EC Number   |
Protein Variants |
Reference |
|---|
   1.2.1.67 | C292A |
site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity |
-, 743803 |
| 1.2.1.67 | E199A |
site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+ the activity of E199A decreases to 78% of the wild-type activity |
-, 743803 |
| 1.2.1.67 | E258A |
site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme |
743803 |
| 1.2.1.67 | K180A |
site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity |
-, 743803 |
| 1.2.1.67 | more |
generation of a vdh deletion mutant, which partially loses its ability to grow on vanillin, indicating the presence of alternative VDH(s) in Corynebacterium glutamicum. When complemented with plasmid pXMJ19-vdhATCC13032, the growth ability of the mutant strain can be restored close to that of the wild type. The wild type, the DELTAvdhATCC13032 mutant and the complementary strain shows no difference when grown in p-cresol, cinnamyl aldehyde and syringaldehyde |
-, 743803 |
| 1.2.1.67 | more |
generation of desV disruption mutants |
743835 |
| 1.2.1.67 | more |
insertional inactivation of ligV negatively affects growth on vanillin (only 11% of the vanillin dehydrogenase activity of the wild-type strain), whereas growth on syringaldehyde, veratraldehyde and coniferyl aldehyde is almost the same as the wild-type activity. Dehydrogenase activity towards benzaldehyde, p-hydroxybenzaldehyde, protocatechualdehyde and m-anisaldehyde is decreased to 27%, 35%, 14% and 54%, respectively of the wild-type activity. Mutant retains ability to grow on ferulate |
-, 691363 |
| 1.2.1.67 | more |
insertional mutagenesis of the vanillin dehydrogenase gene renders the strain unable to grow on vanillin or ferulic acid |
-, 673380 |
| 1.2.1.67 | more |
metabolic engineering of the actinomycete Amycolatopsis sp. strain ATCC 39116 towards enhanced production of natural vanillin. Degradation of vanillin is decreased by more than 90% through deletion of the vdh gene, which codes for the central vanillin catabolism enzyme, vanillin dehydrogenase. This mutation results in improvement of the final concentration of vanillin by more than 2.2 g/liter, with a molar yield of 80.9%. Further improvement is achieved with constitutive expression of the vanillin anabolism genes ech and fcs, coding for the enzymes feruloyl-coenzyme A (CoA) synthetase (fcs) and enoyl-CoA hydratase/aldolase (ech). The transcription of both genes is shown to be induced by ferulic acid, which explains the unwanted adaptation phase in the fermentation process before vanillin is efficiently produced by the wild-type cells. Through the constitutive and enhanced expression of the two genes, the adaptation phase is eliminated and a final vanillin concentration of 19.3 g/liter, with a molar yield of 94.9%, is obtained. Moreover, an even higher final vanillin concentration of 22.3 g/liter is achieved, at the expense of a lower molar yield, by using an improved feeding strategy. The vanillin is produced almost without by-products, with a molar yield that nearly approaches the theoretical maximum. Generation of a vdh deletion mutant with replacement of vdh gene by kanamycin resistance gene, deletion of vdh via homologous recombination |
-, 741700 |
| 1.2.1.67 | N157A |
site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity |
-, 743803 |
