EC Number   |
Protein Variants |
Reference |
|---|
   1.6.5.4 | C117A |
the binding affinity of NADH in the mutant MDAR is lower than that of wild type MDAR as indicated by about 1.5-3fold increase of the Km value for NADH, the mutant is less thermo-stable than the wild type enzyme |
712176 |
| 1.6.5.4 | C117S |
the binding affinity of NADH in the mutant MDAR is lower than that of wild type MDAR as indicated by about 1.5-3fold increase of the Km value for NADH, the mutant is less thermo-stable than the wild type enzyme |
712176 |
| 1.6.5.4 | C69A |
mutation has a negligible effect on enzyme activity under standard reaction conditions. The C69A mutant is more resistant to the inhibitory effects of beta-chloromercuribenzoate than the wild type PpMDHAR2 protein |
689672 |
| 1.6.5.4 | C70A |
about 105% of wild-type activity |
743819 |
| 1.6.5.4 | E196A |
residue E196 forms a hydrogen bond to the O2B molecule in the adenosine ring of NAD. Mutation reduces catalytic activity. Mutant E196A has only about 3 times higher affinity for NAD than that for NADP, i.e. 16fold increase in affinity for NADP compared to the wild-type |
743819 |
| 1.6.5.4 | G72N |
about 70% of wild-type activity |
743819 |
| 1.6.5.4 | more |
overexpression of MDHAR enhanced tolerance to osmotic stress |
-, 726105 |
| 1.6.5.4 | more |
transgenic lines overexpressing MDHAR show a decrease in ascorbate levels in leaves, whereas lines where MDHAR is silenced show an increase in these levels in both fruits and leave. In all three lines where MDHAR3 is silenced (MDS lines), a significant decrease in overall MDHAR activity is observed in leavess. Transcript levels of MDHAR1 (SGN-U584073) and MDHAR2 (SGN-U583672) remain unaffected by modification of MDHAR3 |
-, 726130 |
| 1.6.5.4 | R320A |
about 20% of wild-type activity |
743819 |
| 1.6.5.4 | Y345F |
mutant is a functional enzyme resistant to inhibition by 0.5 mM and 5.0 mM peroxynitrite |
743001 |
