EC Number   |
Protein Variants |
Reference |
|---|
   1.4.3.12 | F317A |
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 30% of the wild-type value |
-, 765258 |
| 1.4.3.12 | F327A |
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 179% of the wild-type value |
765258 |
| 1.4.3.12 | G202A |
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 298% of the wild-type value |
-, 765258 |
| 1.4.3.12 | I173A |
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 67% of the wild-type value |
765258 |
| 1.4.3.12 | I201A |
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 24% of the wild-type value |
-, 765258 |
| 1.4.3.12 | L199A |
the mutant shows generally lower activity (decrease of 15-97%) towards most substrates compared to wild type enzyme with the exception of the larger substrates, such as cyclooctanamine and bicyclic (S)-1-aminotetraline |
-, 724095 |
| 1.4.3.12 | L199F |
2.1fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme |
-, 764488 |
| 1.4.3.12 | L199F |
the mutant is more active than the wild type enzyme toward the primary amines |
743810 |
| 1.4.3.12 | L199I |
the mutant is more active than the wild type enzyme toward the primary amines |
743810 |
| 1.4.3.12 | L199T |
the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme |
-, 741481 |
