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POR, NADPH-cytochrome P450 reductase, cytochrome P450 reductase
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, Jul 2008] (from NCBI)
Top mentioned proteins: oxidoreductase, CAN, ACID, HAD, V1a
Papers using POR antibodies
Effects of α-substitutions on structure and biological activity of anticancer chalcones
Potter Gerry A et al., In Breast Cancer Research : BCR, 2005
... Microsomes containing human cytochrome P450 (CYP1A1 or CYP1B1) and human NADPH-cytochrome P450 reductase (SUPERSOMES™), prepared from recombinant baculovirus-transformed insect cells, were obtained from BD Biosciences.
Papers on POR
Membrane topology and search for potential redox partners of colon cancer specific cytochrome P450 2W1.
Ingelman-Sundberg et al., Stockholm, Sweden. In Febs Lett, Feb 2016
In contrast to other endoplasmic reticulum P450s we found completely inverted ER membrane topology of CYP2W1 using different approaches (redox sensitive luciferase assay and protease protection assay) and demonstrated that canonical CYP reductants, cytochrome P450 reductase and cytochrome b5 cannot serve as electron donors for CYP2W1.
Optimization of a cytochrome P450 oxidation system for enhancing protopanaxadiol production in Saccharomyces cerevisiae.
Yuan et al., Tianjin, China. In Biotechnol Bioeng, Feb 2016
Recently, an artificial biosynthetic pathway of protopanaxadiol was built in Saccharomyces cerevisiae by introducing a P. ginseng dammarenediol-II synthase, a P. ginseng cytochrome P450-type protopanaxadiol synthase (PPDS), and a Arabidopsis thaliana NADPH-cytochrome P450 reductase (ATR1).
Heterologous biosynthesis of triterpenoid dammarenediol-II in engineered Escherichia coli.
Lu et al., Tianjin, China. In Biotechnol Lett, Feb 2016
RESULTS: By the strategy of synthetic biology, dammarenediol-II biosynthetic pathway was reconstituted in E. coli by co-expression of squalene synthase (SS), squalene epoxidase (SE), NADPH-cytochrome P450 reductase (CPR) from Saccharomyces cerevisiae, and SE from Methylococcus capsulatus (McSE), NADPH-cytochrome P450 reductase (CPR) from Arabidopsis thaliana.
Cytochrome P450 17A1 Interactions with the FMN Domain of its Reductase as Characterized by NMR.
Scott et al., United States. In J Biol Chem, Jan 2016
UNASSIGNED: To accomplish key physiological processes from drug metabolism to steroidogenesis, human microsomal cytochrome P450 enzymes require the sequential input of two electrons delivered by the FMN domain of NADPH-cytochrome P450 reductase (CPR).
Effect of Age on the Hepatocellularity Number for Wistar Rats.
Annaert et al., Leuven, Belgium. In Drug Metab Dispos, Jan 2016
Using the NADPH-cytochrome P450 reductase (NCR) activity method, the mean HPGL for the adult rat (8 weeks) was 104 × 106 cells/gram liver (RSD 17%).
Electron Transfer Pathways in Cholesterol Synthesis.
Porter, Lexington, United States. In Lipids, Oct 2015
The electron-donor proteins for these enzymes include cytochrome P450 reductase and the cytochrome b5 pathway.
Light-Dependent Protochlorophyllide Oxidoreductase: Phylogeny, Regulation, and Catalytic Properties.
Mysliwa-Kurdziel et al., Kraków, Poland. In Biochemistry, Oct 2015
This Current Topic focuses on light-dependent protochlorophyllide oxidoreductase (POR, EC
Cytochrome b5 modulates multiple reactions in steroidogenesis by diverse mechanisms.
Swart et al., Stellenbosch, South Africa. In J Steroid Biochem Mol Biol, Jul 2015
Cyt-b5 can augment the 17,20-lyase activity of CYP17A1 by promoting the interaction of CYP17A1 and POR; enhance the 16-ene-synthase activity of CYP17A1 by acting as an electron donor; and enhance the activity of 3βHSD by increasing the affinity of 3βHSD for its cofactor NAD(+).
The post-translational regulation of 17,20 lyase activity.
