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Relevant bibliographies by topics / Cytochrome P450 enzyme system

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Academic literature on the topic 'Cytochrome P450 enzyme system'

Author: Grafiati

Published: 4 June 2021

Last updated: 2 February 2022

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Journal articles on the topic "Cytochrome P450 enzyme system"

1

Marchenko, M. M., G. P. Kopylchuk, and O. V. Ketsa. "Low doses x-ray irradiation influence on liver detoxication system in rats with transplanted guerin's carcinoma." Biomeditsinskaya Khimiya 56, no. 2 (2010): 266–73. http://dx.doi.org/10.18097/pbmc20105602266.

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The activity of detoxication enzymes in liver microsomal fraction of preliminary radiation-exposed rats was investigated. It was shown that preliminary organism exposure to radiation reduced cytochrome Р450 and glutathione-S-transferase activity in liver microsomal fraction in the latent and logarithmic phases of oncogenesis compared with the unirradiated rats with tumor.Low level of cytochrome Р450 activity can be caused by transition of microsomal cytochrome P450 in P420 inactive form.The preliminary radiation does not influence the enzyme activity of liver cytochrome P450 and glutathione-S-transferase on terminal stages of Guerin's carcinoma growth.

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Correia, Maria Almira, Sheila Sadeghi, and Eduardo Mundo-Paredes. "CYTOCHROME P450 UBIQUITINATION: Branding for the Proteolytic Slaughter?" Annual Review of Pharmacology and Toxicology 45, no. 1 (September 22, 2005): 439–64. http://dx.doi.org/10.1146/annurev.pharmtox.45.120403.100127.

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The hepatic cytochromes P450 (P450s) are monotopic endoplasmic reticulum (ER)-anchored hemoproteins engaged in the enzymatic oxidation of a wide variety of endo- and xenobiotics. In the course of these reactions, the enzymes generate reactive O2 species and/or reactive metabolic products that can attack the P450 heme and/or protein moiety and structurally and functionally damage the enzyme. The in vivo conformational unraveling of such a structurally damaged P450 signals its rapid removal via the cellular sanitation system responsible for the proteolytic disposal of structurally aberrant, abnormal, and/or otherwise malformed proteins. A key player in this process is the ubiquitin (Ub)-dependent 26S proteasome system. Accordingly, the structurally deformed P450 protein is first branded for recognition and proteolytic removal by the 26S proteasome with an enzymatically incorporated polyUb tag. P450s of the 3A subfamily such as the major human liver enzyme CYP3A4 are notorious targets for this process, and they represent excellent prototypes for the understanding of integral ER protein ubiquitination. Not all the participants in hepatic CYP3A ubiquitination and subsequent proteolytic degradation have been identified. The following discussion thus addresses the various known and plausible events and/or cellular participants involved in this multienzymatic P450 ubiquitination cascade, on the basis of our current knowledge of other eukaryotic models. In addition, because the detection of ubiquitinated P450s is technically challenging, the critical importance of appropriate methodology is also discussed.

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Li, Zhong, Yuanyuan Jiang, F. Peter Guengerich, Li Ma, Shengying Li, and Wei Zhang. "Engineering cytochrome P450 enzyme systems for biomedical and biotechnological applications." Journal of Biological Chemistry 295, no. 3 (December 6, 2019): 833–49. http://dx.doi.org/10.1074/jbc.rev119.008758.

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Cytochrome P450 enzymes (P450s) are broadly distributed among living organisms and play crucial roles in natural product biosynthesis, degradation of xenobiotics, steroid biosynthesis, and drug metabolism. P450s are considered as the most versatile biocatalysts in nature because of the vast variety of substrate structures and the types of reactions they catalyze. In particular, P450s can catalyze regio- and stereoselective oxidations of nonactivated C–H bonds in complex organic molecules under mild conditions, making P450s useful biocatalysts in the production of commodity pharmaceuticals, fine or bulk chemicals, bioremediation agents, flavors, and fragrances. Major efforts have been made in engineering improved P450 systems that overcome the inherent limitations of the native enzymes. In this review, we focus on recent progress of different strategies, including protein engineering, redox-partner engineering, substrate engineering, electron source engineering, and P450-mediated metabolic engineering, in efforts to more efficiently produce pharmaceuticals and other chemicals. We also discuss future opportunities for engineering and applications of the P450 systems.

