Pub. Date : 2002 Jun 21
PMID : 12079352
14 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthesis. | NADP | ferredoxin reductase | Homo sapiens |
| 2 | The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthesis. | NADP | ferredoxin reductase | Homo sapiens |
| 3 | The three-dimensional structure of FNR presents two distinct domains, one for binding of the FAD prosthetic group and the other for NADP+ binding. | NADP | ferredoxin reductase | Homo sapiens |
| 4 | In spite of extensive experiments and different crystallographic approaches, many aspects about how the NADP+ substrate binds to FNR and how the hydride ion is transferred from FAD to NADP+ remain unclear. | NADP | ferredoxin reductase | Homo sapiens |
| 5 | The structure of an FNR:NADP+ complex from Anabaena has been determined by X-ray diffraction analysis of the cocrystallised units to 2.1 A resolution. | NADP | ferredoxin reductase | Homo sapiens |
| 6 | Structural perturbation of FNR induced by complex formation produces a narrower cavity in which the 2"-phospho-AMP and pyrophosphate portions of the NADP+ are perfectly bound. | NADP | ferredoxin reductase | Homo sapiens |
| 7 | The crystal structure of this FNR:NADP+ complex obtained by cocrystallisation displays NADP+ in an unusual conformation and can be considered as an intermediate state in the process of coenzyme recognition and binding. | NADP | ferredoxin reductase | Homo sapiens |
| 8 | The crystal structure of this FNR:NADP+ complex obtained by cocrystallisation displays NADP+ in an unusual conformation and can be considered as an intermediate state in the process of coenzyme recognition and binding. | NADP | ferredoxin reductase | Homo sapiens |
| 9 | Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. | NADP | ferredoxin reductase | Homo sapiens |
| 10 | Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. | NADP | ferredoxin reductase | Homo sapiens |
| 11 | Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. | NADP | ferredoxin reductase | Homo sapiens |
| 12 | Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. | NADP | ferredoxin reductase | Homo sapiens |
| 13 | Finally, structural comparison with the members of the broad FNR structural family also provides an explanation for the high specificity exhibited by FNR for NADP+/H versus NAD+/H. | NADP | ferredoxin reductase | Homo sapiens |
| 14 | Finally, structural comparison with the members of the broad FNR structural family also provides an explanation for the high specificity exhibited by FNR for NADP+/H versus NAD+/H. | NADP | ferredoxin reductase | Homo sapiens |