EC Number |
Protein Variants |
Reference |
---|
1.1.1.159 | C260S |
the mutant shows 2fold higher specific activity as compared to the wild type enzyme |
-, 760413 |
1.1.1.159 | K163I |
5.25% activity of wild-type activity |
286083 |
1.1.1.159 | K163R |
63.7% activity of wild-type activity |
286083 |
1.1.1.159 | L26M |
the mutant shows 1.26fold higher specific activity as compared to the wild type enzyme |
-, 760413 |
1.1.1.159 | more |
construction of a 7alpha -HSD knockout mutant that shows decreased degradation of testosterone, estradiol and cholesterol compared to the wild-type |
-, 740971 |
1.1.1.159 | more |
development and evaluation of a selected multi-step reaction system for the synthesis of ursodeoxycholic acid, separation of each step by isolation of the intermediates using ultrafiltration membranes, overview |
740787 |
1.1.1.159 | more |
generation of a C-terminaly truncation enzyme mutant. When 2 and 6 amino acids of C-terminal are removed, the catalytic efficiency of Ca7alpha-HSDH remains 19.1% and 2.5%, respectively. No activity remains after deletion of 8, 14 and 17 amino acids |
741371 |
1.1.1.159 | Q255L |
the mutant shows 4.2fold higher specific activity as compared to the wild type enzyme |
-, 760413 |
1.1.1.159 | Q255L/C260S |
the mutant shows 6.5fold higher specific activity and exhibits 10fold higher and 14fold higher catalytic efficiencies toward chenodeoxycholic acid and NADP+, respectively, as compared to the wild type enzyme. The mutant also displays significantly enhanced tolerance in the presence of high concentrations of substrate compared to the wild type |
-, 760413 |
1.1.1.159 | Q255R |
the mutant shows 1.3fold higher specific activity as compared to the wild type enzyme |
-, 760413 |