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Reed, James R., J. Patrick Connick, Dongmei Cheng, George F. Cawley, and Wayne L. Backes. "Effect of homomeric P450–P450 complexes on P450 function." Biochemical Journal 446, no. 3 (August 28, 2012): 489–97. http://dx.doi.org/10.1042/bj20120636.

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Previous studies have shown that the presence of one P450 enzyme can affect the function of another. The goal of the present study was to determine if P450 enzymes are capable of forming homomeric complexes that affect P450 function. To address this problem, the catalytic activities of several P450s were examined in reconstituted systems containing NADPH–POR (cytochrome P450 reductase) and a single P450. CYP2B4 (cytochrome P450 2B4)-, CYP2E1 (cytochrome P450 2E1)- and CYP1A2 (cytochrome P450 1A2)-mediated activities were measured as a function of POR concentration using reconstituted systems containing different concentrations of P450. Although CYP2B4-dependent activities could be explained by a simple Michaelis–Menten interaction between POR and CYP2B4, both CYP2E1 and CYP1A2 activities generally produced a sigmoidal response as a function of [POR]. Interestingly, the non-Michaelis behaviour of CYP1A2 could be converted into a simple mass-action response by increasing the ionic strength of the buffer. Next, physical interactions between CYP1A2 enzymes were demonstrated in reconstituted systems by chemical cross-linking and in cellular systems by BRET (bioluminescence resonance energy transfer). Cross-linking data were consistent with the kinetic responses in that both were similarly modulated by increasing the ionic strength of the surrounding solution. Taken together, these results show that CYP1A2 forms CYP1A2–CYP1A2 complexes that exhibit altered catalytic activity.

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Omura, Tsuneo. "Structural diversity of cytochrome P450 enzyme system." Journal of Biochemistry 147, no. 3 (January 12, 2010): 297–306. http://dx.doi.org/10.1093/jb/mvq001.

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O'Donohoe, Alan, and Michael Gill. "Pharmacogenetics of the hepatic cytochrome P450 enzyme system: its relevance for prescribing in psychiatry." Irish Journal of Psychological Medicine 15, no. 3 (September 1998): 96–99. http://dx.doi.org/10.1017/s0790966700003785.

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AbstractThis article reviews the current knowledge regarding the hepatic cytochrome P450 system, with particular reference to its effect on psychotherapeutic medication. The metabolic processes – by which drugs are broken down in the liver by cytochrome P450 enzymes – are affected by genetic variation between individuals, inhibition and induction of these enzymes by other drugs, disease and age. Genetic influences and enzyme inhibition/induction are discussed in particular detail in this article.

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McLean, K. J., A. J. Dunford, M. Sabri, R. Neeli, H. M. Girvan, P. R. Balding, D. Leys, H. E. Seward, K. R. Marshall, and A. W. Munro. "CYP121, CYP51 and associated redox systems in Mycobacterium tuberculosis: towards deconvoluting enzymology of P450 systems in a human pathogen." Biochemical Society Transactions 34, no. 6 (October 25, 2006): 1178–82. http://dx.doi.org/10.1042/bst0341178.

