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Books on the topic 'Enzyme activation'

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Published: 4 June 2021
Last updated: 5 March 2023

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1

Ottaway, J. H. Regulation of enzyme activity. Oxford: IRL Press, 1988.

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2

H, Stenmark, ed. Phosphoinositides in subcellular targeting and enzyme activation. Berlin: Springer, 2004.

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3

Stein, Ross L. Kinetics of enzyme action: Essential principles for drug hunters. Hoboken, N.J: John Wiley, 2011.

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4

Stenmark, Harald, ed. Phosphoinositides in Subcellular Targeting and Enzyme Activation. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18805-3.

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5

Krupi͡anko, V. I. Vektornyĭ metod predstavlenii͡a fermentativnykh reakt͡siĭ. Moskva: "Nauka", 1990.

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6

Alan, Wiseman, ed. Enzyme induction, mutagen activation, and carcinogen testing in yeast. Chichester, West Sussex, England: E. Horwood, 1987.

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7

H, Schmid-Schönbein, Wurzinger L. J, Zimmermann R. E, and Commission of the European Communities. Committee on Medical and Public Health Research., eds. Enzyme activation in blood-perfused artificial organs: Proceedings of an interdisciplinary meeting. Boston: Nijhoff, 1985.

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8

Mordechai, Liscovitch, ed. Signal-activated phospholipases. Austin: R.G. Landes Co., 1994.

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9

Akira, Arimura, Saʻīd Sāmī, and International Symposium on VIP, PACAP, and Related Peptides (2nd : 1995 : New Orleans, La.), eds. VIP, PACAP, and related peptides: Second international symposium. New York: New York Academy of Sciences, 1996.

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10

Light, P. E. An investigation into factors controlling activation of the enzyme protein Kinase C in the regulation of neurotransmitter release at the frog neuromuscular junction. Birmingham: University of Birmingham, 1990.

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11

Chen, Chang-Hwei. Activation and Detoxification Enzymes. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-1049-2.

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12

1923-, Lorand Laszlo, and Mann Kenneth G, eds. Proteolytic enzymes in coagulation, fibrinolysis, and complement activation. San Diego: Academic Press, 1993.

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13

Rossomando, Edward F. HPLC in enzymatic analysis. 2nd ed. New York: Wiley, 1998.

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14

M, Cunningham Fiona, ed. Lipid mediators. London: Academic Press, 1994.

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15

C, Murphy Robert, and Fitzpatrick Frank A, eds. Arachidonate related lipid mediators. San Diego: Academic Press, 1990.

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16

L, Schramm Vern, and Purich Daniel L, eds. Enzyme kinetics and mechanism. 1999.

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17

Enzyme kinetics and mechanism. San Diego: Academic Press, 2002.

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18

Stein, Ross L. Kinetics of Enzyme Action. Wiley & Sons, Incorporated, John, 2011.

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19

Stenmark, Harald. Phosphoinositides in Subcellular Targeting and Enzyme Activation. Springer London, Limited, 2012.

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20

Stein, Ross L. Kinetics of Enzyme Action: Essential Principles for Drug Hunters. Wiley & Sons, Incorporated, John, 2011.

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21

Stein, Ross L. Kinetics of Enzyme Action: Essential Principles for Drug Hunters. Wiley & Sons, Incorporated, John, 2011.

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22

Stein, Ross L. Kinetics of Enzyme Action: Essential Principles for Drug Hunters. Wiley & Sons, Incorporated, John, 2011.

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23

Stenmark, Harald. Phosphoinositides in Subcellular Targeting and Enzyme Activation. Springer, 2012.

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24

Stenmark, Harald. Phosphoinositides in Subcellular Targeting and Enzyme Activation. Springer, 2003.

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25

Engel, P. C. Enzymology LabFax (Labfax Series). Academic Press, 1996.

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26

Baici, Antonio. Kinetics of Enzyme-Modifier Interactions: Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms. Baici Antonio, 2015.

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27

Baici, Antonio. Kinetics of Enzyme-Modifier Interactions: Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms. Springer, 2016.

