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I368A
the mutant produces ent-pimara-8(14),15-diene, ent-kaur-16-ene, 8alpha-hydroxy-ent-pimara-15-ene, and ent-pimara-7,15-diene from ent-copalyl diphosphate
I368S
the mutant produces ent-pimara-8(14),15-diene and 8alpha-hydroxy-ent-pimara-15-ene from ent-copalyl diphosphate
I368T
the mutant produces ent-pimara-8(14),15-diene from ent-copalyl diphosphate
I368V
the mutant produces ent-kaur-16-ene from ent-copalyl diphosphate
I638A
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces a mixture of four products, pedominantly ent-pimara-8(14),15-diene, and a small amount of the double bond isomer ent-pimara-7,15-diene, and variable amounts of ent-kaur-16-ene, as well as substantial amounts of 8a-hydroxy-ent-pimar-15-ene
I638S
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces a mixture of four products, pedominantly ent-pimara-8(14),15-diene, and a small amount of the double bond isomer ent-pimara-7,15-diene, and variable amounts of ent-kaur-16-ene, as well as substantial amounts of 8a-hydroxy-ent-pimar-15-ene
I638T
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces a mixture of four products, pedominantly ent-pimara-8(14),15-diene, and small amounts of the double bond isomer ent-pimara-7,15-diene and 8a-hydroxy-ent-pimar-15-ene, and variable amounts of ent-kaur-16-ene
I638V
site-directed mutagenesis, the mutant shows unaltered product spectrum compared to the wild-type enzyme and produces just ent-kaur-16-ene
D75A
site-directed mutagenesis
D75C
site-directed mutagenesis, mutant crystal structure determination and analysis
D79C
site-directed mutagenesis
R204A
site-directed mutagenesis
D75A
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site-directed mutagenesis
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D75C
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site-directed mutagenesis, mutant crystal structure determination and analysis
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D79C
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site-directed mutagenesis
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R204A
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site-directed mutagenesis
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I664A
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces significant amounts of 8alpha-hydroxy-ent-pimara-15-ene generated by addition of water prior to deprotonation, it also produces ent-copalol, the dephosphorylated derivative of ent-copalyl diphosphate
I664S
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces significant amounts of 8alpha-hydroxy-ent-pimara-15-ene generated by addition of water prior to deprotonation, it also produces ent-copalol, the dephosphorylated derivative of ent-copalyl diphosphate
I664T
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces high amounts of ent-pimara-8(14),15-diene, it also produces ent-copalol, the dephosphorylated derivative of ent-copalyl diphosphate
I664V
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces ent-isokaurene and ent-copalol, the dephosphorylated derivative of ent-copalyl diphosphate
A710C
no change in reaction product profile compared to wild-type
A710F
mutant converts geranylgeranyl diphosphate to ent-kaurene as the sole product
A710G
no change in reaction product profile compared to wild-type
A710M
mutant converted geranylgeranyl diphosphate to ent-kaurene as the sole product
A710N
no change in reaction product profile compared to wild-type
A710S
no change in reaction product profile compared to wild-type
D635A/D636A
mutation of the DDYFD motif in the kaurene synthase domain
I619A
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme
A676T
site-directed mutagenesis of isozyme RcKSL2, mutation of the catalytically important residue results in 60fold increased product amount composed of essentially the same mix of ent-trachylobane and ent-kaurene as observed for the wild-type enzyme
H212A
the mutant shows altered substrate specificity compared to wild-type, the single histidine to alanine mutation converts FfCPS/KS into a bifunctional ent-13-epi-manoyl oxide synthase
H212A
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the mutant shows altered substrate specificity compared to wild-type, the single histidine to alanine mutation converts FfCPS/KS into a bifunctional ent-13-epi-manoyl oxide synthase
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I645T
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces almost entirely ent-pimara-8(14),15-diene, reaction of EC 4.2.3.30
I645T
the mutant produces ent-pimara-8(14),15-diene from ent-copalyl diphosphate
H302A
the mutant efficiently produces ent-13-epi-manoyl oxide from geranylgeranyl diphosphate
H302A
the mutant shows altered substrate specificity compared to wild-type, the single histidine to alanine mutation converts PpCPS/KS into a bifunctional ent-13-epi-manoyl oxide synthase
I741T
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces almost entirely ent-pimara-8(14),15-diene, reaction of EC 4.2.3.30
I741T
the mutant produces ent-pimara-8(14),15-diene from ent-copalyl diphosphate
additional information
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construction of transgenic Arabidopsis thaliana plants, using the Agrobacterium tumefaciens infection system, overexpressing KS leads to increased ent-kaurene production but not to an increase in bioactive gibberellins, no altered morphology or phenotype compared to wild-type plants
additional information
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construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-86 and Pp131-504 /Js512-886 and produce only ent-kaurene. Chimeric cyclases, Pp131-622 /Js630-886 and Pp131-714 /Js722-886, lose all enzymic activity
additional information
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construction of transgenic rice mutants expressing mutated KS-like genes, the mutant plants show reduced enzyme activity, phenotype analysis and effects on gibberellin metabolism, overview
additional information
several N- and C-terminal truncated enzymes produced, all found to be inactive
additional information
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several N- and C-terminal truncated enzymes produced, all found to be inactive
additional information
construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-886 and Pp131-504 /Js512-886 and produce only ent-kaurene. Chimeric cyclases, Pp131-622 /Js630-886 and Pp131-714 /Js722-886, lose all enzymic activity
additional information
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construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-886 and Pp131-504 /Js512-886 and produce only ent-kaurene. Chimeric cyclases, Pp131-622 /Js630-886 and Pp131-714 /Js722-886, lose all enzymic activity
additional information
generation of a Physcomitrella patens CPS/KS (PpCPS/KS)-gene disruption mutant strain A74, comparisons of photomorphogenesis of protonema in the wild-type and the A74 enzyme mutant, phenotype, detailed overview
additional information
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generation of a Physcomitrella patens CPS/KS (PpCPS/KS)-gene disruption mutant strain A74, comparisons of photomorphogenesis of protonema in the wild-type and the A74 enzyme mutant, phenotype, detailed overview
additional information
construction of a SmKS-SmCPSent fusion enzyme (CPSent is ent-copalyl diphosphate synthase, EC 5.5.1.13), which improves the ent-kaurene precursor supply in transformed Saccharomyces cerevisiae strain SGH5 (BY-T20/pESC-Trp::SmKS-SmCPSent/SmKO + pESC-Leu::SmCPR1)
additional information
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construction of a SmKS-SmCPSent fusion enzyme (CPSent is ent-copalyl diphosphate synthase, EC 5.5.1.13), which improves the ent-kaurene precursor supply in transformed Saccharomyces cerevisiae strain SGH5 (BY-T20/pESC-Trp::SmKS-SmCPSent/SmKO + pESC-Leu::SmCPR1)
additional information
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a synthetic ent-kaurene module, expressing Stevia rebaudiana CPPS and KS, and Rhodobacter sphaeroides GGPPS (crtE gene), is constructed for ent-kaurene production in diverse Escherichia coli strains, best in strain MG1655, method optimization, several crtE genes from Rhodobacter species are validated, overview
additional information
a synthetic ent-kaurene module, expressing Stevia rebaudiana CPPS and KS, and Rhodobacter sphaeroides GGPPS (crtE gene), is constructed for ent-kaurene production in diverse Escherichia coli strains, best in strain MG1655, method optimization, several crtE genes from Rhodobacter species are validated, overview