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An extraordinary array of P450 (cytochrome P450) enzymes are encoded on the genome of the human pathogen Mycobacterium tuberculosis (Mtb) and in related mycobacteria and actinobacteria. These include the first characterized sterol 14α-demethylase P450 (CYP51), a known target for azole and triazole drugs in yeasts and fungi. To date, only two Mtb P450s have been characterized in detail: CYP51 and CYP121. The CYP121 P450 shows structural relationships with P450 enzymes involved in synthesis of polyketide antibiotics. Both P450s exhibit tight binding to a range of azole drugs (e.g. clotrimazole and fluconazole) and the same drugs also have potent effects on growth of mycobacteria (but not of e.g. Escherichia coli). Atomic structures are available for both Mtb CYP51 and CYP121, revealing modes of azole binding and intriguing mechanistic and structural aspects. This paper reviews our current knowledge of these and the other P450 systems in Mtb including recent data relating to the reversible conversion of the CYP51 enzyme between P450 (thiolate-co-ordinated) and P420 (thiol-co-ordinated) species on reduction of the haem iron in the absence of a P450 substrate. The accessory flavoprotein and iron–sulfur proteins required to drive P450 catalysis are also discussed, providing an overview of the current state of knowledge of Mtb P450 redox systems.

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Müller-Enoch, Dieter, and Hans Gruler. "Complexation of Membrane-Bound Enzyme Systems." Zeitschrift für Naturforschung C 55, no. 9-10 (October 1, 2000): 747–52. http://dx.doi.org/10.1515/znc-2000-9-1012.

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Abstract The effect of changes in the N-terminal membrane-binding domain of cytochrome P450 forms and NADPH-cytochrome P450 reductase types on the cytochrome P450-dependent monooxygenase activities, has been examined. The nifedipine oxidase activity of two human P450 forms (CYP3A4, CYP3A4NF14) which differ only in their primary structure by ten amino acid residues in the N-terminal membrane-binding domain, yields nearly the same catalytic cycle time τ =2.65 ± 0.15 s, due to their identical cytosolic catalytic protein structure. In contrast, the complex formation process ([P450]+[reductase]↔[complex]) described by the dissociation constant KD at high substrate concentration ([S]>>KS) and low product concentration ( [ P ]<<Kp ) is determined to be KD/[P450]ᴏ = 0.3 and 2.0, respectively. These values reflect large differences in the affinity of both P450 forms for the same type of reductase which is only due to their modified membrane-binding domains. In the present work, it has been shown for the first time, that the membrane-binding domain of cytochrome P450 enzymes determines the complexation process of the binary P450:reductase system. Furthermore, the nifedipine oxidase activity of the human CYP3A4 form reconstituted with two different types of reductase from human and rabbit also has the same catalytic cycle time τ = 2.65 ± 0.15 s. This result is based on the similarity of the primary structure of the cytosolic catalytic domain of both reductase types. However, the complex was formed with different dissociation constants of KD/[P450]ᴏ = 0.3 and 4.7, respectively. This different affinity of both reductase types to the same P450 form is interpreted as a consequence of the substantial alteration of the amino acids in the N-terminal primary structure of their membrane-binding domains. 7-Ethoxycoumarin O-deethylase activity of two rat P450 forms (CYP2B1 and CYP1A1) were reconstituted with the same rat reductase. The catalytic cycle time for each P450 form is τ = 1.8 and 0.6 s, respectively. Correspondingly, the complex formation process controlled by the dissociation constant KD has changed from KD/[P450]ᴏ = 2.3 to 1.7, respectively. This is because both forms differ in their cytosolic as well as in their membranebinding domains.

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van den Brink, Hans (J ). M., Robert F. M. van Gorcom, Cees A. M. J. J. van den Hondel, and Peter J. Punt. "Cytochrome P450 Enzyme Systems in Fungi." Fungal Genetics and Biology 23, no. 1 (February 1998): 1–17. http://dx.doi.org/10.1006/fgbi.1997.1021.

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Chun, Y. J., T. Shimada, M. R. Waterman, and F. P. Guengerich. "Understanding electron transport systems of Streptomyces cytochrome P450." Biochemical Society Transactions 34, no. 6 (October 25, 2006): 1183–85. http://dx.doi.org/10.1042/bst0341183.