Tee et al., San Francisco, United States. In Mol Cell Endocrinol, Jul 2015
First, 17,20 lyase activity is especially sensitive to the molar abundance of the electron-transfer protein P450 oxidoreductase (POR).
Porphyromonas gingivalis and related bacteria: from colonial pigmentation to the type IX secretion system and gliding motility.
Nakayama, Nagasaki, Japan. In J Periodontal Res, Feb 2015
The Por secretion system, a novel type IX secretion system (T9SS), has been implicated in gingipain secretion in studies using non-pigmented mutants.
Functional characterization of NADPH-cytochrome P450 reductase from Bactrocera dorsalis: Possible involvement in susceptibility to malathion.
Wang et al., Chongqing, China. In Sci Rep, 2014
NADPH cytochrome P450 reductase (CPR) is essential for cytochrome P450 catalysis, which is important in the detoxification and activation of xenobiotics.
Genotype-phenotype analysis in congenital adrenal hyperplasia due to P450 oxidoreductase deficiency.
Arlt et al., Birmingham, United Kingdom. In J Clin Endocrinol Metab, 2012
Clinical, biochemical, and genetic findings in a large PORD cohort.
Effects of the CYP oxidoreductase Ala503Val polymorphism on CYP3A activity in vivo: a randomized, open-label, crossover study in healthy Chinese men.
Zhou et al., Changsha, China. In Clin Ther, 2011
POR*28 C > T polymorphism increases 1-hydroxylation of midazolam after intravenous administration. The polymorphism is associated with increased hepatic, but not intestinal, CYP3A activity in healthy Chinese volunteers.
Deletion of Porcn in mice leads to multiple developmental defects and models human focal dermal hypoplasia (Goltz syndrome).
Van den Veyver et al., Houston, United States. In Plos One, 2011
Porcn inactivation in the mouse produces a model for human FDH and that phenotypic features result from defective WNT signaling in ectodermal- and mesenchymal-derived structures.
PORCN moonlights in a Wnt-independent pathway that regulates cancer cell proliferation.
Virshup et al., Singapore, Singapore. In Plos One, 2011
PORCN protein thus appears to moonlight in a novel signaling pathway that is rate-limiting for cancer cell growth and tumorigenesis independent of its enzymatic function in Wnt biosynthesis and secretion
Heme oxygenase isoforms differ in their subcellular trafficking during hypoxia and are differentially modulated by cytochrome P450 reductase.
Behrends et al., Braunschweig, Germany. In Plos One, 2011
NADPH cytochrome P450 reductase prevents this translocation and promotes oligomerization of HO-1.
Structural basis for androgen specificity and oestrogen synthesis in human aromatase.
Pangborn et al., Buffalo, United States. In Nature, 2009
In a three-step process, each step requiring 1 mol of O(2), 1 mol of NADPH, and coupling with its redox partner cytochrome P450 reductase, aromatase converts androstenedione, testosterone and 16alpha-hydroxytestosterone to oestrone, 17beta-oestradiol and 17beta,16alpha-oestriol, respectively.
Enzyme-catalyzed activation of anticancer prodrugs.
Vermeulen et al., Amsterdam, Netherlands. In Pharmacol Rev, 2004
The following endogenous enzymes are discussed: aldehyde oxidase, amino acid oxidase, cytochrome P450 reductase, DT-diaphorase, cytochrome P450, tyrosinase, thymidylate synthase, thymidine phosphorylase, glutathione S-transferase, deoxycytidine kinase, carboxylesterase, alkaline phosphatase, beta-glucuronidase and cysteine conjugate beta-lyase.
Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family.
Herriott et al., Ithaca, United States. In Science, 1991
With these key residues as a guide, conclusive evidence is presented that the ferredoxin reductase structure is a prototype for the nicotinamide dinucleotide and FAD binding domains of the enzymes NADPH-cytochrome P450 reductase, NADPH-sulfite reductase, NADH-cytochrome b5 reductase, and NADH-nitrate reductase.
Presence of NADPH-cytochrome P450 reductase in central catecholaminergic neurones.
Gustafsson et al., In Nature, 1984
The enzyme system consists of a lipid fraction (phosphatidylcholine), cytochrome P450 and NADPH-cytochrome P450 reductase.
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