Letteratura scientifica selezionata sul tema "Monooxygénases du cytochrome P450"
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Articoli di riviste sul tema "Monooxygénases du cytochrome P450":
Paul Bolwell, G. "Cytochrome P450:". Phytochemistry 35, n. 1 (dicembre 1993): 279. http://dx.doi.org/10.1016/s0031-9422(00)90557-0.
Ehrenpreis, Eli D., e Seymour Ehrenpreis. "CYTOCHROME P450". Clinics in Liver Disease 2, n. 3 (agosto 1998): 457–70. http://dx.doi.org/10.1016/s1089-3261(05)70021-0.
Roos, P. H., e N. Jakubowski. "Cytochrome P450". Analytical and Bioanalytical Chemistry 392, n. 6 (9 ottobre 2008): 1015–17. http://dx.doi.org/10.1007/s00216-008-2415-z.
D'Arcy, P. F. "Cytochrome P450". International Journal of Pharmaceutics 103, n. 1 (febbraio 1994): 99. http://dx.doi.org/10.1016/0378-5173(94)90211-9.
Poulos, Thomas L. "Cytochrome P450". Current Opinion in Structural Biology 5, n. 6 (dicembre 1995): 767–74. http://dx.doi.org/10.1016/0959-440x(95)80009-3.
Coulson, C. J. "Cytochrome P450". Trends in Biochemical Sciences 10, n. 2 (febbraio 1985): 92. http://dx.doi.org/10.1016/0968-0004(85)90255-5.
Yamazaki, Hiroshi, Elizabeth M. J. Gillam, Mi-Sook Dong, William W. Johnson, F. Peter Guengerich e Tsutomu Shimada. "Reconstitution of Recombinant Cytochrome P450 2C10(2C9) and Comparison with Cytochrome P450 3A4 and Other Forms: Effects of Cytochrome P450–P450 and Cytochrome P450–b5Interactions". Archives of Biochemistry and Biophysics 342, n. 2 (giugno 1997): 329–37. http://dx.doi.org/10.1006/abbi.1997.0125.
Guengerich, F. Peter, Martha V. Martin, Christal D. Sohl e Qian Cheng. "Measurement of cytochrome P450 and NADPH–cytochrome P450 reductase". Nature Protocols 4, n. 9 (6 agosto 2009): 1245–51. http://dx.doi.org/10.1038/nprot.2009.121.
de Wildt, Saskia N., Gregory L. Kearns, J. Steven Leeder e John N. van den Anker. "Cytochrome P450 3A". Clinical Pharmacokinetics 37, n. 6 (1999): 485–505. http://dx.doi.org/10.2165/00003088-199937060-00004.
Poulos, T. L. "Cytochrome P450 flexibility". Proceedings of the National Academy of Sciences 100, n. 23 (3 novembre 2003): 13121–22. http://dx.doi.org/10.1073/pnas.2336095100.
Tesi sul tema "Monooxygénases du cytochrome P450":
Vincent, Thierry. "Optimisation des conditions réactionnelles et création de nouveaux mutants à grande performance du cytochrome p450 BM3 CYP102A1 utilisant les cofacteurs alternatifs NADH et N-benzyl-1,4-dihydronicotinamide". Doctoral thesis, Université Laval, 2020. http://hdl.handle.net/20.500.11794/66678.