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Streptomyces spp. are known to produce various types of biologically active compounds including antibiotics, antiparasitic agents, herbicides and immunosuppressants. P450 (cytochrome P450) enzymes may have key roles in these biosynthetic and biotransformation reactions. Recent genomic analysis of Streptomyces coelicolor A3(2) indicates that S. coelicolor may have six ferredoxins (Fdxs), four putative Fdx reductases (FdRs) and 18 P450 genes. However, there are few clues to explain the mechanisms and functions of Streptomyces P450 systems. To solve these questions, we have expressed and purified five S. coelicolor P450s, four FdRs and six Fdxs in Escherichia coli. Of the purified P450s, CYP105D5 has fatty acid hydroxylation activity in a system reconstituted with putidaredoxin reductase and Fdx4 or with spinach FdR and spinach Fdx, although the reconstitutions with FdR2 or FdR3 and any of the Fdxs did not support CYP105D5-catalysed oleic acid hydroxylation. Elucidation of the detailed mechanisms of electron transport system for Streptomyces P450 may provide the perspective for usefulness of P450s as a biocatalyst.

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Dissertations / Theses on the topic "Cytochrome P450 enzyme system"

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Henne, Kirk R. "The active site characteristics of the cytochrome P450 4B1 bioactivation enzyme /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/8159.

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Bertrand-Thiébault, Céline. "Cytochromes P450 et tonus vasculaire." Nancy 1, 2004. https://tel.archives-ouvertes.fr/tel-00120305.

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Les cytochromes P450 (CYP) sont des enzymes dont le rôle principalement connu est la détoxification. Cependant leur activité peut conduire à la formation de métabolites ayant des effets pharmacologiques, toxicologiques ou physiologiques. Depuis quelques années le rôle des cytochromes P450 dans le métabolisme de l'acide arachidonique est bien décrit. Parmi les métabolites produits lors de cette biotranformation, les acides epoxyeicosatriènoi͏̈ques (les EETs) et les acides hydroxyeicosatetraènoi͏̈ques (les HETEs ) occupent une place importante dans la régulation du tonus vasculaire. Ainsi les EETs ont des propriétés vasodilatatrices tandis que les HETEs ont des propriétés surtout vasoconstrictrices. Au cours de ce travail, nous avons étudié l'expression de certains cytochromes P450 dans les veines saphènes humaines et nous avons caractérisé le profil d'expression de ces enzymes dans différents types cellulaires contenus dans les parois vasculaires. Nous avons montré que l'expression de la plupart des cytochromes P450 notamment CYPlBl, CYP2C, CYP2El, CYP2J2 et CYP3A était augmentée dans les échantillons de veines pathologiques humaines. Nous avons ensuite étudié dans une lignée de cellules endothéliales humaines (ECV304) et une lignée d'hépatomes d'origine humaine (HepG2), la régulation par quelques statines de certains cytochromes P450 dont les CYP2C, occupant une place importante dans la régulation de l'homéostasie vasculaire. Les statines sont des molécules utilisées dans le traitement de l'hypercholestérolémie présentant des effets plei͏̈otropiques notamment sur l'état vasculaire. Nous avons observé que l'atorvastatine était la molécule ayant le plus d'effet sur l'expression des cytochromes P450 2C8, 2C9, 2J2, 3AS et 3A7. En effet, cette molécule diminue l'expression des différents cytochromes P450 dans les cellules ECV304 alors qu'elle augmente leur expression dans les cellules HepG2. Les statines influencent également l'expression de deux types de récepteurs nucléaires impliqués dans la régulation des cytochromes P450. Ainsi, la fluvastatine augmente l'expression des récepteurs nucléaires CAR et PXR. Enfin, nous avons étudié l'effet du polymorphisme d'un cytochrome P450 de la famille 2C sur la pression sanguine et sur les marqueurs inflammatoires des pathologies cardiovasculaires. Nous avons observé que les valeurs de pressions sanguines ne variaient pas en fonction du polymorphisme de CYP2Cl9. En revanche, les taux plasmatiques d'interleukine-6 sont plus élevés chez les porteurs de l'allèle muté de CYP2Cl9*2. De la même façon, les taux plasmatiques des paramètres lipidiques tels que les triglycérides sont également plus élevés chez les mêmes sujets. Ainsi, une modification de l'expression des cytochromes P450 peut jouer un rôle dans la pathologie variqueuse et dans la pathologie vasculaire à composante inflammatoire. Cette expression peut être modulée par les statines. Enfin, le polymorphisme CYP2Cl9*2 est corrélé avec la composante inflammatoire des pathologies variqueuses probablement par l'intermédiaire des métabolites de l'acide arachidonique. Ces résultats posent alors la question de la modulation de la production des molécules vaso-actives issues de l'acide arachidonique dans les pathologies vasculaires et d'éventuels traitements par les molécules inhibitrices de l'HMGCoA réductase ou par des inhibiteurs de cytochromes P450.

