EC Number   |
Protein Variants |
Reference |
|---|
   1.14.13.39 | C415A |
contains no heme, no bound tetrahydrobiopterin, unable to oxidize NADPH and to synthezise nitric oxide, unaltered ability to reduce cytochrome c |
440234 |
| 1.14.13.39 | C415H |
contains nearly no heme, no bound tetrahydrobiopterin, unable to oxidize NADPH and to synthezise nitric oxide, unaltered ability to reduce cytochrome c |
440234 |
| 1.14.13.39 | C563R |
interdomain electron transfer rate is similar to that of the wildtype |
725550 |
| 1.14.13.39 | D1393E |
normal composition, spectral properties and binding of cofactors, substrates and calmodulin, slower NADPH-dependent cytochrome c and ferricyanide reductase activity |
659330 |
| 1.14.13.39 | D1393N |
normal composition, spectral properties and binding of cofactors, substrates and calmodulin, slower NADPH-dependent cytochrome c and ferricyanide reductase activity |
659330 |
| 1.14.13.39 | D1393V |
normal composition, spectral properties and binding of cofactors, substrates and calmodulin, slower NADPH-dependent cytochrome c and ferricyanide reductase activity |
659330 |
| 1.14.13.39 | D597N/M336V |
mutant of nNOS, the Ki values for the nNOS double mutant increase for all inhibitors but the mutant still binds these inhibitors better than eNOS |
699457 |
| 1.14.13.39 | DELTAG810 |
deletion changes redox behaviour of mutant. In the early stage of flavin reduction, similar to the case of wild-type, the hydroquinone FADH2-FMN quickly converts to the disemiquinone and does not accumulate. Since more FADH2-FMN is generated and not consumed quickly enough, the decreased flavin absorption band of FADH2-FMN will blur the isosbestic point after 100 ms, most likely due to a slower two-electron reduction of FMN in the mutant |
725652 |
| 1.14.13.39 | E298D |
comparable to wild-type in heme and flavin content, in affinity to calmodulin and dimerization |
660022 |
| 1.14.13.39 | G2A |
the mutant is defective in activity and cellular localization |
700937 |
