Relevant bibliographies by topics / Oxidation with P450 enzymes

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Academic literature on the topic 'Oxidation with P450 enzymes'

Author: Grafiati
Published: 4 June 2021
Last updated: 16 February 2022

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Journal articles on the topic "Oxidation with P450 enzymes"

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Cryle, Max J., Jeanette E. Stok, and James J. De Voss. "Reactions Catalyzed by Bacterial Cytochromes P450." Australian Journal of Chemistry 56, no. 8 (2003): 749. http://dx.doi.org/10.1071/ch03040.

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The cytochromes P450 are a large family of oxidative haemoproteins that are responsible for a wide variety of oxidative transformations in a variety of organisms. This review focuses upon the reactions catalyzed specifically by bacterial enzymes, which includes aliphatic hydroxylation, alkene epoxidation, aromatic hydroxylation, oxidative phenolic coupling, heteroatom oxidation and dealkylation, and multiple oxidations including C–C bond cleavage. The potential for the practical application of the oxidizing power of these enzymes is briefly discussed.
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Fasan, Rudi. "Tuning P450 Enzymes as Oxidation Catalysts." ACS Catalysis 2, no. 4 (March 20, 2012): 647–66. http://dx.doi.org/10.1021/cs300001x.

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Frank, Daniel J., Yarrow Madrona, and Paul R. Ortiz de Montellano. "Cholesterol Ester Oxidation by Mycobacterial Cytochrome P450." Journal of Biological Chemistry 289, no. 44 (September 10, 2014): 30417–25. http://dx.doi.org/10.1074/jbc.m114.602771.

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Mycobacteria share a common cholesterol degradation pathway initiated by oxidation of the alkyl side chain by enzymes of cytochrome P450 (CYP) families 125 and 142. Structural and sequence comparisons of the two enzyme families revealed two insertions into the N-terminal region of the CYP125 family (residues 58–67 and 100–109 in the CYP125A1 sequence) that could potentially sterically block the oxidation of the longer cholesterol ester molecules. Catalytic assays revealed that only CYP142 enzymes are able to oxidize cholesteryl propionate, and although CYP125 enzymes could oxidize cholesteryl sulfate, they were much less efficient at doing so than the CYP142 enzymes. The crystal structure of CYP142A2 in complex with cholesteryl sulfate revealed a substrate tightly fit into a smaller active site than was previously observed for the complex of CYP125A1 with 4-cholesten-3-one. We propose that the larger CYP125 active site allows for multiple binding modes of cholesteryl sulfate, the majority of which trigger the P450 catalytic cycle, but in an uncoupled mode rather than one that oxidizes the sterol. In contrast, the more unhindered and compact CYP142 structure enables enzymes of this family to readily oxidize cholesteryl esters, thus providing an additional source of carbon for mycobacterial growth.
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Mirzaei, Saber, Avat Arman Taherpour, and Shahryar Mohamadi. "Mechanistic study of allopurinol oxidation using aldehyde oxidase, xanthine oxidase and cytochrome P450 enzymes." RSC Advances 6, no. 111 (2016): 109672–80. http://dx.doi.org/10.1039/c6ra19197e.

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The oxidation reaction of allopurinol to its active metabolite (oxypurinol) is investigated using the AO and P450 enzymes. To the contrary of AO (and XO), the P450 enzyme can metabolize the allopurinol with a not self-inhibitory mechanism.
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McLean, Kirsty J., Marcus Hans, and Andrew W. Munro. "Cholesterol, an essential molecule: diverse roles involving cytochrome P450 enzymes." Biochemical Society Transactions 40, no. 3 (May 22, 2012): 587–93. http://dx.doi.org/10.1042/bst20120077.

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Cholesterol is an essential molecule for eukaryotic life and is an important precursor for a wide range of physiological processes. Biosynthesis and homoeostasis of cholesterol are complex mechanisms that are tightly regulated and interlinked with activities of a number of cytochrome P450 enzymes. These P450s play central critical roles in cholesterol metabolism. Key roles include a rate-limiting reaction in the synthesis of cholesterol itself, and in the oxidative transformations of cholesterol into steroid hormones and bile acids. However, microbial P450s also have important roles that impinge directly on human cholesterol synthesis and oxidation. Recent data reveal that Mycobacterium tuberculosis (which infects more than one-third of the world's human population) uses P450s to initiate breakdown of host cholesterol as an energy source. Microbial P450s also catalyse industrially important transformations in the synthesis of cholesterol-lowering statin drugs, with clear benefits to humans. The present article reviews the various roles of P450s in human cholesterol metabolism, from endogenous P450s through to microbial oxidases that enable catabolism of human cholesterol, or facilitate production of statins that regulate cholesterol production with positive outcomes in cardiovascular disease.
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Gillam, Elizabeth M. J., Lisa M. Notley, Hongliang Cai, James J. De Voss, and F. Peter Guengerich. "Oxidation of Indole by Cytochrome P450 Enzymes†." Biochemistry 39, no. 45 (November 2000): 13817–24. http://dx.doi.org/10.1021/bi001229u.