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McConn, Donavon J. "Metabolic and inhibitory differences between cytochromes P450 3A4 and 3A5 /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/7980.

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Westlind, Johnsson Anna. "Pharmacogenetics of human cytochrome P450 3A (CYP3A) enzymes /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-688-x.

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Liu, Kang-Cheng. "Influence of lipid membrane environment on the kinetics of the cytochrome P450 reductase- cytochrome P450 3A4 enzyme system in nanodiscs." Thesis, University of Manchester, 2017. https://www.research.manchester.ac.uk/portal/en/theses/influence-of-lipid-membrane-environment-on-the-kinetics-of-the-cytochrome-p450-reductase-cytochrome-p450-3a4-enzyme-system-in-nanodiscs(b8ee4e84-1230-40cf-9b98-b5d6f457f54c).html.

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The cytochrome P450 enzyme system is a multicomponent electron-transfer chain composed of a haem-containing monooxygenase cytochrome P450 (CYP) and one or more redox partners. Eukaryotic CYPs and their redox partner NADPH-dependent cytochrome P450 oxidoreductase (CPR) are involved in many biological processes. Each protein has one N- terminal membrane anchor domain for location within the endoplasmic reticulum (ER). In mammals, CYPs and CPR are especially abundant in liver cells, where they play important roles in the metabolism of steroids, fatty acids, and xenobiotic compounds including numerous drugs of pharmaceutical importance. Incorporation into lipid membranes is an important aspect of CYP and CPR function, influencing their kinetic properties and interactions. In this thesis, soluble nanometer-scale phospholipid bilayer membrane discs, "nanodiscs", were used as a reconstitution system to study the influence of lipid membrane composition on the activities of the abundant human CYP3A4 and human CPR. Both enzymes were expressed and purified from bacteria, and assembled into functionally active membrane-bound complexes in nanodiscs. Nanodisc assembly was assessed by a combination of native and denaturing gel electrophoresis, and a fluorimetric assay was developed to study CYP3A4 reaction kinetics using 7-benzyloxyquinoline as substrate. Kinetic properties were investigated with respect to different lipid membrane compositions: phosphatidyl choline; a synthetic lipid mixture resembling the ER; and natural lipids extracted from liver microsomes. Full activity of the CYP3A4 system, with electron transfer from NADPH via CPR, could only be reconstituted when both CYP3A4 and CPR were membrane-bound within the same nanodiscs. No activity was observed when CPR and CYP3A4 were each incorporated seperately into naodiscs then mixed together, or when soluble forms of CPR were mixed with pre-assembled CYP3A4-nanodiscs. Thus, assembly of the two proteins within the same membrane was shown to be essential for the function of the CPR-CYP3A4 electron transfer system. Comparison of the reaction kinetics in different membrane compositions revealed liver microsomal lipid to have an enhancing effect both on the activity of the assembled CPR-CYP3A4 nanodisc complex, and on the activity of CPR alone incorporated in nanodiscs, when compared either to the synthetic lipid mixture or to phosphatidyl choline alone. Thus, natural lipids appear to possess properties or include components important for the catalytic function of the CYP system, which are absent from synthetic lipid. Input of electrons, measured by NADPH consumption, exceeded product formation rate by the CPR-CYP3A4 complex in nanodiscs, indicating "leakage" in the electron flow, possibly due to uncoupling of the two enzymes. Uncoupling was shown to occur by developing a novel fluorimetric method using the dye MitSOX to detect superoxide production. The significance of this, and to what extent control of coupling could be a natural means of regulation of the CPR-CYP system, remains to be determined. Thus, phospholipid bilayer nanodiscs prove a powerful tool to enable detailed analysis of the reaction kinetics of membrane-reconstituted CPR-CYP systems, and to allow pertinent questions to be addressed concerning the integral significance of the membrane environment.

