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Results 1 - 10 of 16 > >>
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EC Number Protein Variants Commentary Reference
Display the reaction diagram Show all sequences 1.14.99.14A106T/A395I site-directed mutagenesis, the mutant shows 14.3fold higher regioselectivity for 11alpha-hydroxylation and 39.3fold increased catalytic efficiency compared to the wild-type enzyme 727305
Display the reaction diagram Show all sequences 1.14.99.14A106T/A395I/R409L site-directed mutagenesis, the mutant shows 12.6fold higher regioselectivity for 11alpha-hydroxylation and 108fold increased catalytic efficiency compared to the wild-type enzyme 727305
Display the reaction diagram Show all sequences 1.14.99.14A106T/A395W/G379K/R409L site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme 727305
Display the reaction diagram Show all sequences 1.14.99.14A243V/A395I site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme 727305
Display the reaction diagram Show all sequences 1.14.99.14A243V/A395W/G397K site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme 727305
Display the reaction diagram Show all sequences 1.14.99.14A395I site-directed mutagenesis, the mutant shows 8.9fold higher 11alpha-hydroxylation activity compared to the wild-type enzyme 727305
Display the reaction diagram Show all sequences 1.14.99.14A395W/G397K site-directed mutagenesis, the mutant shows 11.5fold higher 11alpha-hydroxylation activity compared to the wild-type enzyme 727305
Display the reaction diagram Show all sequences 1.14.99.14D217V/A395I site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme 727305
Display the reaction diagram Show all sequences 1.14.99.14M155I/F165L/A395I site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme 727305
Display the reaction diagram Show all sequences 1.14.99.14more direction of the regioselectivity of the enzyme towards hydroxylation at position 11 in the C ring of the steroid through a combination of saturation mutagenesis and rational site-directed mutagenesis, with aid of data from a homology model of CYP106A2 containing docked progesterone, together with site-directed mutagenesis of active site residues. Distributions of amounts of monohydroxylated progesterone products (15beta-,11alpha-, 9alpha-, and 6beta-hydroxyprogesterone) in vivo of wild-type and mutant enzymes, overview 727305
Results 1 - 10 of 16 > >>
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