EC Number   |
Protein Variants |
Reference |
|---|
    1.2.1.13 | C349S/C358S |
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+ |
656096 |
| 1.2.1.13 | c358S |
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+ |
656096 |
| 1.2.1.13 | D351N |
the mutation only marginally affects the redox sensitivity |
689747 |
| 1.2.1.13 | E356Q |
the mutation only marginally affects the redox sensitivity |
689747 |
| 1.2.1.13 | E356Q/E357Q |
complete redox insensitivity is achieved in the double mutant |
689747 |
| 1.2.1.13 | E357Q |
the mutation only marginally affects the redox sensitivity |
689747 |
| 1.2.1.13 | K128A |
Km-value for NADPH is nearly identical to wild-type value, turnover-number for NADPH is decreased about 2fold. Km-value for NADH is increased 2.1fold compared to wild-type enzyme, turnover-number for NADH is decreased 2.6fold |
655492 |
| 1.2.1.13 | K128E |
Km-value for NADPH is about 80% of the wild-type value, turnover-number for NADPH is decreased 2.7fold. Km-value for NADH is increased 2.3fold compared to wild-type enzyme, turnover-number for NADH is decreased 1.9fold |
655492 |
| 1.2.1.13 | K225A |
K225 is critical for binding of GAPDH to Siah1, an ubiquitin-E3-ligase, eliciting the translocation of GAPDH to the nucleus |
676851 |
| 1.2.1.13 | more |
construction of hybrid enzymes between the glyceraldehyde-3-phosphate dehydrogenases from the mesophilic Methanobacterium bryantii and the thermophilic Methanothermus fervidus |
287989 |