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Hidestrand, Mats. "Structure and function of hepatic cytochromes P450 - implications for drug development /." Stockholm, 2002. http://diss.kib.ki.se/2002/91-7349-418-6/.

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Wennerholm, Agneta. "Characteristics of cytochrome P450-catalysed drug metabolism with focus on a black Tanzanian population /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-697-9/.

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Modarai, Maryam. "Interactions of echinacea liquid preparations and selected constituents with the cytochrome P450 enzyme system." Thesis, University College London (University of London), 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.500092.

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Kabulski, Jarod L. "Development of Au-immobilized P450 platform for exploring the effect of oligomer formation on P450-mediated metabolism for In vitro to In vivo drug metabolism predictions." Morgantown, W. Va. : [West Virginia University Libraries], 2010. http://hdl.handle.net/10450/10892.

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Thesis (Ph. D.)--West Virginia University, 2010.
Title from document title page. Document formatted into pages; contains xiv, 180 p. : ill. (some col.). Includes abstract. Includes bibliographical references.

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Larbat, Romain Bourgaud Frédéric. "Contribution à l'étude des P450 impliqués dans la biosynthèse des furocoumarines." S. l. : S. n, 2006. http://www.scd.inpl-nancy.fr/theses/2006_LARBAT_R.pdf.

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Books on the topic "Cytochrome P450 enzyme system"

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Paul R. Ortiz de Montellano, Ian R. Phillips, and Elizabeth A. Shephard. Cytochrome P450 protocols. 3rd ed. New York: Humana, 2013.

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Ahlström, Marie. Cytochrome P450, metabolism and inhibition: Computational and experimental studies. Göteborg: Göteborg University, 2007.

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International Conference on Cytochrome P-450 (15th 2007 Bled, Slovenia). Proceedings of the 15th International Conference on Cytochromes P450: Biochemistry, biophysics, and functional genomics : Bled, Slovenia, June 17-21, 2007. Bologna, Italy: Medimond International Proceedings, 2007.

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Cozza, Kelly L. Concise guide to the cytochrome P450 system: Drug interaction principles for medical practice. Washington, DC: American Psychiatric Pub., 2001.

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Zhang, Yanhua. Effects of steroid hormones on cytochrome P450 enzyme activity in women. Ottawa: National Library of Canada, 2002.

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Wilson, Joanna Yvonne. Cytochrome P450 1A1 and aromatase (CYP19) in cetaceans: Enzyme expression and relationship to contaminant exposure. Cambridge, Mass: Massachusetts Institute of Technology, 2003.

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Cozza, Kelly L. Quick guide to the Cytochrome P450 system: Overview of drug interaction principles. Washington, DC: American Psychiatric Pub., 2002.

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International, Conference on Biochemistry and Biophysics of Cytochrome P.-450 (6th 1988 :. Vienna Austria). Cytochrome P-450: Biochemistry and biophysics : proceedings of the 6th International Conference on Biochemisty and Biophysics of Cytochrome P-450 held in Vienna at the University of Economics, July 3-8, 1988. London: Taylor & Francis, 1989.

