Abstract
Detoxification enzyme-catalyzed metabolism forms more hydrophilic and less reactive foreign compounds, thus facilitating their excretion from the body. Detoxification enzymes consist of conjugation and non-conjugation enzymes. Conjugation enzymes include uridine diphosphate-glucuronosyltransferase, glutathione S-transferases, sulfotransferase, N-acetyltransferase, methyltransferase, and acyltransferase, while non-conjugation detoxification enzymes are such as quinone reductase and epoxide hydrolases. A variety of functional groups or atoms of foreign compounds that are targets of detoxification enzyme-catalyzed reactions include phenol, sulfhydryl, polyphenol, carboxylic acid, amino acid, and epoxide.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Bibliography
Arand M, Cronin A, Adamska M (2005) Oesch F. Epoxide hydrolases: structure, function, mechanism, and assay. Methods Enzymol 400:569-588.
Benson AM, Hunkeler MJ, Talalay P (1980) Increase of NAD(P)H:quinone reductase by dietary antioxidants: possible role in protection against carcinogenesis and toxicity. Proc Natl Acad Sci U S A 177:5216–5220
Chen CH (2012) Activation and detoxification enzymes: functions and implications. Springer, New York
Decker M, Arand M, Cronin A (2009) Mammalian epoxide hydrolases in xenobiotic metabolism and signalling. Arch Toxicol 83:297–318
Dekant W, Vamvakas S (1993) Glutathione-dependent bioactivation of xenobiotics. Xenobiotica 23:873–887
Evans D (1992) N-acetyltransferase. In: Kalow W (ed) Pharmacogenetics of drug metabolism. Pergamon, New York
Fretland AJ, Omiecinski CJ (2000) Epoxide hydrolases: biochemistry and molecular biology. Chem Biol Interact 129:41–59
Gamage N, Barnett A, Hempel N et al (2006) Human sulfotransferases and their role in chemical metabolism. Toxicol Sci 90:5–22
Grant DM, Blum M, Meyer UA (1992) Polymorphisms of N-acetyltransferase genes. Xenobiotica 9–10:1073–1081
Hayes JD, Flanagan JU, Jowsey IR (2005) Glutathione transferases. Annu Rev Pharmacol Toxicol 45:51–88
Kato R, Yamazoe Y (1994) Metabolic activation of N-hydroxylated metabolites of carcinogenic and mutagenic arylamines and arylamides by esterification. Drug Metab Rev 26:413–429
King C, Rios G, Green M, Tephly T (2000) UDP-glucuronosyltransferases. Curr Drug Metab 1:143–161
Klaassen CD, Boles JW (1997) Sulfation and sulfotransferases 5: the importance of 3′- phosphoadenosine 5′-phosphosulfate (PAPS) in the regulation of sulfation. FASEB J 11:404–418
Mannervik B (1988) Danielson UH. Glutathione transferases--structure and catalytic activity. CRC Crit Rev Biochem 23:283-337.
Meech R, Mackenzie PI (1997) Structure and function of uridine diphosphate glucuronosyl transferases. Clin Exp Pharmacol Physiol 24:907–915
Miners JO, Knights KM, Houston JB et al (2006) In vitro-in vivo correlation for drugs and other compounds eliminated by glucuronidation in humans: pitfalls and promises. Biochem Pharmacol 71:1531–1539
Negishi M, Pedersen LG, Petrotchenko E et al (2001) Structure and function of sulfotransferases. Arch Biochem Biophys 390:149–157
Rao PV, Krishna CM, Zigler JS Jr (1992) Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase. J Biol Chem 267:96–102
Weinshilboum RM, Otterness DM, Szumlanski CL (1999) Methylation pharmacogenetics: catechol O-methyltransferase, thiopurine methyltransferase, and histamine N-methyltransferase. Annu Rev Pharmacol Toxicol 39:19–52
Wilce MC, Parker MW (1994) Structure and function of glutathione S-transferases. Biochim Biophys Acta 1205(1):1–18
Wildfang E, Zakharyan RA, Aposhian HV (1998) Enzymatic methylation of arsenic compounds. VI Characterization of hamster liver arsenite and methylarsonic acid methyltransferase activities in vitro. Toxicol Appl Pharmacol 152:366–375
Wood TC, Salavagionne OE, Mukherjee B et al (2006) Human arsenic methyltransferase (AS3MT) pharmacogenetics: gene resequencing and functional genomics studies. J Biol Chem 281:7364–7373
Talalay P (2000) Chemoprotection against cancer by induction of phase 2 enzymes. Biofactors 12:5–11
Zakharyan RA, Wildfang E, Aposhian HV (1996) Enzymatic Methylation of Arsenic Compounds. Toxicol Appl Pharmacol 140:77–84
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2020 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Chen, CH. (2020). Detoxifying Metabolism: Detoxification Enzymes. In: Xenobiotic Metabolic Enzymes: Bioactivation and Antioxidant Defense. Springer, Cham. https://doi.org/10.1007/978-3-030-41679-9_7
Download citation
DOI: https://doi.org/10.1007/978-3-030-41679-9_7
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-41678-2
Online ISBN: 978-3-030-41679-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)