Pub. Date : 2019 Nov
PMID : 31276316
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | CPR shows a stringent preference for NADPH over the less expensive cofactor, NADH, economically limiting its use as a biocatalyst. | NAD | cytochrome p450 oxidoreductase | Homo sapiens |
| 2 | The complexity of cofactor-linked CPR protein dynamics and the incomplete understanding of the interaction of CPR with both cofactors and electron acceptors present challenges for the successful rational engineering of a CPR with enhanced activity with NADH. | NAD | cytochrome p450 oxidoreductase | Homo sapiens |
| 3 | The complexity of cofactor-linked CPR protein dynamics and the incomplete understanding of the interaction of CPR with both cofactors and electron acceptors present challenges for the successful rational engineering of a CPR with enhanced activity with NADH. | NAD | cytochrome p450 oxidoreductase | Homo sapiens |
| 4 | The complexity of cofactor-linked CPR protein dynamics and the incomplete understanding of the interaction of CPR with both cofactors and electron acceptors present challenges for the successful rational engineering of a CPR with enhanced activity with NADH. | NAD | cytochrome p450 oxidoreductase | Homo sapiens |
| 5 | Here, we report a rational evolution approach to enhance the activity of CPR with NADH, in which mutations were introduced into the NADPH-binding flavin adenine dinucleotide (FAD) domain. | NAD | cytochrome p450 oxidoreductase | Homo sapiens |
| 6 | Multiple CPR mutants that used NADH more effectively than the wild-type CPR in the reduction of the surrogate electron acceptor, cytochrome c were found. | NAD | cytochrome p450 oxidoreductase | Homo sapiens |
| 7 | Multiple CPR mutants that used NADH more effectively than the wild-type CPR in the reduction of the surrogate electron acceptor, cytochrome c were found. | NAD | cytochrome p450 oxidoreductase | Homo sapiens |