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Literature summary for 1.6.2.4 extracted from
- NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family (2012), Arch. Biochem. Biophys., 528, 72-89.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | membrane-bound protein associated with the cytoplasmic side of the endoplasmic reticulum | Homo sapiens | 16020 | - |
| membrane | membrane-bound protein associated with the cytoplasmic side of the endoplasmic reticulum | Rattus norvegicus | 16020 | - |
| microsome | - |
Homo sapiens | - |
- |
| microsome | - |
Rattus norvegicus | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| NADPH + oxidized hemoprotein = NADP+ + reduced hemoprotein + H+ | catalytic cycle and the rate-limiting step, which is at or after the introduction of the second electron from the reductase to the heme iron | Homo sapiens | |
| NADPH + oxidized hemoprotein = NADP+ + reduced hemoprotein + H+ | catalytic cycle and the rate-limiting step, which is at or after the introduction of the second electron from the reductase to the heme iron | Rattus norvegicus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | domain-domain interactions, structure-activity analysis and structure comparisons, overview | Homo sapiens |
| More | domain-domain interactions, structure-activity analysis and structure comparisons, overview | Rattus norvegicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CYPOR | - |
Homo sapiens |
| CYPOR | - |
Rattus norvegicus |
| NADPH-cytochrome P450 oxidoreductase | - |
Homo sapiens |
| NADPH-cytochrome P450 oxidoreductase | - |
Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Homo sapiens |  |
| FAD | - |
Rattus norvegicus | |
| FMN | - |
Homo sapiens | |
| FMN | - |
Rattus norvegicus | |
| additional information | FAD accepts a hydride ion from NADPH, and reduced FAD donates electrons to FMN, which in turn transfers electrons to the heme center of cytochrome P450 or NOS oxygenase domain. The FAD and FMN domains are connected by a flexible hinge region, which spans 12 residues from Gly232 to Arg243. The amino acids of the connecting domain are interspersed with the FNR-like domain, (residues 244-266 and 326-450 in rat CYPOR numbering). The connecting domain, composed mainly of alpha-helices, is tightly bound to the FNR-like domain, and together they form the FAD domain, electron transfer mechanism, structure, and redox potentials of the individual redox couples of FAD and FMN of CYPOR, overview | Rattus norvegicus | |
| additional information | FAD accepts a hydride ion from NADPH, and reduced FAD donates electrons to FMN, which in turn transfers electrons to the heme center of cytochrome P450 oxygenase domain, electron transfer mechanism, structure, and redox potentials of the individual redox couples of FAD and FMN of CYPOR, overview. The FAD and FMN domains are connected by a flexible hinge region. The amino acids of the connecting domain are interspersed with the FNR-like domain. The connecting domain, composed mainly of alpha-helices, is tightly bound to the FNR-like domain, and together they form the FAD domain | Homo sapiens | |
| NADPH | - |
Homo sapiens | |
| NADPH | - |
Rattus norvegicus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme is a member of the diflavin oxidoreductase family. They are multi-domain enzymes containing distinct FAD and FMN domains connected by a flexible hinge. The protein has evolved by fusing two ancestral genes that encode proteins related to a FMN-containing flavodoxin and a FAD-containing ferredoxin-NADP+ oxidoreductase | Homo sapiens |
| evolution | the enzyme is a member of the diflavin oxidoreductase family. They are multi-domain enzymes containing distinct FAD and FMN domains connected by a flexible hinge. The protein has evolved by fusing two ancestral genes that encode proteins related to a FMN-containing flavodoxin and a FAD-containing ferredoxin-NADP+ oxidoreductase | Rattus norvegicus |
| metabolism | microsomal P450 systems, overview | Homo sapiens |
| metabolism | microsomal P450 systems, overview | Rattus norvegicus |
| additional information | FAD accepts a hydride ion from NADPH, and reduced FAD donates electrons to FMN, which in turn transfers electrons to the heme center of cytochrome P450 or NOS oxygenase domain, electron transfer mechanism, overview. The two flavin domains undergo large domain movements during catalysis, domain-domain interactions, structure-activity analysis, overview | Rattus norvegicus |
| additional information | FAD accepts a hydride ion from NADPH, and reduced FAD donates electrons to FMN, which in turn transfers electrons to the heme center of cytochrome P450 oxygenase domain, electron transfer mechanism, overview. The two flavin domains undergo large domain movements during catalysis, domain-domain interactions, structure-activity analysis, overview | Homo sapiens |
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Release 2023.1 (January 2023)
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