Pub. Date : 2002 Apr 9
PMID : 11926825
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The slow phase (1/tau = 55 +/- 2 s(-1)) observed in the absorption transients obtained with CPR reduced at the two-electron level with NADPH reports on internal electron transfer: FAD(sq)-FMN(sq) --> FAD(ox)-FMN(hq). | NADP | formin 1 | Homo sapiens |
| 2 | The slow phase (1/tau = 55 +/- 2 s(-1)) observed in the absorption transients obtained with CPR reduced at the two-electron level with NADPH reports on internal electron transfer: FAD(sq)-FMN(sq) --> FAD(ox)-FMN(hq). | NADP | formin 1 | Homo sapiens |
| 3 | Temperature perturbation experiments with CPR reduced with 10-fold molar excess of NADPH produce monophasic absorption transients (1/tau = 20 +/- 0.2 s(-1)) reporting on internal electron transfer: FAD(sq)-FMN(hq) --> FAD(hq)-FMN(sq). | NADP | formin 1 | Homo sapiens |
| 4 | Temperature perturbation experiments with CPR reduced with 10-fold molar excess of NADPH produce monophasic absorption transients (1/tau = 20 +/- 0.2 s(-1)) reporting on internal electron transfer: FAD(sq)-FMN(hq) --> FAD(hq)-FMN(sq). | NADP | formin 1 | Homo sapiens |
| 5 | Replacement of Trp-676 with His-676 reduces approximately 2-fold the observed rate of internal electron transfer in two-electron-reduced enzyme, whereas the observed rate for FAD(sq)-FMN(hq) --> FAD(hq)-FMN(sq) transfer is increased approximately 13-fold in the W676H mutant reduced with a 10-fold molar excess of NADPH. | NADP | formin 1 | Homo sapiens |