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Harken, Lauritz, and Shu-Ming Li. "Modifications of diketopiperazines assembled by cyclodipeptide synthases with cytochrome P450 enzymes." Applied Microbiology and Biotechnology 105, no. 6 (February 24, 2021): 2277–85. http://dx.doi.org/10.1007/s00253-021-11178-1.

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Abstract2,5-Diketopiperazines are the smallest cyclic peptides comprising two amino acids connected via two peptide bonds. They can be biosynthesized in nature by two different enzyme families, either by nonribosomal peptide synthetases or by cyclodipeptide synthases. Due to the stable scaffold of the diketopiperazine ring, they can serve as precursors for further modifications by different tailoring enzymes, such as methyltransferases, prenyltransferases, oxidoreductases like cyclodipeptide oxidases, 2-oxoglutarate-dependent monooxygenases and cytochrome P450 enzymes, leading to the formation of intriguing secondary metabolites. Among them, cyclodipeptide synthase-associated P450s attracted recently significant attention, since they are able to catalyse a broader variety of astonishing reactions than just oxidation by insertion of an oxygen. The P450-catalysed reactions include hydroxylation at a tertiary carbon, aromatisation of the diketopiperazine ring, intramolecular and intermolecular carbon-carbon and carbon-nitrogen bond formation of cyclodipeptides and nucleobase transfer reactions. Elucidation of the crystal structures of three P450s as cyclodipeptide dimerases provides a structural basis for understanding the reaction mechanism and generating new enzymes by protein engineering. This review summarises recent publications on cyclodipeptide modifications by P450s.Key Points• Intriguing reactions catalysed by cyclodipeptide synthase-associated cytochrome P450s• Homo- and heterodimerisation of diketopiperazines• Coupling of guanine and hypoxanthine with diketopiperazines Graphical abstract
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Uehara, Shotaro, Toru Oshio, Kazuyuki Nakanishi, Etsuko Tomioka, Miyu Suzuki, Takashi Inoue, Yasuhiro Uno, Erika Sasaki, and Hiroshi Yamazaki. "Survey of Drug Oxidation Activities in Hepatic and Intestinal Microsomes of Individual Common Marmosets, a New Nonhuman Primate Animal Model." Current Drug Metabolism 20, no. 2 (April 30, 2019): 103–13. http://dx.doi.org/10.2174/1389200219666181003143312.

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Background: Common marmosets (Callithrix jacchus) are potentially useful nonhuman primate models for preclinical studies. Information for major drug-metabolizing cytochrome P450 (P450) enzymes is now available that supports the use of this primate species as an animal model for drug development. Here, we collect and provide an overview of information on the activities of common marmoset hepatic and intestinal microsomes with respect to 28 typical human P450 probe oxidations. Results: Marmoset P450 2D6/8-dependent R-metoprolol O-demethylation activities in hepatic microsomes were significantly correlated with those of midazolam 1′- and 4-hydroxylations, testosterone 6β-hydroxylation, and progesterone 6β-hydroxylation, which are probe reactions for marmoset P450 3A4/5/90. In marmosets, the oxidation activities of hepatic microsomes and intestinal microsomes were roughly comparable for midazolam and terfenadine. Overall, multiple forms of marmoset P450 enzymes in livers and intestines had generally similar substrate recognition functionalities to those of human and/or cynomolgus monkey P450 enzymes. Conclusion: The marmoset could be a model animal for humans with respect to the first-pass extraction of terfenadine and related substrates. These findings provide a foundation for understanding individual pharmacokinetic and toxicological results in nonhuman primates as preclinical models and will help to further support understanding of the molecular mechanisms of human P450 function.
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Murphy, Sharon E., Vytautas Raulinaitis, and Kathryn M. Brown. "NICOTINE 5′-OXIDATION AND METHYL OXIDATION BY P450 2A ENZYMES." Drug Metabolism and Disposition 33, no. 8 (April 28, 2005): 1166–73. http://dx.doi.org/10.1124/dmd.105.004549.

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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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Dissertations / Theses on the topic "Oxidation with P450 enzymes"

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Urata, Kouji. "Hydrogen-driven hydrocarbon oxidation by cytochrome P450 enzymes." Thesis, University of Oxford, 2017. https://ora.ox.ac.uk/objects/uuid:d5ec728a-2aa8-4040-92b0-56dad59e6dc4.

