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Gene Review

NCP1  -  Ncp1p

Saccharomyces cerevisiae S288c

Synonyms: CPR, CPR1, NADPH--cytochrome P450 reductase, NCPR1, P450R, ...
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Disease relevance of NCP1

  • Native yeast NADPH-cytochrome P450 oxidoreductase (CPR; EC and a soluble derivative lacking 33 amino acids of the NH(2)-terminus have been overexpressed as recombinant proteins in Escherichia coli [1]
  • We isolated cDNA (pgCYR, about 2.1 kb) and genomic DNA (pgGYR, about 4 kb) clones coding for NADPH-cytochrome P450 reductase by immunoscreening of yeast Saccharomyces cerevisiae cDNA and genomic DNA libraries in phage lambda gt11 [2].

High impact information on NCP1

  • Phenylalanine ammonia lyase (PAL), cinnamate 4-hydroxylase (C4H), and the C4H redox partner cytochrome p450 reductase (CPR) are important in allocating significant amounts of carbon from phenylalanine into phenylpropanoid biosynthesis in plants [3].
  • Purification of the cytosolic mutant CPR indicated properties identical to native CPR and an ability to reconstitute ergosterol biosynthesis when added to a cell-free system, as well as to allow reconstitution of activity with purified CYP61, sterol 22-desaturase [4].
  • The disruption of Saccharomyces cerevisiae NADPH- cytochrome P450 oxidoreductase (CPR) gene resulted in a viable strain accumulating approximately 25% of the ergosterol observed in a sterol wild-type parent [4].
  • The associated phenotypes could be reversed in transformants after expression of native CPR and a mutant lacking the N-terminal 33 amino acids, which localized in the cytosol [4].
  • Purified recombinant cytochrome P450 52A3 and the corresponding NADPH-cytochrome P450 reductase from the alkane-assimilating yeast Candida maltosa were reconstituted into an active alkane monooxygenase system [5].

Biological context of NCP1


Anatomical context of NCP1


Associations of NCP1 with chemical compounds


Other interactions of NCP1

  • Furthermore, reconstitution of the soluble enzyme with soluble yeast Ncpr1p, expressed and purified as an N-terminal deletion of 33 amino acids encompassing its membrane anchor, resulted in a fully functional and soluble eukaryotic Erg11p system [11].
  • In contrast, cells that overexpressed FRE2 had maximal ferrireductase activity when NCP1 was repressed [12].
  • Overexpression of FRE1 did not lead to an increased ferrireductase activity of the cells when NCP1 was repressed [12].
  • Transcripts for the three poplar CPR genes were present ubiquitously in all tissues examined, but CPR2 showed highest expression in young leaf tissue [18].
  • The divergent CPR isoforms (CPR1 and CPR2/3) contained entirely different N-terminal sequences, which are conserved in other plant CPRs and are diagnostic for two distinct classes of CPRs within the angiosperms [18].

