Abstract
S-Adenosylmethionine:protein carboxyl O-methyltransferase (EC 2.1.1.24; protein methylase II; PM II) methyl esterifies free carboxyl groups of proteins with S-adenosylmethionine (AdoMet) as the methyl donor (Kim et al., 1970; Paik et al., 1980). The protein carboxyl methyl esters formed are unstable and are enzymatically and/or spontaneously hydrolyzed yielding methanol and the unmodified protein (Paik et al., 1980). This reaction, involving the reversible neutralization of the negative charges of proteins, can be considered as an “on-off” mechanism by which a number of cellular events are regulated. The role of PM II in the synaptic function, neurose-cretory processes, and bacterial and mammalian chemotaxis has been reported by several laboratories (Paik et al., 1980; O’Dea et al., 1981). Furthermore, it has been suggested that protein methylase II could modulate the calcium-dependent cellular activities trough the methyl esterification of calmodulin (Gagnon et al., 1981). Because of the involvement of PM II in such a number of basic cellular functions, the regulatory role of the enzyme in the cell growth and differentiation appears highly conceivable.
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Galletti, P., Oliva, A., Manna, C., Ingrosso, D., Cartenì-Farina, M. (1982). Inhibition of protein carboxyl methyl esterification by 5’-methylthioadenosine. In: Biochemistry of S-Adenosylmethionine and Related Compounds. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06343-7_6
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DOI: https://doi.org/10.1007/978-1-349-06343-7_6
Publisher Name: Palgrave Macmillan, London
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