EC Number   |
Protein Variants |
Reference |
|---|
   2.7.1.23 | D45N |
only minor changes, its active site is similar to that of the wild-type enzyme with the ligand present in the same conformation. The asparagine adopts the same buried conformation as the aspartate but does not form any hydrogen bond with NAD. Mutation results in a 10fold decrease in activity |
693014 |
| 2.7.1.23 | G183R |
decrease both in NAD+ kinase and NADH kinase activity |
662376 |
| 2.7.1.23 | G190A |
no enzymic activity |
661147 |
| 2.7.1.23 | G198A |
no enzymic activity |
661147 |
| 2.7.1.23 | G207A |
no enzymic activity |
661147 |
| 2.7.1.23 | G208A |
decrease in Vmax-value |
661147 |
| 2.7.1.23 | H223E |
is twice less active than the wild-type on the biologically relevant substrate NAD. In contrast, its activity toward di-(5'-thioadenosine) is increased 2fold |
693014 |
| 2.7.1.23 | L192A |
no enzymic activity |
661147 |
| 2.7.1.23 | more |
enzyme knockout mutant, growth inhibition and smaller rosette leaves than wild-type, with pale yellow colour. Mutant plant show a reduced chlorophyll content, and hypersensitivity to environmental stress such as UV-B, drought, heat shock and salinity |
663106 |
| 2.7.1.23 | more |
mutant for NadF is lethal |
691390 |