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Worrall, Stephen Frederick. An investigation into the association between cytochrome P450 and glutathione S-transferase detoxification enzyme polymorphisms and human oral squamous cell carcinoma. Birmingham: University of Birmingham, 1998.

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1946-, Bachmanova G. I., ed. Cytochrome P-450 and active oxygen. London: Taylor & Francis, 1990.

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Book chapters on the topic "Cytochrome P450 enzyme system"

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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.

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Urlacher, Vlada B., and Sebastian Schulz. "Multi-Enzyme Systems and Cascade Reactions Involving Cytochrome P450 Monooxygenases." In Cascade Biocatalysis, 87–132. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527682492.ch5.

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Crespi, C. L., R. Langenbach, H. V. Gelboin, F. J. Gonzalez, and B. W. Penman. "Human Cells as an Expression System for Cytochromes P450." In Assessment of the Use of Single Cytochrome P450 Enzymes in Drug Research, 111–34. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-03019-6_7.

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Kühn-Velten, W. N. "Cytochrome P450c17: Regulation of Gene Expression and Enzyme Function at the Bifurcation in Steroid Hormone Synthesis." In Cytochrome P450, 667–76. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77763-9_43.

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Schenkman, J. B. "Historical Background and Description of the Cytochrome P450 Monooxygenase System." In Cytochrome P450, 3–13. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77763-9_1.

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Ortiz de Montellano, Paul R. "The Cytochrome P450 Oxidative System." In Handbook of Drug Metabolism, 57–82. Third edition / [edited by] Paul G. Pearson, Larry C. Wienkers.: CRC Press, 2019. http://dx.doi.org/10.1201/9780429190315-3.

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Reed, James R. "The Use of Liposomes in the Study of Drug Metabolism: A Method to Incorporate the Enzymes of the Cytochrome P450 Monooxygenase System into Phospholipid, Bilayer Vesicles." In Methods in Molecular Biology, 11–20. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-447-0_2.

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Rabe, Kersten S., and Christof M. Niemeyer. "Screening for Cytochrome P450 Reactivity with a Reporter Enzyme." In Methods in Molecular Biology, 149–56. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-321-3_13.

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Warner, Margaret, and Jan-Åke Gustafsson. "Cytochrome P450 in the Central Nervous System." In Neurosteroids, 51–65. Totowa, NJ: Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-693-5_3.

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Obach, R. Scott, Odette A. Fahmi, and Robert L. Walsky. "Inactivation of Human Cytochrome P450 Enzymes and Drug–Drug Interactions." In Enzyme- and Transporter-Based Drug-Drug Interactions, 473–95. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-0840-7_19.

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Conference papers on the topic "Cytochrome P450 enzyme system"

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Shoemaker, James T., and Jelena Vukasinovic. "Abstract 4080: Cytochrome P450 enzyme activity is enhanced in hepatocytes grown using a perfused 3D cell culture drug screening system." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-4080.

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Özgen, İlker Tolga, Esra Kutlu, Hatice Nursoy, Yaşar Cesur, and 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.

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Krivec, Matic, Raimund Leitner, Florian Überall, and Johannes Hochleitner. "Inkjet-printed selective microfluidic biosensor using CNTs functionalized by cytochrome P450 enzyme." In SPIE Microtechnologies, edited by Sander van den Driesche, Ioanna Giouroudi, and Manuel Delgado-Restituto. SPIE, 2017. http://dx.doi.org/10.1117/12.2264095.

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Li, Yanfang, Kenneth A. Bachmann, and Brent D. Cameron. "In vivo cytochrome P450 drug metabolizing enzyme characterization using surface-enhanced Raman spectroscopy." In Biomedical Optics 2003, edited by Alexander P. Savitsky, Darryl J. Bornhop, Ramesh Raghavachari, and Samuel I. Achilefu. SPIE, 2003. http://dx.doi.org/10.1117/12.478394.

