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Books on the topic 'Oxidation with P450 enzymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 16 February 2022

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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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2

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

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3

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

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4

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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5

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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6

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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7

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

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8

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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9

Paul R. Ortiz de Montellano. Cytochrome P450. Springer, 2008.

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10

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

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11

Tarascon. Tarascon Pocket P450 Enzymes Pharmacopoeia 2007. Tarascon Publishing, 2007.

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12

Schenkman, John B. Molecular Aspects of Oxidative Drug Metabolizing Enzymes: Their Significance in Environmental Toxicology, Chemical Carcinogenesis and Health (Nato a S I Series Series H, Cell Biology). Springer-Verlag Telos, 1995.

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13

Paul R. Ortiz de Montellano. Cytochrome P450: Structure, Mechanism, and Biochemistry. Springer, 2010.

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14

Cytochrome P450: Structure, Mechanism, and Biochemistry. Springer, 2015.

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15

Paul R. Ortiz de Montellano. Cytochrome P450: Structure, Mechanism, and Biochemistry. Springer, 2012.

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16

Paul R. Ortiz de Montellano. Cytochrome P450: Structure, Mechanism, and Biochemistry. Springer, 2016.

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17

S, Lee Jae, Obach R. Scott, and Fisher Michael B, eds. Drug metabolizing enzymes: Cytochrome P450 and other enzymes in drug discovery and development. Lausanne, Switzerland: FontisMedia SA, 2003.

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18

Schmid, Rolf D., and Vlada Urlacher. Modern Biooxidation: Enzymes, Reactions and Applications. Wiley & Sons, Limited, John, 2007.

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19

Schmid, Rolf D., and Vlada Urlacher. Modern Biooxidation: Enzymes, Reactions and Applications. Wiley & Sons, Incorporated, John, 2007.

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20

Pub, Tarascon. Tarascon P450 Enzymes Quick Reference Card 2008 (Tarascon Pocket Pharmacopoeia). Not Avail, 2007.

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21

Mechanisms of Biological Oxidations. University of Cambridge ESOL Examinations, 2015.

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22

1942-, Schmid Rolf, and Urlacher Vlada B, eds. Modern biooxidation: Enzymes, reactions, and applications. Weinheim: Wiley-VCH, 2007.

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23

Modern biooxidation: Enzymes, reactions and applications. Weinheim, DE: Wiley-VCH, 2008.

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24

R, Waterman Michael, and Hildebrand M, eds. Assessment of the use of single cytochrome P450 enzymes in drug research. Berlin: Springer-Verlag, 1994.

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25

Waterman, M. R. Assessment of the Use of Single Cytochrome P450 Enzymes in Drug Research. Springer, 2012.

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26

Deng, Shiping. Sulfur oxidation and rhodanese activity in soils. 1990.

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27

Schomburg, Dietmar, Ida Schomburg, and Antje Chang. Class 1 Oxidoreductases XII: EC 1.14.15 - 1.97. Springer, 2014.

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28

Hirao, Toshikazu. Functionalized Redox Systems: Synthetic Reactions and Design of π- and Bio-Conjugates. Springer, 2015.

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29

Hirao, Toshikazu. Functionalized Redox Systems: Synthetic Reactions and Design of π- and Bio-Conjugates. Springer, 2016.

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30

M, Roberts Stanley, and Poignant Geraldine, eds. Hydrolysis, oxidation and reduction. Chichester, West Sussex, England: Wiley, 2002.

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31

Araya, Zufan. Cytochrome P450 Enzymes in the Biosynthesis and Metabolism of Bile Acids and Active Forms of Vitamin D3. Uppsala Universitet, 1999.

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32

King, Sarah J. Development of a technique to investigate the role of cytochromes p450 in oxidation of human low density lipoprotein. 1997.

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33

Sinnott, Michael. Comprehensive Biological Catalysis: A Mechanistic Reference : Radical Reactions and Oxidation/Reduction. Academic Press, 1997.

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34

Sinnott, Michael. Comprehensive Biological Catalysis: A Mechanistic Reference : Radical Reactions and Oxidation/Reduction. Academic Press, 1997.

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35

Redox Biocatalysis Fundamentals And Applications. John Wiley & Sons, 2012.