Analytical, diagnostic and therapeutic context of NCP1


  1. Activities and kinetic mechanisms of native and soluble NADPH-cytochrome P450 reductase. Lamb, D.C., Warrilow, A.G., Venkateswarlu, K., Kelly, D.E., Kelly, S.L. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  2. Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 reductase deduced from nucleotide sequence of its cloned gene. Yabusaki, Y., Murakami, H., Ohkawa, H. J. Biochem. (1988) [Pubmed]
  3. Reconstitution of the entry point of plant phenylpropanoid metabolism in yeast (Saccharomyces cerevisiae): implications for control of metabolic flux into the phenylpropanoid pathway. Ro, D.K., Douglas, C.J. J. Biol. Chem. (2004) [Pubmed]
  4. The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity. Venkateswarlu, K., Lamb, D.C., Kelly, D.E., Manning, N.J., Kelly, S.L. J. Biol. Chem. (1998) [Pubmed]
  5. Oxygenation cascade in conversion of n-alkanes to alpha,omega-dioic acids catalyzed by cytochrome P450 52A3. Scheller, U., Zimmer, T., Becher, D., Schauer, F., Schunck, W.H. J. Biol. Chem. (1998) [Pubmed]
  6. Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction. Lamb, D.C., Kelly, D.E., Manning, N.J., Kaderbhai, M.A., Kelly, S.L. FEBS Lett. (1999) [Pubmed]
  7. A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases. Lamb, D.C., Kim, Y., Yermalitskaya, L.V., Yermalitsky, V.N., Lepesheva, G.I., Kelly, S.L., Waterman, M.R., Podust, L.M. Structure (2006) [Pubmed]
  8. Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5. Urban, P., Mignotte, C., Kazmaier, M., Delorme, F., Pompon, D. J. Biol. Chem. (1997) [Pubmed]
  9. Functional co-expression of human oxidoreductase and cytochrome P450 1A1 in Saccharomyces cerevisiae results in increased EROD activity. Eugster, H.P., Bärtsch, S., Würgler, F.E., Sengstag, C. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  10. Cloning and heterologous expression of the NADPH cytochrome P450 oxidoreductase genes from an industrial dicarboxylic acid-producing Candida tropicalis. He, F., Chen, Y.T. Yeast (2005) [Pubmed]
  11. Generation of a complete, soluble, and catalytically active sterol 14 alpha-demethylase-reductase complex. Lamb, D.C., Kelly, D.E., Venkateswarlu, K., Manning, N.J., Bligh, H.F., Schunck, W.H., Kelly, S.L. Biochemistry (1999) [Pubmed]
  12. Cytochrome P-450 reductase is responsible for the ferrireductase activity associated with isolated plasma membranes of Saccharomyces cerevisiae. Lesuisse, E., Casteras-Simon, M., Labbe, P. FEMS Microbiol. Lett. (1997) [Pubmed]
  13. NADPH-cytochrome P-450 reductase of yeast microsomes. Aoyama, Y., Yoshida, Y., Kubota, S., Kumaoka, H., Furumichi, A. Arch. Biochem. Biophys. (1978) [Pubmed]
  14. Deformylation of 32-oxo-24,25-dihydrolanosterol by the purified cytochrome P-45014DM (lanosterol 14 alpha-demethylase) from yeast evidence confirming the intermediate step of lanosterol 14 alpha-demethylation. Aoyama, Y., Yoshida, Y., Sonoda, Y., Sato, Y. J. Biol. Chem. (1989) [Pubmed]
  15. NADPH cytochrome P-450 oxidoreductase and susceptibility to ketoconazole. Venkateswarlu, K., Kelly, D.E., Manning, N.J., Kelly, S.L. Antimicrob. Agents Chemother. (1998) [Pubmed]
  16. Functional cloning, based on azole resistance in Saccharomyces cerevisiae, and characterization of Rhizopus nigricans redox carriers that are differentially involved in the P450-dependent response to progesterone stress. Kunic, B., Truan, G., Breskvar, K., Pompon, D. Mol. Genet. Genomics (2001) [Pubmed]
  17. Enhanced production of ethylene from methional by iron chelates and heme containing proteins in the system consisting of quinone compounds and NADPH-cytochrome P-450 reductase. Komiyama, T., Sawada, M.T., Kobayashi, K., Yoshimoto, A. Biochem. Pharmacol. (1985) [Pubmed]
  18. Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar. Ro, D.K., Ehlting, J., Douglas, C.J. Plant Physiol. (2002) [Pubmed]
  19. Disruption of the Saccharomyces cerevisiae gene for NADPH-cytochrome P450 reductase causes increased sensitivity to ketoconazole. Sutter, T.R., Loper, J.C. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  20. Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase. Shimizu, T., Tateishi, T., Hatano, M., Fujii-Kuriyama, Y. J. Biol. Chem. (1991) [Pubmed]
  21. Maximizing the expression of mammalian cytochrome P-450 monooxygenase activities in yeast cells. Urban, P., Cullin, C., Pompon, D. Biochimie (1990) [Pubmed]
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