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Hirakawa, Hidehiko, and 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.

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Chachibaia, Tamar, and Joy Hoskeri. "In silico computer simulation risk assessment of triazole fungicides on human cytochrome p450 aromatase enzyme: cyp19a1 inhibition by triazoles using autodock software." In MOL2NET, International Conference on Multidisciplinary Sciences. Basel, Switzerland: MDPI, 2015. http://dx.doi.org/10.3390/mol2net-1-f002.

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Wooten, Jonathan V., Shaniece Wauchope, Nicole Mavingire, Petreena Campbell, JéAnn Watson, Maxine Gossell-Williams, Rupika Delgoda, and Eileen Brantley. "Abstract C126: Plant isolate dibenzyl trisulfide potently inhibits cytochrome P450 1 enzyme activity and the growth of breast cancer cells derived from African American patients." In Abstracts: Eleventh AACR Conference on The Science of Cancer Health Disparities in Racial/Ethnic Minorities and the Medically Underserved; November 2-5, 2018; New Orleans, LA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7755.disp18-c126.

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MacLean, Mandy, Kevin White, and Anne Katrine Johansen. "The Estrogen-Metabolising Enzyme, Cytochrome P450 1B1 Influences The Development Of Exaggerated Hypoxia-Induced Pulmonary Arterial Hypertension In Female Mice Over-Expressing The Serotonin Transporter." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a6520.

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Wernet, P., M. Haurand, W. Nüsing, E. M. Schneider, K. Jaschonek, and V. Ullrich. "Production and characterization of a murine monoclonal antibody against human thromboxane synthetase." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643382.

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Abstract:

Eicosanoids appear to have an important role in the actual momentary regulation of tissue blood flow. The function of constricting blood vessels by affecting the vascular tone has been assigned to thromboxane. Thromboxane synthetase, the enzyme responsible for the conversion of Prostaglandin-H2 into thromboxane A2, has been shown to be present in platelets, lung fibroblasts and the brain. Recently, thromboxane synthetase has been totally purified. The enzyme isolated from platelets appears to have a molecular weight of 58,800 Dalton and to belong to the group of cytochrome P450 proteins. In order to make a monoclonal antibody against thromboxane synthetase, BALB/c mice were injected four times i.m. with 10, 5, 5 and 4 μg of the platelet purified enzyme in complete Freund's adjuvant. The serum antibody titer against thromboxane synthetase in an ELISA was higher than 1:1000 after the second boost. One mouse received a fifth i.v. injection of 10 μg of the purified enzyme. One monoclonal antibody of the several hundreds of hybridomas screened in an ELISA revealed specific activity against thromboxane synthetase with a titer of 1:512 present in the culture supernatant. After recloning this reagent, called T0300, was used for the preparation of an immunoaffinity column, where it also reacted specifically. In immunoprecipitation experiments T0300 was able to precipitate a 58,000 D molecule. Also the biological activity of thromboxane synthetase could be blocked by monoclonal antibody T0300. In addition this reagent was employed in indirect immunofluorescence on leukemic cells employing a FACS IV cytofluorometer. Here specific staining of two megacaryocytic blast cell populations could be demonstrated. Thus T0300 appears to be a monoclonal antibody against human thromboxane synthetase.

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Shishkin, Viktor, Galina Kudriavtseva, Yuri Malenkov, and Viktor V. Shishkin. "AB0128 ANTIOXIDATIVE PROTECTION AND MONOXIGENASE SYSTEM ACTIVITY OF CYTOCHROME P450 (MOG) OF NEUTROPHYLIC LEUKOCYTES (NL) FROM SYNOVIAL FLUID (SF) IN RHEUMATOID ARTHRITIS (RA)." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.836.

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Reports on the topic "Cytochrome P450 enzyme system"

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Alworth, William L., and 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, November 2000. http://dx.doi.org/10.21236/ada391816.

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