The p450 cytochrome CYP102A1, better known as BM3, comes from the bacteria Bacillus megaterium. This enzyme possesses a prosthetic heme group enabling it to catalyze the insertion of oxygen into a carbon-hydrogen bond generally resulting in the hydroxylation of the substrate, the enzyme is therefore a monooxygenase. This type of reaction remains difficult to achieve by traditional chemistry. Unlike other p450 cytochromes, BM3 is soluble (is not membrane bound) and is naturally fused to its reductase partner forming a single polypeptide chain. As such, in recent years, BM3 has garnered much attention from the pharmaceutical and fine chemical industries, due to its high biocatalytic potential. However, its use in industry remains constrained by its instability as well as by the prohibitive cost of its cofactor, NADPH. This thesis describes the development of different strategies aiming at liberating reactions driven with BM3 from their dependence to NADPH whilst maximizing the specific yield of the monooxygenase. Instead of NADPH, two other inexpensive cofactors were used, namely NADH and N-benzyl-1,4-dihydronicotinamide (NBAH) by using the BM3 mutant R966D/W1046S. To maximize BM3 specific yield, one of the strategies used in this thesis work, the optimization of the reaction medium, rested on two key elements. Firstly, favouring the stabilization of the cofactor, as it was found to be more unstable than the enzyme itself and secondly lowering the reaction temperature as this effectively augmented oxidase/reductase reactions coupling and as such the stability of the enzyme. The net effect of the optimized reaction was to enhance the specific yield of the BM3 mutant R966D/W1046S by a factor of 2 and 2,6 depending on which cofactor was used. Two other enzymatic engineering strategies were explored to generate mutations which could enhance the performance of BM3. One of these, consensus guided mutagenesis, generated a library of mutants from which mutants NTD5 and NTD6 were identified enhancing the specific yield of the enzyme comparatively to their parent, R966D/W1046S, by a factor of 5,24 and 2,3 for NBAH and NADH respectively. The other strategy explored was to apply a selective pressure on Bacillus megaterium to force, by experimental evolution, the performance of the enzyme. From this strategy, a new mutant of BM3 called DE, possessing 34 new amino acid substitutions, was generated. This new mutant displayed a greater resistance to organic solvents as well as an augmentation of specific yields when used alongside NADPH and NADH comparatively to wild type BM3 by a factor of 1,23 and 1,76 respectively. The strategies described in this thesis allowed a significative enhancement of BM3 specific yield as well as represent two new methodologies by which new beneficial mutations can be identified.
Trigui, Mohamed. "Biodégradation des amines cycliques par Mycobacterium sp. RP1 et Pseudomonas putida O1G3 : Caractérisation des monooxygénases impliquées dans l'hydroxylation des liaisons C-N". Compiègne, 2002. http://www.theses.fr/2002COMP1415.
Buronfosse, Thierry. "Métabolisme énantiosélectif de trois molécules à groupement thioéthers par des monooxygénases à cytochrome P450 et à flavine chez le rat : implications pharmacologiques et toxicologiques". Lyon 1, 1995. http://www.theses.fr/1995LYO1T202.
Mascia, Francesco. "Engineering ferredoxin-dependent oxyfunctionalization in cyanobacteria". Electronic Thesis or Diss., Aix-Marseille, 2022. http://www.theses.fr/2022AIXM0648.
Cyanobacteria are attracting growing attention as photo-biocatalysts meeting the criteria of Green Chemistry. They are able to grow using only light and CO2 as energy and carbon sources. The addition of sacrificial electron donors (i.e. glucose) for the recycling of the NADPH cofactor of oxidoreductases is not necessary because it is regenerated by electrons from the photosynthetic oxidation of water, while the oxygenases can use the oxygen produced in-situ during photosynthesis. A strain of Synechocystis sp. PCC 6803, modified to express CYP153A6, a cytochrome P450, selectively hydroxylates limonene, a cheap and widely available substrate, to perillyl alcohol, usable as a flavor or drug. Another strain, expressing only CYP110D1 without any electron-carrier proteins of this cytochrome P450, catalyzes the regioselective hydroxylation of testosterone to 15β-hydroxytestosterone, which is more bioavailable and suitable for oral formulations. The activity (1 U gCDW-1) is twice as high as that of the reactions biocatalyzed by the bacterium Escherichia coli. A CYP110D1-Fed1 fusion protein, one of the native Synechocystis ferredoxins, was also designed, aiming to channel photosystem I electrons more efficiently to monooxygenase. This work demonstrated the efficacy of modified cyanobacteria expressing cytochromes P450 when used as biocatalysts in whole-cell processes. They enable the sustainable production of high-value products, such as pharmaceuticals
Mougin, Christian. "Métabolisme oxydatif du chlortoluron chez des cultures cellulaires de blé : intervention de monooxygénases à cytrochrome P-450". Toulouse, INPT, 1990. http://www.theses.fr/1990INPT034G.
Lemoine, Antoinette. "Rôle des monooxygénases à cytochrome P-450 et à flavine dans le métabolisme de l'imipramine : étude de la régulation hormonale chez le rat". Paris 11, 1991. http://www.theses.fr/1991PA114837.