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28

Baici, Antonio. Kinetics of Enzyme-Modifier Interactions: Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms. Springer London, Limited, 2015.

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29

Activation And Detoxification Enzymes Functions And Implications. Springer, 2011.

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30

Cooper, A. The Enzyme Catalysis Process:Energetics, Mechanism and Dynamics. Springer, 1989.

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31

Cascorbi, Ingolf. Polymorphic cytochrome P450 2D6 as the responsible enzyme of activation. Edited by Paul Farquhar-Smith, Pierre Beaulieu, and Sian Jagger. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198834359.003.0079.

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The landmark paper discussed in this chapter is ‘Bioactivation of the narcotic drug codeine in human liver is mediated by the polymorphic monooxygenase catalyzing debrisoquine 4-hydroxylation (cytochrome P-450 dbl/bufI)’, published by Dayer et al. in 1988. Codeine is an old but frequently prescribed drug used for the treatment of mild-to-moderate pain. However, its use is nowadays restricted after observations of partly fatal respiratory repression in children. Codeine itself exhibits no analgesic effect, but is partly activated by O-demethylation to morphine by cytochrome P450 2D6 (CYP2D6). The identification of the polymorphic CYP2D6 as the enzyme responsible for activation was achieved by Dayer et al. in 1998 and was an important milestone contributing to the widely observed inter-individual differences of drug action and side effects of codeine. Translating the pharmacogenetics of codeine into clinical practice is currently underway in clinical trials, to identify ineffective analgesics and, in particular, avoid severe adverse events.
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32

Soda, Kenji, and Toshio Fukui. Molecular Aspects of Enzyme Catalysis. Wiley & Sons, Incorporated, John, 2008.

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33

Molecular aspects of enzyme catalysis. Tokyo: Kodansha, 1994.

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34

Fukui, Tukui, and Kenji Soda. Molecular Aspects of Enzyme Catalysis. Vch Pub, 1994.

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35

Soda, Kenji, and Toshio Fukui. Molecular Aspects of Enzyme Catalysis. Wiley & Sons, Limited, John, 2007.

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36

Lyle, Stephen. The sulfate-activation pathway: A bifunctional enzyme which utilizes intermediate channeling. 1993.

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37

Clarke, Andrew. Temperature and reaction rate. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780199551668.003.0007.

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All other things being equal, physiological reaction rate increases roughly exponentially with temperature. Organisms that have adapted over evolutionary time to live at different temperatures can have enzyme variants that exhibit similar kinetics at the temperatures to which they have adapted to operate. Within species whose distribution covers a range of temperatures, there may be differential expression of enzyme variants with different kinetics across the distribution. Enzymes adapted to different optimum temperatures differ in their amino acid sequence and thermal stability. The Gibbs energy of activation tends to be slightly lower in enzyme variants adapted to lower temperatures, but the big change is a decrease in the enthalpy of activation, with a corresponding change in the entropy of activation, both associated with a more open, flexible structure. Despite evolutionary adjustments to individual enzymes involved in intermediary metabolism (ATP regeneration), many whole-organism processes operate faster in tropical ectotherms compared with temperate or polar ectotherms. Examples include locomotion (muscle power output), ATP regeneration (mitochondrial function), nervous conduction and growth.
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38

Brown, Stephanie Leanne. The biosynthesis of poly (ribitol-phosphate) wall teichoic acids and the roles of individual tailoring modifications. 2011.

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39

Smerage, Jeffrey. Activated Transcription of the Glycolytic Enzyme Genes of Saccharomyces Cerevisiae: The Chromatin Structures of TP11 and Mechanisms of RAP1P Mediated Activation. Dissertation Discovery Company, 2018.

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40

Smerage, Jeffrey. Activated Transcription of the Glycolytic Enzyme Genes of Saccharomyces Cerevisiae: The Chromatin Structures of TP11 and Mechanisms of RAP1P Mediated Activation. Creative Media Partners, LLC, 2018.

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41

Chen, Chang-Hwei. Activation and Detoxification Enzymes: Functions and Implications. Springer, 2014.