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P450BM3 (CYP102A1) from Bacillus megaterium is a 119 kDa, 1,046-residue polypeptide with the FAD/FMN reductase domain fused to the C-terminus of the haem domain and, as such it is catalytically self-sufficient; only NADPH and oxygen are required for monooxygenase activity. P450BM3 is a sub-terminal fatty acid hydroxylase, but generations of CYP102A1 engineering allowed them to be used in, e.g. drug metabolism and alkane oxidation. This thesis describes protein engineering of P450BM3 and altering reaction conditions to enhance C1 – C8 alkane oxidation activities, with the long-term goal of oxidising methane, and using the hydrogen-driven cofactor regeneration system to drive these reactions. Catalytic hydrocarbon oxidation under mild conditions is highly desirable in fuel synthesis and energy applications. Methane is a greenhouse gas and its effect can be minimised if methane is selectively oxidised to methanol, which can be used as a liquid fuel or feedstock. The R47L/Y51F, KT2, I401P and A330P mutants, which previously showed higher activities for a wide range of substrates, were used as templates to build a library of mutants. The R47L/Y51F/KT2/A330P mutant (RT2/AP) showed total turnover number (TTN) of 680 ± 10 under atmospheric pressure at ambient temperature for propane oxidation, and the TTN improved by 16-fold under 5 bar propane pressure (TTN is defined as the maximum number of moles of substrate converted per mole of P450BM3). TTN values of 14,250 ± 1,370 (KU4/AP) and 920 ± 50 (KU3/AP) were observed under 5 bar propane and 8 bar ethane, respectively, at ambient temperature. The effect of adding an inert perfluorocarboxylic acid (PFC), which resembles the structures of natural substrates and constrains small alkanes to bind closer to the haem, was investigated. The R47L/Y51F/N70S/M237L/A328V mutant (RL/YF/NMA) with PFC11 gave a TTN of 13,590 ± 30 under 5 bar propane at ambient temperature. Higher TTNs of 26,320 ± 1,010 for propane and 1,440 ± 70 for ethane oxidation were observed for the RL/YF/NMA mutant at 4 °C due to improved aqueous alkane solubility. Octane and propane oxidations were performed using a hydrogen-driven NADP+ recycling system without changing the selectivity of products, although the observed propane oxidation activity was 15% of the glucose/GDH cofactor recycling system.
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Larsen, Aaron. "Harnessing the power of P450 enzymes: a chemical auxiliary-based approach to predictable P450 oxidations at inactivated C-H bonds." Thesis, McGill University, 2012. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=107745.

