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Validated All-in-One™ qPCR Primer for POR(NM_000941.2) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
This gene encodes an endoplasmic reticulum membrane oxidoreductase with an FAD-binding domain and a flavodoxin-like domain. The protein binds two cofactors, FAD and FMN, which allow it to donate electrons directly from NADPH to all microsomal P450 enzymes. Mutations in this gene have been associated with various diseases, including apparent combined P450C17 and P450C21 deficiency, amenorrhea and disordered steroidogenesis, congenital adrenal hyperplasia and Antley-Bixler syndrome. [provided by RefSeq].
Gene References into function
- activation of HIF-1 is modulated by cytochrome P-450 reductase in cell membrane
- role of coenzyme binding in regulating interflavin electron transfer in human cytochrome P450 reductase
- Molecular pathogenesis of this form of congenital adrenal hyperplasia is caused by mutations in the gene encoding P450 oxidoreductase
- POR deficiency is a new disorder of adrenal and gonadal steroidogenesis that affects all microsomal cytochrome P450 enzymes, hence may have important implications for genetic differences in drug metabolism.
- POR deficiency is a new disease, distinct from the craniosynostosis syndromes caused by FGFR mutations.
- analysis of FAD binding in the Y459H and V492E Antley-Bixler syndrome mutants of human cytochrome P450 reductase
- Antticancer activity of motexafin gadolinium may involve inhibition of this enzyme.
- data suggest that African Americans harbor an allele at the POR locus that may increase breast cancer risk
- A287P homozygous patients had preferential inhibition of CYP17A1, whereas Steroid 21-Hydroxylase retained near normal activity.
- The energetics of 2',5'-ADP binding to the FAD-binding domain of cytochrome P450 reductase were characterized.
- Mutations R457H and V492E located in the FAD domain of NADPH P450 oxidoreductase (POR) that disrupt electron transfer caused a complete loss of CYP19A1 activity.
- clinical, structural and functional implications of mutations and polymorphisms in POR
- TG100435 and TG100855 were interconverted metabolically. FMO3 seem to be the major N-oxidizing enzyme, whereas cytochrome P450 reductase seems to be responsible for the retroreduction reaction.
- The POR gene in a representative population of 842 healthy unrelated individuals in four ethnic groups was sequenced and compared.
- The prognosis for patients with POR deficiency appears to depend on the severity of the bony malformations and their timely treatment.
- The common P450 oxidoreductase variant A503V is not a modifier gene for 21-hydroxylase deficiency.
- POR deficiency can masquerade clinically as isolated 17,20-lyase deficiency.
- patients with Antley-Bixler-like skeletal anomalies, but with mutations in the POR gene and disordered steroidogenesis, represent a new disorder called POR deficiency.
- Experiments using excess NADPH over cytochrome P450 reductase provide evidence that both pH and solvent significantly influence the kinetic exposure of the blue di-semiquinone intermediate, yet the observed rate constants are essentially pH independent.
- CPR's putative membrane topology indicates that the Q153R and R316W missense mutations found in patients with disordered steroidogenesis are located within the membrane-associated regions.