Diversified Classes of Enzyme Modulators

Chapter

Abstract

Enzymatic catalyses are mediated by functional groups present in amino acid side chains. The amino acid side chains of enzymes that are frequently directly involved in enzyme catalytic processes include histidine, serine, cystein, lysine, glutamate, and aspartate. The active site of an enzyme is usually larger than the substrate, since in most cases the substrate is partially surrounded by the active site. The structure of an enzyme is required to stabilize the conformation of the active site for achieving enzymatic function.

Keywords

Phenol Tyrosine Glutathione Superoxide Cysteine 

Bibliography

  1. Bock KW, Lilienblum W, Fischer G et al (1987) The role of conjugation reactions in detoxication. Arch Toxicol 60:22–29PubMedCrossRefGoogle Scholar
  2. Bolton JL, Trush MA, Penning TM et al (2000) Role of quinones in toxicology. Chem Res Toxicol 13:135–160PubMedCrossRefGoogle Scholar
  3. Chen CH, Battaglioli G, Martin DL et al (2003) Distinctive interactions in the holoenzyme formation for two isoforms of glutamate decarboxylase. Biochim Biophys Acta 1645:63–71PubMedCrossRefGoogle Scholar
  4. Ciaccio PJ, Jaiswal AK, Tew KD (1994) Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics. J Biol Chem 269:15558–15562PubMedGoogle Scholar
  5. Cuendet M, Oteham CP, Moon RC et al (2006) Quinone reductase induction as a biomarker for cancer chemoprevention. J Nat Prod 69:460–463PubMedCrossRefGoogle Scholar
  6. Dinkova-Kostova AT, Abeygunawardana C, Talalay P (1998) Chemoprotective properties of phenylpropenoids, bis(benzylidene)cycloalkanones, and related Michael reaction acceptors: correlation of potencies as phase 2 enzyme inducers and radical scavengers. J Med Chem 41:5287–5296PubMedCrossRefGoogle Scholar
  7. Dinkova-Kostova AT, Cheah J, Samouilov A et al (2007) Phenolic Michael reaction acceptors: combined direct and indirect antioxidant defenses against electrophiles and oxidants. Med Chem 3:261–268PubMedCrossRefGoogle Scholar
  8. Dinkova-Kostova AT, Holtzclaw WD, Cole RN et al (2002) Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc Natl Acad Sci U S A 99:11908–11913PubMedCrossRefGoogle Scholar
  9. Dinkova-Kostova AT, Massiah MA, Bozak RE et al (2001) Potency of Michael reaction acceptors as inducers of enzymes that protect against carcinogenesis depends on their reactivity with sulfhydryl groups. Proc Natl Acad Sci U S A 98:3404–3409PubMedCrossRefGoogle Scholar
  10. Prochaska HJ, Talalay P (1988) Regulatory mechanisms of monofunctional and bifunctional anticarcinogenic enzyme inducers in murine liver. Cancer Res 48:4776–4782PubMedGoogle Scholar
  11. Rinaldi R, Eliasson E, Swedmark S et al (2002) Reactive intermediates and the dynamics of glutathione transferases. Drug Metab Dispos 30:1053–1058PubMedCrossRefGoogle Scholar
  12. Schultz TW, Yarbrough JW, Hunter RS et al (2007) Verification of the structural alerts for Michael acceptors. Chem Res Toxicol 20:1359–1363PubMedCrossRefGoogle Scholar
  13. Talalay P (1989) Mechanisms of induction of enzymes that protect against chemical carcinogenesis. Adv Enzyme Regul 28:237–250PubMedCrossRefGoogle Scholar
  14. Talalay P, De Long MJ, Prochaska HJ (1988) Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis. Proc Natl Acad Sci USA 85:8261–5PubMedCrossRefGoogle Scholar
  15. Zhang F, Thottananiyil M, Martin DL, Chen CH (1999) Conformational alteration in serum albumin as a carrier for pyridoxal phosphate: a distinction from pyridoxal phosphate-dependent glutamate decarboxylase. Arch Biochem Biophys 364:195–202PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2012

Authors and Affiliations

  1. 1.Department of Biomedical SciencesUniversity at Albany, State University of New YorkAlbanyUSA

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