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Enantioselective hydroxylation of one specific methylene in the presence of many similar groups is debatably the most challenging chemical transformation. Although chemists have recently made progress towards the hydroxylation of inactivated C-H bonds, enzymes like P450s (CYPs) remain unsurpassed in specificity and scope. The substrate promiscuity of many P450s is desirable for synthetic applications; however, the inability to predict the products of these enzymatic reactions and the poor activity and stability of these enzymes is impeding advancement. In chapter 2 of this thesis, we evaluate several strategies to improve the activity and stability of CYP3A4. These strategies include the immobilization of CYP3A4 inside molecular hydrogels and silica in addition to the chemical modification of CYP3A4 using various anhydrides. Although none of the strategies we investigate here greatly enhance the catalytic utility of the enzyme, CYP3A4 is shown to be highly tolerant to functionalization at a large number of surface residues and to the presence of extremely high concentrations of silica during catalysis. Recognizing the potential for enzymes containing small, hydrophobic active sites to catalyze Diels-Alder reactions, chapter 3 describes the design and application of several assays to evaluate the Diels-Alderase activity of CYP2E1. Although the presence of CYP2E1 is not found to increase the rates of the reactions we investigate here, the results do demonstrate that there is an interaction between one or more of the substrates and the enzyme at either the active site or at another binding pocket. In chapter 4, we evaluate 4 auxiliaries for their ability to direct CYP3A4 oxidations. When linked to substrates, several of these auxiliaries are shown to direct CYP3A4 oxidations at specific C-H bonds. Although the auxiliaries we explore here are found to be limited in utility, several important lessons are learned which we apply to the design of a next generation auxiliary to be discussed in the following chapter. In chapter 5, we demonstrate the utility of theobromine as a chemical auxiliary to control the selectivity of CYP3A4 reactions. When linked to substrates, inexpensive, achiral theobromine directs the reaction to produce hydroxylation or epoxidation at the fourth carbon from the auxiliary with pro-R facial selectivity. This strategy provides a versatile yet controllable system for regio-, chemo- and stereo-selective oxidations at inactivated C-H bonds and establishes the utility of directing auxiliaries to mediate the activity of highly promiscuous enzymes. Recognizing the importance of product recovery, chapter 6 evaluates molecularly imprinted polymers for the selective purification of theobromine-containing molecules. When used for the solid-phase extraction, these materials allow for the near complete recovery of theobromine-containing products and starting materials from biocatalytic mixtures. This strategy represents an easily-tailored, effective, and reusable method of improving the recovered yield of theobromine-directed CYP3A4 oxidations.
L'hydroxylation énantiosélective d'un méthylène spécifique en présence de nombreux autres groupes semblables est défendablement la transformation chimique la plus difficile. Bien que les chimistes aient récemment fait du progrès vers l'hydroxylation de liaisons C-H inactivées, il existe des enzymes comme les cytochromes P450 (CYP) qui demeurent inégalées par rapport à leur spécificité et leur portée. La promiscuité de substrat démontré par plusieurs P450 est souhaitable pour certaines applications de synthèse, mais une prévisibilité des produits difficiles, en plus de leur faible activité et stabilité empêchent l'avancement dans ce domaine. Dans le chapitre 2 de cette thèse, nous évaluons plusieurs stratégies pour améliorer l'activité et la stabilité de CYP3A4. Ces stratégies comprennent son immobilisation à l'intérieur d'hydrogels moléculaire et de silice, en plus de sa modification chimique avec une variété d'anhydrides. Bien qu'aucunes des stratégies étudiées ici n'aient grandement amélioré l'utilité catalytique de l'enzyme, elles démontrent quand-même que CYP3A4 est très tolérantes envers la fonctionnalisation d'un grand nombre de ses résidus de surface et à la présence de concentrations extrêmement élevées de silice pendant la catalyse. Reconnaissant le potentiel des enzymes possédant de petits sites actifs hydrophobes de catalyser des réactions Diels-Alder, chapitre 3 décrit la conception et l'application de plusieurs tests pour évaluer l'activité Diels-Alderase de CYP2E1. Bien que la présence de CYP2E1 n'a pas augmenter le taux des réactions étudiées ici, les résultats démontrent qu'il existe une interaction entre un ou plusieurs des substrats et l'enzyme, soit au site actif ou à un autre poche de liaison.Dans le chapitre 4, nous évaluons quatre auxiliaires pour leur capacité de diriger des oxydations par CYP3A4. Quand ils sont reliés à des substrats, nous avons trouvé que plusieurs de ces auxiliaires dirigent les oxydations par CYP3A4 à des liaisons C-H spécifiques. Bien que les auxiliaires explorés ici se trouvent à être limitées dans leur utilité, nous avons appris plusieurs leçons importantes que nous avons appliqué envers la conception d'une nouvelle génération d'auxiliaires à être discutés dans le chapitre suivant. Dans le chapitre 5, nous démontrons l'utilité de la théobromine en tant qu'auxiliaires chimique pour contrôler la sélectivité des réactions du CYP3A4. Quand il est relié à des substrats peu coûteux, la théobromine achiral dirige la réaction, donnant naissance à des produits hydroxylés ou époxydés au niveau du quatrième carbone à partir de l'auxiliaire avec une sélectivité faciale pro-R. Cette stratégie fournit un système versatile et contrôlable offrant des produits oxydés de façon regio-, chimio- et stéréo-sélective à des liaisons CH inactivé. Elle démontre aussi l'utilité des auxiliaires par rapport à leur habileté de contrôler l'activité des enzymes hautement promiscues. Reconnaissant l'importance de la récupération du produit, le chapitre 6 évalue des polymères à empreintes moléculaires pour la purification sélective de molécules contenant la théobromine. Quand ils sont utilisés pour l'extraction en phase solide, ces matériaux permettent la récupération quasi-complète de produits et de substrats contenant la théobromine à partir de mélanges biocatalytiques. Cette stratégie représente une méthode adaptable, efficace et réutilisable permettant d'améliorer le rendement récupéré des produits d'oxydations dirigée par la théobromine.
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Rodriguez, Patricia Fernandez. "Streamlined synthesis of taxol analogues." Thesis, University of Oxford, 2017. https://ora.ox.ac.uk/objects/uuid:58d4a7f3-038e-4c4a-9aec-67267277670f.

