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F82I
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continues to catalyze strongly both the first and second C1-transfer activities and generates product sets similar to the control
F82L
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first C1-transfer activity is relatively unaffected, loss of the second C1-transfer activity
F85L
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first C1-transfer activity is relatively unaffected, loss of the second C1-transfer activity
F91L
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first C1-transfer activity reduced from the control activity, loss of the second C1-transfer activity
F93L
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first C1-transfer activity reduced from the control activity, loss of the second C1-transfer activity
W87L
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first and second C1-transfer activities are greatly reduced from the control activities
Y81F
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site-directed mutagenesis, the mutation causes a preferential change in affinity for DELTA24-sterols that affords alter partitioning in the direction of 24-ethyl(idene) product formation
Y81L
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site-directed mutagenesis, the mutation causes a preferential change in affinity for DELTA24-sterols that affords alter partitioning in the direction of 24-ethyl(idene) product formation
Y88F
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site-directed mutagenesis, the mutation causes a 10% loss in activity compared to the wild-type enzyme
Y88L
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site-directed mutagenesis, the mutation causes a 50% loss in activity compared to the wild-type enzyme
Y81F
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site-directed mutagenesis, the mutation causes a preferential change in affinity for DELTA24-sterols that affords alter partitioning in the direction of 24-ethyl(idene) product formation
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Y81L
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site-directed mutagenesis, the mutation causes a preferential change in affinity for DELTA24-sterols that affords alter partitioning in the direction of 24-ethyl(idene) product formation
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Y88F
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site-directed mutagenesis, the mutation causes a 10% loss in activity compared to the wild-type enzyme
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Y88L
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site-directed mutagenesis, the mutation causes a 50% loss in activity compared to the wild-type enzyme
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Y83F
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first C1-transfer activity is relatively unaffected whereas the second C1-transfer activity generates different amounts of product compared to the control
Y83F
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Km and kcat, of wild-type enzyme and mutant enzyme are similar for cycloartenol as substrate
Y83L
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first C1-transfer activity greatly reduced from the control activity, loss of the second C1-transfer activity
Y83L
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Km and kcat, of wild-type enzyme and mutant enzyme are similar for cycloartenol as substrate
additional information
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overexpression of SMT2 gene in a mutant strain leads to an accumulation of sitosterol and to an altered phenotype, some of the changes can be restored by brassinosteroid treatment, some cannot, sterol profile of wild-type and mutant plants
additional information
construction of SMT1-deficient mutants with altered phenotype, reduced fertility and root growth defects, transgenic plant seedlings are sensitive against brassinosteroids and transfection with a genomic clone or a SMT1 cDNA can complement the mutants
additional information
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GhSMT2-1 and GhSMT2-2 have high homology with the SMT2 from Arabidopsis thaliana and Nicotiana tabacum. The typical conserved structures characterized by the sterol C-24 methyltransferase, such as region I (LDVGCGVGGPMRAI), region II (IEATCHAP), and region III (YEWGWGQSFHF), are present in both deduced proteins