Clair, Philippe. "Expression de cytochromes P-450, de la NADPH cytochrome P-450 réductase et de monooxygénases à flavine par baculovirus recombinants : Une contribution à l'étude du métabolisme des xénobiotiques chez l'homme". Montpellier 2, 1993. http://www.theses.fr/1993MON20248.
Siddique, Muhammad Hussnain. "Study of the biosynthesis pathway of the geosmin in Penicillium expansum". Thesis, Toulouse, INPT, 2012. http://www.theses.fr/2012INPT0085/document.
Geosmin is a terpenoid, an earthy-musty compound associated with off-flavors in water and wine. In bacteria, the biosynthesis pathway of geosmin is well characterized, but little is known about its biosynthesis in eukaryotes, especially in filamentous fungi. The origin of geosmin in grapevine is largely attributable to the presence of Penicillium expansum on grapes. In this thesis, we have described the characterization and analysis of "gpe1", a gene encoding a cytochrome P450 monooxygenase probably involved in the biosynthesis of geosmin in P. expansum M2230, in order to better understand of the biosynthesis pathway of geosmin in this species. We demonstrated that the two DNA fragments i.e. p450-1 and p450-2 belong to a single cytochrome p450 gene (gpe1). We showed that the deduced amino acid sequence of gpe1 has an average identity of 40 % with PbP450-2 and P450-4 enzymes which have been found involved in indole diterpene synthesis and in gibberellin synthesis respectively. Then, the results of PCRs performed on the fourteen Penicillium species showed that only Penicillium species which were producers of geosmin gave the same fragment of ~1.2 kb like gpe1. Analysis of the gpe1 gene enabled us to identify the presence of some conserved domains of cytochromes P450 monoxygenases in the amino acid sequence of gpe1. Then, the functional characterization of the gpe1 gene in P. expansum M2230 was described. We illustrated that the mutants of gpe1 lost their potential to produce geosmin whereas the reverse complements of gpe1 restored their potential to produce geosmin. Finally, we demonstrated that a putative polyketide synthase and a putative NRPS-like enzyme are present on the right side of the gpe1 gene suggesting that gpe1 gene might be the part of a gene cluster encoding the biosynthesis of secondary metabolites
Lafite, Pierre. "ETUDE du CYTOCHROME P450 2J2 HUMAIN :Recherche de substrats et d'inhibiteurs sélectifs ;Détermination de la topologie de son site actif". Phd thesis, Université René Descartes - Paris V, 2007. http://tel.archives-ouvertes.fr/tel-00192090.
Dugrand-Judek, Audray. "Contribution à l’étude phytochimique et moléculaire de la synthèse des coumarines et furocoumarines chez diverses variétés d’agrumes du genre Citrus". Thesis, Université de Lorraine, 2015. http://www.theses.fr/2015LORR0238/document.
Coumarins and furanocoumarins are phytoalexines synthesized by some plant families (e.g. Rutaceæ that include citrus), to defend themselves against bioaggressors. Furanocoumarins can be toxic for humans, when combined with some drugs: this is the grapefruit juice effect. Nowadays, most of the cytochrome P450s involved in the furanocoumarin synthesis in Apiaceæ, have already been characterized. However, despite the economical importance of citrus, a little is known about the coumarins and furanocoumarins pathway in these plants. In this work, we created, optimized and validated an analytical method by ultra high performance liquid chromatography coupled with mass spectrometry (UPLC-MS), to identify and quantitate 28 coumarins and furanocoumarins in citrus peel and pulp. This method allowed us to chemotype 62 citrus varieties, distinguished by their low or high capacity to produce these compounds. In parallel, a bioinformatic work on public banks of genomic DNA from citrus, allowed to identify seven genes with high sequence homologies with those involved in the synthesis of furanocoumarins in Pastinaca sativa (CYP71) and in Arabidopsis thaliana (CYP82). A quantitative analysis of their expression level in citrus showed that four of them were more expressed in high coumarins and furanocoumarins producing fruits. The cloning of these genes and their heterologous expression in yeast, revealed the function of grapefruit and Combava CYP82D64, which catalyzes the hydroxylation of xanthotoxin in 5-hydroxy-xanthotoxin. The synthesis of coumarins and furanocoumarins in citrus, then better apprehended, allowed us to propose a breeding scheme aiming at decreasing the levels of these compounds in Citrus. We also showed the convergent evolution of CYP71 and CYP82 in their synthesis in Apiaceæ and in Rutaceæ respectively. The discovery of the first cytochrome P450 from Citrus involved in the production of these compounds, opens up new prospects for the elucidation of their biosynthetic pathway in citrus
Libri sul tema "Monooxygénases du cytochrome P450":
Yan, Zhengyin, e Gary W. Caldwell, a cura di. Cytochrome P450. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1542-3.