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This thesis centres on the synthesis of taxol analogues via late-stage hydroxylation with P450 enzymes. To accomplish this, the taxane core, specifically taxa-4(5),11(12)-dien-2-one, was synthesised by classical synthetic methods, and subsequently oxidised using P450BM3 mutants. Chapter 1 introduces enzymatic catalysis, and the advantages and disadvantages of its application to organic synthesis. Additionally, an overview of taxol, including its discovery, mode of action, biosynthesis and large-scale production, and a summary of the previously reported approaches to the taxane core are described. Chapter 2 details the problems encountered and solutions implemented when reproducing Baran's route to taxa-4(5),11(12)-dien-2-one. Furthermore, approaches to some of its intermediates and an alternative route to taxa-4(5),11(12)-dien-2-one, which is based on Baran's, are discussed. Chapter 3 describes the development of a new, practical and short synthetic route to taxa-4(5),11(12)-dien-2-one which, ultimately, led to 1,3-di-epi-taxa-4(5),11(12)-dien-2-one. Additionally, the application of this route to the synthesis of a model compound and attempts to convert this racemic synthesis into an enantioselective route are reported. Finally, the enzymatic oxidation of taxa-4(5),11(12)-dien-2-one and related molecules using P450BM3 mutants is explored in Chapter 4. A preliminary study to determine the substrate enantioselectivity of the mutants is also described, along with the biological assays of the oxidised compounds produced during the study.
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Celik, Haydar. "Enzyme-catalyzed Reductive Activation Of Anticancer Drugs Idarubicin And Mitomycin C." Phd thesis, METU, 2008. http://etd.lib.metu.edu.tr/upload/3/12609247/index.pdf.

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Idarubicin (IDA) and mitomycin C (MC) are clinically effective quinone-containing anticancer agents used in the treatment of several human cancers. Quinone-containing anticancer drugs have the potential to undergo bioreduction by oxidoreductases to reactive species, and thereby exert their cytotoxic effects. In the present study, we investigated, for the first time, the potential of IDA, in comparison to MC, to undergo reductive activation by NADPH-cytochrome P450 reductase (P450R), NADH-cytochrome b5 reductase (b5R) and P450R-cytochrome P4502B4 (CYP2B4) system by performing both in vitro plasmid DNA damage experiments and enzyme assays. In addition, we examined the potential protective effects of some antioxidants against DNA-damaging effects of IDA and MC resulting from their reductive activation. To achieve these goals, we obtained P450R from sheep lung, beef liver and PB-treated rabbit liver microsomes, b5R from beef liver microsomes and CYP2B4 from PB-treated rabbit liver microsomes in highly purified forms. The plasmid DNA damage experiments demonstrated that P450R is capable of effectively reducing IDA to DNA-damaging species. The effective protections provided by antioxidant enzymes, SOD and catalase, as well as scavengers of hydroxyl radical, DMSO and thiourea, revealed that the mechanism of DNA damage by IDA involves the generation of ROS by redox cycling of IDA with P450R under aerobic conditions. The extent of DNA damages by both IDA and MC were found to increase with increasing concentrations of the drug or the enzyme as well as with increasing incubation time. IDA was found to have a greater ability to induce DNA damage at high drug concentrations than MC. The plasmid DNA experiments using b5R, on the other hand, showed that, unlike P450R, b5R was not able to reduce IDA to DNA-damaging reactive species. It was also found that in the presence of b5R and cofactor NADH, MC barely induced DNA strand breaks. All the purified P450Rs reduced IDA at about two-fold higher rate than that of MC as shown by the measurement of drug-induced cofactor consumption. This indicates that IDA may be a more potent cytotoxic drug than MC in terms of the generation of reactive metabolites. The results obtained from enzyme assays confirmed the finding obtained from plasmid DNA experiments that while MC is a very poor substrate for b5R, IDA is not a suitable substrate for this enzyme unlike P450R. The reconstitution experiments carried out under both aerobic and anaerobic conditions using various amounts of CYP2B4, P450R and lipid DLPC revealed that reconstituted CYP2B4 produced about 1.5-fold and 1.4-fold rate enhancements in IDA and MC reduction catalyzed by P450R alone, respectively. The present results also showed that among the tested dietary antioxidants, quercetin, rutin, naringenin, resveratrol and trolox, only quercetin was found to be highly potent in preventing DNA damage by IDA. These results may have some practical implications concerning the potential use of P450R as therapeutic agent on their own in cancer treatment strategies. Selective targeting of tumor cells with purified P450R by newly developed delivery systems such as using polymers, liposomes or antibodies may produce greater reductive activation of bioreductive drugs in tumor cells. Consequently, this strategy has a high potential to increase the efficacy and selectivity of cancer chemotherapy.
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Leclaire, Jacques. "Oxydations catalysees par les cytochromes p-450 et les systemes metalloporphyriniques modeles : cas des alcenes monosubstitues et du leucotriene b::(4)." Paris 6, 1987. http://www.theses.fr/1987PA066473.

