Abstract
Enzymatic methylations, in the presence of S-adenosyl-L-methionine (SAM) as a methyl donor, play a significant role in several cellular functions. During the past decade, three of these SAM-mediated methylations have received special attention: (a) stepwise conversion of membrane phosphatidylethanolamine (PE) to phosphatidyl-N-methylethanolamine (PME), phosphatidyl-N,N-dimethylethanolamine (PMME) and phosphatidylcholine (PC) by two phospholipid N-methyltransferases (PMT I and II) in several tissues (Hirata et al., 1978; Hirata and Axelrod, 1978a,b, 1980; Crews et al., 1980; Sastry et al., 1981a, b, 1982; Sastry and Janson, 1983; Jaiswal et al., 1983), (b) formation of protein carboxymethlyesters (PCME) by protein carboxymethylase (PCM) in several cell systems (Gagnon et al., 1978, 1979; Alder, 1979; Sastry et al., 1983), and (c) methylation of endogenous fatty acids by fatty acid carboxymethylases (FACM) in several tissues (Zatz et al., 1981; Engelsen and Zatz, 1982; Stephan and Sastry, 1984, 1985).
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Barnwell, S.L., Sastry, B.V.R. (1987). S-Adenosyl-L-Methionine Mediated Enzymatic Methylations in the Plasma Membranes of the Human Trophoblast. In: Miller, R.K., Thiede, H.A. (eds) Cellular Biology and Pharmacology of the Placenta. Trophoblast Research. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1936-9_8
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