Schenkman, John B., e Helmut Greim, a cura di. Cytochrome P450. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77763-9.
Ortiz de Montellano, Paul R., a cura di. Cytochrome P450. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-12108-6.
Ortiz de Montellano, Paul R., a cura di. Cytochrome P450. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/b139087.
de Montellano, Paul R. Ortiz, a cura di. Cytochrome P450. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5.
R, Waterman Michael, e Johnson Eric F, a cura di. Cytochrome P450. San Diego: Academic Press, 1991.
F, Johnson Eric, e Waterman Michael R, a cura di. Cytochrome P450. San Diego: Academic Press, 1996.
Emel, Arinç, Schenkman John B e Greim Helmut, a cura di. Cytochrome P450. Berlin: Springer-Verlag, 1993.
Phillips, Ian R., e Elizabeth A. Shephard. Cytochrome P450 Protocols. New Jersey: Humana Press, 1998. http://dx.doi.org/10.1385/0896035190.
Ian, Phillips R., e Shephard A. Elizabeth. Cytochrome P450 Protocols. New Jersey: Humana Press, 2005. http://dx.doi.org/10.1385/1592599982.
Capitoli di libri sul tema "Monooxygénases du cytochrome P450":
Webb, Nadia. "Cytochrome P450". In Encyclopedia of Clinical Neuropsychology, 764–65. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-0-387-79948-3_1761.
Webb, Nadia. "Cytochrome P450". In Encyclopedia of Clinical Neuropsychology, 1–2. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-56782-2_1761-2.
Webb, Nadia. "Cytochrome P450". In Encyclopedia of Clinical Neuropsychology, 1036–37. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-57111-9_1761.
van Schaik, Ron H. N. "Cytochrome P450". In Encyclopedia of Cancer, 1–9. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_1460-2.
Hoyer, Daniel, Eric P. Zorrilla, Pietro Cottone, Sarah Parylak, Micaela Morelli, Nicola Simola, Nicola Simola et al. "Cytochrome P450". In Encyclopedia of Psychopharmacology, 364. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_1190.
Guengerich, F. Peter. "Cytochrome P450". In Enzyme Systems that Metabolise Drugs and Other Xenobiotics, 33–65. Chichester, UK: John Wiley & Sons, Ltd, 2002. http://dx.doi.org/10.1002/0470846305.ch2.
van Schaik, Ron H. N. "Cytochrome P450". In Encyclopedia of Cancer, 1282–90. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_1460.
Ando, Yuichi. "Cytochrome P450". In Cancer Drug Discovery and Development, 273–88. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-9135-4_16.
Talevi, Alan, e Carolina L. Bellera. "Cytochrome P450". In The ADME Encyclopedia, 290–97. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-84860-6_65.
Talevi, Alan, e Carolina L. Bellera. "Cytochrome P450". In The ADME Encyclopedia, 1–8. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-51519-5_65-1.
Atti di convegni sul tema "Monooxygénases du cytochrome P450":
Burris-Hiday, Sarah, Mengqi Chai, Michael L. Gross e Emily Scott. "Human Cytochrome P450 Interactions with Redox Partner Cytochrome P450 Reductase". In ASPET 2023 Annual Meeting Abstracts. American Society for Pharmacology and Experimental Therapeutics, 2023. http://dx.doi.org/10.1124/jpet.122.267650.
"Cytochrome P450 Enzymes and Microbial Drug Preparation". In 2017 International Conference on Materials Science and Biological Engineering. Francis Academic Press, 2017. http://dx.doi.org/10.25236/icmsbe.2017.14.
Seguin, Ryan P., Libin Xu e Ryan Nguyen. "Unusual Metabolism of Benzethonium by Cytochrome P450". In ASPET 2023 Annual Meeting Abstracts. American Society for Pharmacology and Experimental Therapeutics, 2023. http://dx.doi.org/10.1124/jpet.122.564180.