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La selectivite des oxydations catalysees par les monooxygenases a cytochrome p-450 tient compte de deux facteurs principaux: 1) le role de la chaine proteique bordant le site actif du cytochrome p450. 2) la chimioselectivite du complexe a oxygene actif implique dans la reaction. Oxydation du phenoxy-6 hexene 1 et du leucotriene b4 fait intervenir des familles de cytochromes p-450 tres differentes. L'utilisation de systemes metalloporphyriniques permet de faire, en partie, la difference entre les facteurs dus a la reactivite intriseque de l'entite a oxygene actif et ceux dus a l'environnement proteique. L'apoproteine est absente et la reconnaissance du substrat est reduite a son strict minimum puisqu'elle n'est plus excitee que par la metalloporphyrine. Mise au point de catalyseurs selectifs d'oxydation des olefine monosubstituees
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Adams, Delyth Ann. "Characterisation of human hepatic P450 enzymes." Thesis, Imperial College London, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.266507.

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Schulz-Utermoehl, Timothy. "Identification and inhibition of hepatic p450 enzymes." Thesis, Imperial College London, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.313273.

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Luciakova, Dominika. "Characterisation of novel cytochrome P450-fusion enzymes." Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/characterisation-of-novel-cytochrome-p450fusion-enzymes(08d9f0eb-666c-4f0f-b3ad-1fbf52555a0e).html.

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This study focuses on the characterisation of three novel cytochrome P450-partner (P450-fusion) enzymes of unknown structure and function. Despite several well-established P450 functions, new structures of P450s are published frequently, with the P450-redox partner fusion systems being among the most discussed, due to their enhanced activity and biotechnological potential. Other, more intriguing, P450-fusions involve partners with functions distinct from electron transfer. Understanding why evolution drove the ‘partner’ proteins to evolve into a single unit is often unclear, but provides an important challenge for the understanding of the breadth of biochemical reactions mediated by P450s. The first P450-fusion analysed (Chapter 3) is CYP116B1 from a soil bacterium, Cupriavidus metallidurans, that displays important environmental implications. The enzyme was characterised as a functional fusion, composed of three domains: a P450 from the CYP116B family, and a phthalate dioxygenase reductase (PDOR)-like reductase binding FMN and a 2Fe-2S cluster. CYP116B1 is a stable, cytosolic enzyme but can undergo FMN cofactor loss. Studies included redox potentiometry of the intact fusion and its individual domains using spectro-electrochemical and EPR methods to enable the determination of midpoint redox potentials for individual cofactors. The CYP116B1 EPR signature was shown to be typical of P450s, and changed upon binding heme-coordinating inhibitors of the azole class. Extensive compound library screening did not reveal a substrate-like physiological “hit”. However, catalytic activity was detected towards selected thiocarbamate herbicides. GC-MS data revealed the enzymatic mechanism of herbicide degradation. The second system studied (Chapter 4) is P450-CAD, an atypical fusion of an uncharacterised soluble P450 and a cinnamyl alcohol dehydrogenase (ADH) module from Streptomyces ghanaensis; a member of the major antibiotic producing genus of bacteria. The CAD module appears unlikely to be a redox partner, but instead possibly mediates substrate/product exchange with the P450. The intact fusion was shown to aggregate during extraction. Genetic dissection of domains revealed that this was due to the highly insoluble ADH moiety. The heme domain (HD) was soluble and was characterised extensively. The enzyme displays an unusual spectrum when in the FeII-CO complex (Amax = 445 nm). The P450-CAD HD catalytic activity is supported by heterologous redox partners (E. coli flavodoxin reductase [FldR] and flavodoxin [FldA], and spinach ferredoxin reductase [FdR] and ferredoxin [Fdx]). The CAD-HD binds fatty acid substrates of carbon chain length C8-14, with the highest affinity for 12-methylmyristic acid (12M14C acid), the C12 lauric acid, its aldehyde and alcohol, indicating that the terminal methyl group is important for binding to the enzyme. Unusually, the CAD-HD also binds a range of detergent compounds. Further analysis included SEC-MALLS, thermostability and structural studies. The final enzyme studied (Chapter 5) is the P450-BDOR (a P450 linked to a benzoate dioxygenase reductase) redox-partner fusion. The unconventional trait of this enzyme is the inclusion of an FCD (a fatty acid metabolism regulator protein [FadR] C-terminal DNA-binding domain). From the point of view of P450s, DNA interaction would represent an unprecedented function, suggesting novel functions for a P450 enzyme. Thus, this enzyme requires extensive research with the expectations that new information will contribute to an expansion of knowledge of P450 diversity. This study provides initial analytical insights into the P450-BDOR system, supported with functional and kinetic data on the P450 and its reductase domain.
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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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Caprotti, Domenico. "Control of electron transfer in cytochrome p450 enzymes." Thesis, University of Oxford, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.509901.