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42

Chen, Chang-Hwei. Activation and Detoxification Enzymes: Functions and Implications. Springer, 2011.

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43

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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44

O’Neal, M. Angela. Pain in the Back. Edited by Angela O’Neal. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780190609917.003.0006.

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This case explores how bone health can be affected by antiepileptic drugs (AEDs), and why this is an important issue in women with epilepsy (WWE). AEDs affect bone health through activation of the cytochrome P450 system in the liver, leading to increased metabolism of vitamin D. The enzyme-inducing AEDs include phenytoin, carbamazepine, phenobarbital, and primidone. Risk factors for osteoporosis include female gender, low body mass, inadequate vitamin D intake, and smoking. The specific AEDs used and the length of treatment confer additional risks. Furthermore, in WWE, risks are magnified related to falls, either from seizures or related to medication toxicity. Screening with bone density and measures to promote bone health are extremely important in these at-risk women.
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45

Hester, Charles K. Mitogen-Activated Protein Kinases: Activation, Functions and Regulation. Nova Science Publishers, Incorporated, 2019.

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46

Rossomando, Edward F. HPLC in Enzymatic Analysis. Wiley & Sons, Incorporated, John, 2009.

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47

Frenkel, Joost, and Hans R. Waterham. Mevalonate Kinase Deficiency. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0039.

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Mevalonate kinase deficiency (MKD) is an autosomal recessive inborn error of isoprenoid biosynthesis, a pathway yielding sterols and nonsterol isoprenoids.In patients, the enzyme activity of mevalonate kinase is severely reduced due to mutations in the encoding gene, MVK. The substrate, mevalonate, accumulates and is elevated in blood and urine. Shortage of certain downstream products of the pathway, nonsterol isoprenoids, leads to dysregulation of the innate immune system, activation of inflammasomes, and interleukin (IL)-1 mediated inflammation.Symptoms start in early childhood with recurrent attacks of fever, vomiting, diarrhea, headache, sore throat, abdominal pain, arthralgias, painful lymphadenopathy, hepatosplenomegaly, skin rash, and mucosal ulcers. Severely affected patients have additional symptoms, such as intellectual impairment, progressive cerebellar ataxia, and tapetoretinal degeneration. Complications include intestinal obstruction, AA-amyloidosis, hemophagocytosis, and severe infection.Management of MKD is directed at controlling inflammation.
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48

(Editor), John N. Abelson, Melvin I. Simon (Editor), Laszlo Lorand (Editor), and Kenneth G. Mann (Editor), eds. Proteolytic Enzymes in Coagulation, Fibrinolysis, and Complement Activation, Part B, Volume 223: Volume 223: Proteolytic Enzymes in Coagulation, Fibrinolysis ... Activation Part B (Methods in Enzymology). Academic Press, 1993.

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49

Rider, Lisa G., and Frederick W. Miller. Outcome assessment in the idiopathic inflammatory myopathies. Edited by Hector Chinoy and Robert Cooper. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198754121.003.0016.

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Due to their rarity, heterogeneity, and multispecialty nature, the myositis syndromes have limited data-driven consensus on appropriate outcome measures. Recently, two international, multispecialty consortia developed new tools and consensus on core set measures of myositis disease activity and damage, as well as response criteria that are now recommended for use as clinical trial endpoints but will also be useful in clinical practice. Magnetic resonance imaging, muscle ultrasound, selected laboratory tests, and immunological biomarkers—including cytokines, chemokines, lymphocyte flow cytometry, and endothelial activation markers—can all be helpful adjuncts to serum muscle enzyme levels in assessing disease activity and damage, but these have not yet been fully validated. Definitions of clinically inactive disease, complete clinical response, and remission have also been proposed but require further validation. These advances should enhance the development of therapies by standardizing our ability to demonstrate their efficacy in treating the idiopathic inflammatory myopathies.
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50

Abelson, John N., Laszlo Lorand, Melvin I. Simon, and Kenneth G. Mann. Proteolytic Enzymes in Coagulation, Fibrinolysis, and Complement Activation, Part B. Elsevier Science & Technology Books, 1993.

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