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36

Schussel, Leonard J. Synthesis and oxidation of metal-thiolate compounds which mimic the active site function of thiolate dioxygenase enzymes. 1987.

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37

Bylund, Johan. Cytochrome P450 Enzymes in Oxygenation of Prostaglandin Endoperoxides & Arachidonic Acid: Cloning, Expression & Catalytic Properties of Cyp4F8 & Cyp4F21 ... from the Faculty of Pharmacy, 231). Uppsala Universitet, 2000.

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38

Zhao, Sheyun. Induction of freezing tolerance in jack pine seedlings: Changes in lipids, oxidation-reduction and antioxidant enzymes during cold acclimation. 1998.

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39

Foulon, Veerie. Oxidation of 3-Methly-Branched Fatty Acids: Study of the Enzymes Involved in the Reaction Sequence (Acta Biomedica Lovaniensia, 235). Leuven Univ Pr, 2001.

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40

(Editor), Andreas Holzenburg, and Nigel S. Scrutton (Editor), eds. Enzyme-Catalyzed Electron and Radical Transfer (Subcellular Biochemistry Volume 35). Springer, 2000.

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41

Bogaert, Lucas, and Noah Coppens. Peroxidases: Biochemical Characteristics, Functions and Potential Applications. Nova Science Publishers, Incorporated, 2013.

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42

(Editor), Bernard Testa, and John Caldwell (Editor), eds. Biochemistry of Redox Reactions (Metabolism of Drugs and Other Xenobiotics). Academic Press, 1994.

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43

A. Ertekin, B.A. Yıldırım, S. Yıldırım, F. Yıldırım, and M. Tütüncü. Investigation of the lipid peroxidation, antioxidant enzymes, antioxidant vitamins, oxidation products of nitric oxide and some biochemical parameters in chicken with infectious bursal disease (IBD). Verlag Eugen Ulmer, 2016. http://dx.doi.org/10.1399/eps.2016.164.

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44

(Editor), Mark D. Evans, and Marcus S. Cooke (Editor), eds. Oxidative Damage to Nucleic Acids (Molecular Biology Intelligence Unit). Springer, 2007.

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45

1962-, Evans Mark D., and Cooke Marcus S, eds. Oxidative damage to nucleic acids. Austin, Tex: Landes Bioscience, 2007.

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46

Promises and Limits of Reductionism in the Biomedical Sciences (Catalysts for Fine Chemical Synthesis). Wiley, 2002.

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47

O, Hill H. A., Sadler P. J, and Thompson A. J, eds. Metal sites in proteins and models: Iron centres. Berlin: Springer, 1997.

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48

O, Hill H. A., Sadler P. J, Thomson A. J, and Chapman S. K, eds. Metal sites in proteins and models. Berlin: Springer, 1997.

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49

Deegan, Patrick. Porphyria. Edited by Patrick Davey and David Sprigings. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199568741.003.0179.

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This chapter discusses six diseases caused by inborn errors of metabolism affecting the biosynthesis of haem. Haem is a tetracyclic metal-binding compound involved in oxygen transport (in haemoglobin and myoglobin) and redox reactions (e.g. in the cytochrome P450 system). Each of these conditions is caused by a single gene defect in one of the enzymes involved in the biosynthesis of haem. Inheritance is usually autosomal dominant with incomplete penetrance. The enzyme defect results in disease, not as a result of deficiency of the reaction product, but as a result of accumulation of precursors. Early, soluble precursors, 5-aminolaevulinic acid, and porphobilinogen (not porphyrins as such) are neurotoxic and, when present in great excess, as occurs when flux through the haem synthetic pathway is increased in response to particular medications or hormones, lead to acute neurovisceral crises. Later cyclical precursors (porphyrins) in the pathway are also water soluble and excreted in urine, but are susceptible to activation by electromagnetic radiation in the visible spectrum and are converted to free-radical metabolites that cause pain, inflammation, and tissue damage in the skin. The final haem precursors (also porphyrins) are hydrophobic and excreted in the bile and faeces and are also activated by light to toxic metabolites.

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50

O, Hill H. A., Sadler P. J, and Thompson A. J, eds. Metal sites in proteins and models: Redox centres. Berlin: Springer, 1998.

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