EC number:1.6.2.4
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.6 Acting on NADH or NADPH |
| 1.6.2 With a heme protein as acceptor |
| ID: | 1.6.2.4 |
|---|---|
| Description: | NADPH--hemoprotein reductase. |
| Alternative Name: |
TPNH-cytochrome c reductase. TPNH(2) cytochrome c reductase. phosphate). Reductase, cytochrome c (reduced nicotinamide adenine dinucleotide Reduced nicotinamide adenine dinucleotide phosphate-cytochrome c NADPH:P450 reductase. NADPH:ferrihemoprotein oxidoreductase. NADPH-dependent cytochrome c reductase. NADPH--ferrihemoprotein reductase. NADPH--ferricytochrome c oxidoreductase. NADPH--cytochrome P450 reductase. NADPH--cytochrome P450 oxidoreductase. NADPH--cytochrome c reductase. NADPH--cytochrome c oxidoreductase. NADP--cytochrome reductase. NADP--cytochrome c reductase. Ferrihemoprotein P-450 reductase. FAD-cytochrome c reductase. reductase. Dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c Cytochrome P450 reductase. phosphate, NADPH, NADPH-dependent). Cytochrome c reductase (reduced nicotinamide adenine dinucleotide CPR. Aldehyde reductase (NADPH-dependent). |
| Cath: | 1.10.630.10; 3.30.70.100; 3.30.70.3430; 3.40.50.80; 1.20.910.10; 1.20.990.10; 2.40.30.10; 3.40.50.360; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.6.2.4 |
| BRENDA Enzyme Link: | BRENDA 1.6.2.4 |
| KEGG Enzyme Link: | KEGG1.6.2.4 |
| BioCyc Enzyme Link: | BioCyc 1.6.2.4 |
| ExPASy Enzyme Link: | ExPASy1.6.2.4 |
| EC2PDB Enzyme Link: | EC2PDB 1.6.2.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.6.2.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.6.2.4 |
| IntEnz Enzyme Link: | IntEnz 1.6.2.4 |
| MEDLINE Enzyme Link: | MEDLINE 1.6.2.4 |
| RHEA:24040 | NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450] |
| RULE(radius=1) | [*:1]-[Fe-;H0:2](-[*:3])(-[*:4])-[*:5].[*:6]-[Fe-;H0:7](-[*:8])(-[*:9])-[*:10].[*:11]-[N;H0;+0:12]1-[CH;+0:13]=[C;H0;+0:14](-[*:15])-[CH2;+0:16]-[CH;+0:17]=[CH;+0:18]-1>>[*:1]-[FeH2-2:2](-[*:3])(-[*:4])-[*:5].[*:6]-[Fe-2:7](-[*:8])(-[*:9])-[*:10].[*:11]-[n+;H0:12]1:[cH;+0:13]:[c;H0;+0:14](-[*:15]):[cH;+0:16]:[cH;+0:17]:[cH;+0:18]:1 |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. | Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ | 1997 Aug 5 | 9237990 |
| NADPH-P-450 reductase: structural and functional comparisons of the eukaryotic and prokaryotic isoforms. | Sevrioukova IF, Peterson JA | 1995 | 8589067 |
| Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components. | Lu AY, Junk KW, Coon MJ | 1969 Jul 10 | 4389465 |
| The mechanism of 1- and 2-electron transfers catalyzed by reduced triphosphopyridine nucleotide-cytochrome c reductase. | Masters BS, Bilimoria MH, Kamin H, Gibson QH | 1965 Oct | 4378860 |
| STUDIES ON THE MECHANISM OF MICROSOMAL TRIPHOSPHOPYRIDINE NUCLEOTIDE-CYTOCHROME C REDUCTASE. | MASTERS BS, KAMIN H, GIBSON QH, WILLIAMS CH Jr | 1965 Feb | 14275154 |
| Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver. | WILLIAMS CH Jr, KAMIN H | 1962 Feb | 14007123 |
| Electron transfer in human cytochrome P450 reductase. | Gutierrez A, Grunau A, Paine M, Munro AW, Wolf CR, Roberts GC, Scrutton NS | 2003 Jun | 12773143 |
| Determination of the redox properties of human NADPH-cytochrome P450 reductase. | Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK | 2001 Feb 20 | 11329262 |