Mechanism of Protein Carboxyl Methyl Transfer Reactions: Structural Requirements of Methyl Accepting Substrates

  • Patrizia Galletti
  • Diego Ingrosso
  • Gabriele Pontoni
  • Adriana Oliva
  • Vincenzo Zappia
Part of the Advances in Experimental Medicine and Biology book series (NATO ASI F, volume 231)


The enzyme S-adenosylmethionine: protein carboxyl-O-methyltransfe-rase (PCMT) was first identified in 1965 by Axelrod and Daly as “methanol forming “ enzyme, since it was thought to catalyze the hydrolysis of S-adenosylmethionine (AdoMet) yielding methanol and S-adenosylhomocysteine (AdoHcy) (1). A few years later Liss et al. (2) and Kim and Paik (3) described an AdoMet-dependent methyl transferase which methylates free carboxyl groups in protein substrates and leads to the formation of unstable methyl esters. The two enzymes shared methanol as a common end product and were found to be identical on the basis of their properties and tissue distribution (4). During the following fifteen years the enzyme was purified from eukaryotic and prokaryotic sources, extensively characterized, and a number of different regulatory roles have been attributed to it, as reviewed by Paik and Kim in 1980 (5). However, in eukaryotes none of the hypothesized regulatory functions has been unequivocally demonstrated. More recently the eukaryotic and prokaryotic enzymes were found to differ in terms of methylation site, substrate specificity and functional role (6,7); therefore a new systematic name and classification number have been assigned to the eukaryotic PCMT. This enzyme indeed has been shown to recognize and selectively modify proteins at D-aspartyl and L-isoaspartyl residue levels (6,7).


Disulfide Bridge Methyl Esterification Isopeptide Bond Erythrocyte Membrane Protein Normal Peptide 
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Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Patrizia Galletti
    • 1
  • Diego Ingrosso
    • 1
  • Gabriele Pontoni
    • 1
  • Adriana Oliva
    • 1
  • Vincenzo Zappia
    • 1
  1. 1.Department of Biochemistry of Macromolecules, 1st Medical SchoolUniversity of NaplesNaplesItaly

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