Substrates of Protein Carboxyl Methyltransferase: Kinetics and Mechanism of their Formation
Protein carboxyl methyltransferase (PCM, EC 18.104.22.168) is an ubiquitous enzyme capable of methylating a great variety of proteins. The reaction that it catalyzes takes place in a sub-stoichiometric way. This puzzling fact was explained when Clarke and Aswad and their co-workers reported that PCM only recognizes D-aspartic and L-isoaspartic residues (for review see reference 1).
KeywordsHuman Lens Native Protein Structure Cyclic Imide Adjacent Amino Acid Aspartic Acid Racemization
Unable to display preview. Download preview PDF.
- 1.D. W. Aswad, and B. A. Johnson, The unusual substrate specificity of eukaryotic protein carboxyl methyltransferase, Trends Biochem. Sci. 155 (1987).Google Scholar
- 8.G. G. Smith, and R. C. Evans, The effect of structure and conditions on the rate of racemization of free and bound amino acids, in: “Biogeochemistry of Amino Acids”, P. E. Hare, T. C. Hoering, and K. King, eds, J. Wiley and Sons, New York (1980).Google Scholar
- 10.A. Neuberger, Stereochemistry of amino acids, Adv. Prot. Chem. 4:298 (1948).Google Scholar
- 11.P. Bornstein, and G. Balian, G., Cleavage at Asn-Gly bonds with hydroxylamine, Meth. Enzymol. 47:132 (1977).Google Scholar
- 13.L. J. Summers, G. Wistow, N. M. Narebor, D. S. Moss, P. F. Lindley, C. Slingsby, T.L. Blundell, H. Bartunik, and K. Bartels, K., X-ray studies of the lens specific proteins: the crystallins, Pept. Protein Rev. 3:147 (1984).Google Scholar