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Books on the topic "Oxidation with P450 enzymes"

1

Waterman, M. R., and M. Hildebrand, eds. Assessment of the Use of Single Cytochrome P450 Enzymes in Drug Research. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-03019-6.

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England) Frontiers in Biological Catalysis (Conference) (2012 Cambridge. Frontiers in Biological Catalysis. London: Portland Press Limited, 2012.

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Holland, H. L. Organic synthesis with oxidative enzymes. New York: VCH, 1992.

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Raleigh, Stuart Martin. Involvement of cytochromes P450 (CYP) and other haem associated enzymes in the bioreduction of AQ4N, and antitumour prodrug. Leicester: De Montfort University, 1998.

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Lam, Maria Shuk Mun. Genetic polymorphisms in AH receptor and cytochrome P450 drug-metabolizing enzymes in relation to estradiol metabolism and breast cancer susceptibility. Ottawa: National Library of Canada, 2000.

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Emel, Arinç, Schenkman John B, Hodgson Ernest 1932-, and NATO Advanced Study Institute on Molecular Aspects of Drug Metabolizing Enzymes (1993 : Kus̜adası, Turkey), eds. Molecular aspects of oxidative drug metabolizing enzymes: Their significance in environmental toxicology, chemical carcinogenesis, and health. Berlin: Springer-Verlag, 1995.

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F, Johnson Eric, and Waterman Michael R, eds. Cytochrome P450. San Diego: Academic Press, 1996.

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Olkkola, Klaus T., Hugo E. M. Vereecke, and Martin Luginbühl. Drug interactions in anaesthetic practice. Edited by Michel M. R. F. Struys. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199642045.003.0021.

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When two or more drugs are administered simultaneously, the pharmacological response may be greater or less than the sum of the effects of the individual drugs. One drug may antagonize or potentiate the effects of the other and there may be also qualitative differences in response. Although some drug interactions increase the toxicity or result in loss of therapeutic effect, others are beneficial. Indeed, modern anaesthetic techniques depend on beneficial drug interactions. A sound combination of drugs helps clinicians to increase both the efficacy and safety of drug treatment. Drugs may interact on a pharmaceutical, pharmacodynamic, or pharmacokinetic basis. Many pharmacodynamic interactions are predictable and can be avoided by the use of common sense. However, it is much more difficult to predict the likelihood of pharmacokinetic and pharmaceutical interactions despite good prior knowledge of pharmacokinetics and chemical properties of individual drugs. Pharmaceutical drug interactions usually occur before the drug is given to the patient and they are caused by chemical (such as acid–base, salt formation, oxidation–reduction, hydrolysis, or epimerization) or physical (such as adsorption/absorption or emulsion breaking) reactions. When drugs have a pharmacokinetic interaction, one drug alters the absorption, distribution, or the elimination of the other drug. Many pharmacokinetic drug interactions are due to inhibition or induction of cytochrome P450 enzymes. Pharmacodynamic drug interactions are caused by drugs having an effect on the same receptors or the same physiological system. This chapter gives anaesthetists an overview of clinically relevant perioperative drug interactions.
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Paul R. Ortiz de Montellano. Cytochrome P450. Springer, 2008.

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Green, Steven M. Tarascon Pocket Pharmacopoeia 2006: P450 Enzymes. 2nd ed. Tarascon Publishing, 2005.

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Book chapters on the topic "Oxidation with P450 enzymes"

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Edin, Matthew L., Jennifer Cheng, Artiom Gruzdev, Samantha L. Hoopes, and Darryl C. Zeldin. "P450 Enzymes in Lipid Oxidation." In Cytochrome P450, 881–905. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-12108-6_13.

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Ortiz de Montellano, Paul R., and James J. De Voss. "Substrate Oxidation by Cytochrome P450 Enzymes." In Cytochrome P450, 183–245. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-27447-2_6.

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Ortiz de Montellano, Paul R. "Substrate Oxidation by Cytochrome P450 Enzymes." In Cytochrome P450, 111–76. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-12108-6_4.

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Schenkman, John B., and Ingela Jansson. "Introduction to Cytochrome P450." In Molecular Aspects of Oxidative Drug Metabolizing Enzymes, 1–19. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79528-2_1.

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Hodgson, Ernest, R. Michael Roe, Joyce E. Goldstein, Siming Liu, Scott C. Coleman, and Randy L. Rose. "Cytochrome P450 Isoforms." In Molecular and Applied Aspects of Oxidative Drug Metabolizing Enzymes, 145–55. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4855-3_10.

