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• W3021505455 endingPage "457" @default.
• W3021505455 startingPage "435" @default.
• W3021505455 abstract "There are over 150 documented methyltransferase enzymes, many with very different overall structures but with very similar properties within the local active site. Methyl conjugation is a good example of convergent evolution with over 95% of these enzymes using S-adenosyl-l-methionine (Ado-Met) as the methyl donor. Methyl transfer is an important pathway in the metabolism of both xenobiotic and endogenous compounds. Many drugs undergo methylation as do neurotransmitters, hormones, proteins, lipids, polysaccharides, and nucleic acids; methylation is fundamental to the control of gene transcription. Nitrogen or oxygen atoms are the most common targets for protein methylation. N-Methylation in vivo is not readily reversible and the amino acid targets include lysine, histidine, arginine, glutamine, and asparagine. N-Methylation reactions play an important metabolic role in the termination of the action of histamine and in the formation of epinephrine from norepinephrine. O-Methylation targets include catechols, hydroxyindoles, and the carboxy groups of proteins and these reactions can be reversed. Thus, the reversible O-methylation of glutamates and aspartates produces methyl esters of a finite life span, which relate to protein function. The primary role of S-methylation is in the detoxification of xenobiotics. Thiopurine methyltransferase (TPMT) plays a key role in the metabolism of thiopurine anticancer and immunosuppressive drugs; there is no known endogenous substrate. The role played by the TPMT genetic polymorphism in the profound myelotoxicity induced by the thiopurine drugs azathioprine, mercaptopurine (MP), and thioguanine (TG) is a well-validated example of the clinical importance of pharmacogenetics; a textbook example of applied pharmacogenomic research. This chapter concentrates on those human methyltransferases whose study has furthered our understanding of the fundamental role of methyl conjugation or whose analysis has illustrated basic concepts in the understanding of the methyl transfer reaction, that is, catechol O-methyltransferase (COMT, EC 2.1.1.6), histamine N-methyltransferase (HNMT, EC 2.1.1.8), thiol methyltransferase (TMT, EC 2.1.1.9), and TPMT (EC 2.1.1.67)." @default.
• W3021505455 created "2020-05-13" @default.
• W3021505455 creator A5089667999 @default.
• W3021505455 date "2010-01-01" @default.
• W3021505455 modified "2023-09-27" @default.
• W3021505455 title "Methyltransferases" @default.
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