Tian, Haijin, Paul Quehl, Joel Hollender e Joachim Jose. "Surface display of human cytochrome P450 enzymes 3A4, 1A2, 2C9, 2C19 and 2D6 with cytochrome P450 reductase for drug metabolism studies". In 5th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2019. http://dx.doi.org/10.3390/ecmc2019-06333.
Özgen, İlker Tolga, Esra Kutlu, Hatice Nursoy, Yaşar Cesur e Gözde Yeşil. "P94 Cytochrome P450 oxidoreductase enzyme deficiency: a case report". In Faculty of Paediatrics of the Royal College of Physicians of Ireland, 9th Europaediatrics Congress, 13–15 June, Dublin, Ireland 2019. BMJ Publishing Group Ltd and Royal College of Paediatrics and Child Health, 2019. http://dx.doi.org/10.1136/archdischild-2019-epa.449.
Wu, Huan, Yun-Qiang Di, Chun-Hou Zheng e Junfeng Xia. "Prediction of cytochrome P450 inhibition using ensemble of extreme learning machine". In 2013 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2013. http://dx.doi.org/10.1109/bibm.2013.6732515.
Casper, Jessica A., Diane R. Bielenberg, Jennifer Cheng, Birgitta Schmidt, Bruce D. Hammock, Darryl C. Zeldin, Mark W. Kieran e Dipak Panigrahy. "Abstract 3952: Cytochrome P450-derived eicosanoids regulate pancreatic cancer and metastasis." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3952.
Abraham, JE, M. Maranian, K. Driver, D. Greenberg, MN Shah, HM Earl, AM Dunning, PP Pharoah e C. Caldas. "Cytochrome P450 2D6 variants and their association with breast cancer survival." In CTRC-AACR San Antonio Breast Cancer Symposium: 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-3089.
Hirakawa, Hidehiko, e Teruyuki Nagamune. "Nanoarchitechture of cytochrome P450 system using a ring-shaped protein complex". In 2010 IEEE 10th Conference on Nanotechnology (IEEE-NANO). IEEE, 2010. http://dx.doi.org/10.1109/nano.2010.5698070.
Xi, Zhian. "Overview: Some Basic Controversies and Applications of Cytochrome P450 Compound I". In ICCBB '21: 2021 5th International Conference on Computational Biology and Bioinformatics. New York, NY, USA: ACM, 2021. http://dx.doi.org/10.1145/3512452.3512464.
Rapporti di organizzazioni sul tema "Monooxygénases du cytochrome P450":
Ahsan, Habibul. Cytochrome P450-17alpha Polymorphism and Risk of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, agosto 1999. http://dx.doi.org/10.21236/ada390825.
Arnold, Frances H. Structural and Kinetic Studies of Novel Cytochrome P450 Small-Alkane Hydroxylases. Office of Scientific and Technical Information (OSTI), febbraio 2012. http://dx.doi.org/10.2172/1035499.
Loper, J. C. Third international symposium: Cytochrome P450 biodiversity. Final report, January 1, 1995--December 31, 1995. Office of Scientific and Technical Information (OSTI), marzo 1997. http://dx.doi.org/10.2172/508155.
Sherr, David H. The Aryl Hydrocarbon (Dioxin) Receptor/Transcription Factor and Cytochrome P450 1B1 as Targets for Breast Cancer Immunotherapy. Fort Belvoir, VA: Defense Technical Information Center, settembre 2002. http://dx.doi.org/10.21236/ada413137.
Alworth, William L., e David A. Mullin. Use of Genetic Engineering to Produce a Mutated Cytochrome P450 Enzyme Capable of Both Oxidizing and Reductively Dechlorinating Hazardous Organic Chemicals. Fort Belvoir, VA: Defense Technical Information Center, novembre 2000. http://dx.doi.org/10.21236/ada391816.
Amir, Rachel, David J. Oliver, Gad Galili e Jacline V. Shanks. The Role of Cysteine Partitioning into Glutathione and Methionine Synthesis During Normal and Stress Conditions. United States Department of Agriculture, gennaio 2013. http://dx.doi.org/10.32747/2013.7699850.bard.
Meidan, Rina, e Robert Milvae. Regulation of Bovine Corpus Luteum Function. United States Department of Agriculture, marzo 1995. http://dx.doi.org/10.32747/1995.7604935.bard.