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Lu, Anthony Y. H. "Therapeutic Agents and Cytochrome P450." In Molecular Aspects of Oxidative Drug Metabolizing Enzymes, 503–13. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79528-2_24.

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Schenkman, John B., and Andrei I. Voznesensky. "Interaction Between Cytochrome P450 and Reductase." In Molecular Aspects of Oxidative Drug Metabolizing Enzymes, 47–63. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79528-2_3.

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Buhler, Donald R. "Cytochrome P450 Expression in Rainbow Trout: An Overview." In Molecular Aspects of Oxidative Drug Metabolizing Enzymes, 159–80. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79528-2_8.

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Hanukoglu, Israel. "Structures of Mitochondrial P450 System Proteins." In Molecular and Applied Aspects of Oxidative Drug Metabolizing Enzymes, 41–54. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4855-3_3.

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Kupfer, David. "Metabolism of Xenobiotic Proestrogens and Estrogens by Cytochrome P450." In Molecular Aspects of Oxidative Drug Metabolizing Enzymes, 479–89. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79528-2_22.

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Conference papers on the topic "Oxidation with P450 enzymes"

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"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.

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Li, Wen Lan, Yang Yang, Yubin Ji, and Zheng Ting Hu. "The Study on Biotransformation of Paeonol and Interrelation with Cytochrome P450 Enzymes." In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5163674.

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Tian, Haijin, Paul Quehl, Joel Hollender, and 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.

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Tesfamichael, Aron B. "Abstract 5466: Butyrate effect on expression of quinone oxidoreductase (NQO1) and cytochrome P450 CYP1A1 enzymes." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-5466.

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Liu, Jiawang, Shannon Taylor, Patrick Dupart, Corey Arnold, and Maryam Foroozesh. "Abstract 2464: Flavone derivatives as small-molecule probes of cytochrome P450 enzymes: Inhibitory activity and selectivity." 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.am2013-2464.

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Shih, Tsan-huang, Tsai-Ling Lee, Kuan-Yuan Chang, Yu-Ping Hsu, and Tun-Wen Pai. "Designing a dedicated database for eukaryotic algae species — A case study on cross-species comparison of P450 enzymes." In 2010 International Computer Symposium (ICS 2010). IEEE, 2010. http://dx.doi.org/10.1109/compsym.2010.5685413.

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Alonso, Salvador, Meng Su, Richard Jones, and Gabriel Ghiaur. "Abstract 4842: The stem cell niche detoxifies chemotherapy and protects malignant hematopoietic cells via expression of cytochrome P450 enzymes." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4842.

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Zahner, C., E. Kruttschnitt, J. Uricher, M. Lissy, M. Hirsch, S. Nicolussi, S. Krähenbühl, and J. Drewe. "No clinically relevant interactions of St. John’s wort extract Ze 117 low in hyperforin with cytochrome P450 enzymes and P-glycoprotein." In 67th International Congress and Annual Meeting of the Society for Medicinal Plant and Natural Product Research (GA) in cooperation with the French Society of Pharmacognosy AFERP. © Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-3400128.

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Shnyder, Steven D., Paul M. Loadman, Mark Sutherland, Helen M. Sheldrake, Mark Searcey, Laurence H. Patterson, and Klaus Pors. "Abstract 4541: Tumor-selective bioactivation of duocarmycin bioprecursors by cytochrome P450 enzymes provides an opportunity to treat drug-resistant breast cancer cells." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4541.

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Harris, Kelly, Mohammad Niaz, Mary Washington, and Aramandla Ramesh. "Abstract 4572: Western diet enhances benzo(a)pyrene [B(a)P]-induced colon tumorigenesis in the PIRC rat model via cytochrome P450 drug metabolizing enzymes." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4572.

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Reports on the topic "Oxidation with P450 enzymes"

1

Blake, R. II. Enzymes of respiratory iron oxidation. Office of Scientific and Technical Information (OSTI), January 1992. http://dx.doi.org/10.2172/6558600.

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Blake, R. II. Enzymes of respiratory iron oxidation. Office of Scientific and Technical Information (OSTI), January 1991. http://dx.doi.org/10.2172/5620317.

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Blake, R. II. Enzymes of respiratory iron oxidation. Progress report, March 1990--June 1992. Office of Scientific and Technical Information (OSTI), December 1992. http://dx.doi.org/10.2172/10149887.

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Blake, R. II. Enzymes of respiratory iron oxidation. Progress report, March 1990--November 1991. Office of Scientific and Technical Information (OSTI), December 1991. http://dx.doi.org/10.2172/10122599.

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