-type 729601 5.4.99.39 F728Y activity comparable to wild-type 729601 5.4.99.39 G257W site-directed mutagenesis 749323 5.4.99.39 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 749323 5.4.99.39 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 683581 5.4.99.39 M729A site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio 747546 5.4.99.39 M729F site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio 747546 5.4.99.39 M729G site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio 747546 5.4.99.39 M729L site-directed mutagenesis, the mutant shows an unaltered enzymatic activity compared to wild-type and altered roduct distribution ratio 747546 5.4.99.39 M729N site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio 747546 5.4.99.39 M729V site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio 747546 5.4.99.39 M729W site-directed mutagenesis, the mutant with the bulky substitution is inactive 747546 5.4.99.39 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 683580 5.4.99.39 additional information functional expression in Pichia pastoris results in production of beta-amyrin 683972 5.4.99.39 additional information functional expression in Saccharomyces cerevisiae mutant lacking lanosterol synthase activity results in production of beta-amyrin 683214, 683215, 683420, 683422 5.4.99.39 additional information functional expression in Saccharomyces cerevisiae mutant with disruption in oxidosqualene cyclase gene results in production of beta-amyrin 682450 5.4.99.39 additional information functional expression in Saccharomyces cerevisiae results in production of beta-amyrin 683462, 683463, 683984, 683985 5.4.99.39 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 748812 5.4.99.39 additional information RNAi-directed suppression of GsAS1 in Gentiana straminea decreasing oleonolic acid levels by 65.9% 749323 5.4.99.39 additional information RNAi-directed suppression of GsAS2 in Gentiana straminea decreasing oleonolic acid levels by 21.0% 749323 5.4.99.39 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 748772 5.4.99.39 V483A site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type, and affords monocyclic camelliol C 747546 5.4.99.39 V483F site-directed mutagenesis 747546 5.4.99.39 V483G site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type, and affords monocyclic camelliol C 747546 5.4.99.39 V483I site-directed mutagenesis, the mutant shows unaltered substrate specificity compared to wild-type, and affords beta-amyrin as major product 747546 5.4.99.39 W259L mutation in region responsible for product differentiation. Mutant produces 30.3% beta-amyrin, 54.6% lupeol, 3.6% butyrospermol and 3.4% germanicol 683581 5.4.99.39 W534A site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product 747546 5.4.99.39 W534F site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product 747546 5.4.99.39 W534H site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product 747546 5.4.99.39 W534I site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product 747546 5.4.99.39 W534M site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product 747546 5.4.99.39 W534V site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product 747546 5.4.99.39 W534Y site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product 747546 5.4.99.39 Y259A site-directed mutagenesis, functional analysis 748812 5.4.99.39 Y259F site-directed mutagenesis, functional analysis 748812 5.4.99.39 Y259H site-directed mutagenesis, functional analysis 748812 5.4.99.39 Y259L site-directed mutagenesis, functional analysis 748812 5.4.99.39 Y259V site-directed mutagenesis, functional analysis 748812 5.4.99.39 Y259W site-directed mutagenesis, functional analysis 748812 5.4.99.39 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 683581 5.4.99.39 Y560F site-directed mutagenesis, the mutation of the key residue of GsAS2 results in 71.15% reduced catalytic efficiency compared to wild-type GsAS2 749323 5.4.99.39 Y560H site-directed mutagenesis, the mutation of the key residue of GsAS2 results in 41.3% reduced catalytic efficiency compared to wild-type GsAS2 749323