Carboxyl methyltransferases

Murray, Jr., E. D. and Clarke, S., Synthetic peptide substrates for the erythrocyte protein carboxyl methyltransferase, J. Biol. Chem., 259, 10722, 1984. 

Johnson B.A., Langmark E.L., and Aswad D.W. (1987), Partial repair of deamidation damaged calmodulin by protein carboxyl methyltransferase, J. Biol. Chem. 262, 12283-12287. 

Aswad DW. Stoichiometric methylation of porcine adrenocorticotropin by protein carboxyl methyltransferase requires deamidation of asparagine 25. Evidence for methylation at the alpha-carboxyl group of atypical L-isoaspartyl residues. J Biol Chem 1984 259 10714-10721. 

Originally isolated and characterized from the petals of Clarkia breweri, salicylic acid carboxyl methyltransferase (SAMT), converts salicylic acid to methylsalicylate.14 Methysalicylate, a volatile ester, has a characteristic wintergreen scent Apart from its putative role in defense, methylsalicylate is an important chemoattractant for moth-pollinated flowers and one of the main volatiles released from Clarkia breweri flowers.44,55 SAMT is a member of the type 3 family of plant MTs. Similarly to the previously discussed families of methyltransferases, type 3 MTs are homodimeric proteins. 

Because the three genes encoding the canonical members of this family -SAMT, BAMT, and JMT have only recently been characterized, the full extent of this family is not known. Database searches using the BLAST 2.0 program reveal a number of unknown gene products and putative SAMT -like enzymes as well as caffeine synthases belonging to the type 3 family of MTs. Thus, the family includes not only carboxyl methyltransferases but also some alkaloid N-methyltransferases. 

ROSS, J.R., NAM, K.H., D AURIA, J.C., PICHERSKY, E., S-Adenosyl-L-methionine salicylic acid carboxyl methyltransferase, an enzyme involved in floral scent production and plant defense, represents a new class of plant methyltransferases, Arch. Biochem. Biophys., 1999,367,9-16. 

CROWELL, D. N., KENNEDY, M., Identification and functional expression in yeast of a prenylcysteine alpha-carboxyl methyltransferase gene from Arabidopsis thaliana., Plant Mol.Biol, 2001,45,469-476. 

SAPPERSTEIN, S BERKOWER, C., MICHAELIS, S., Nucleotide-sequence of the yeast Stel4 Gene, which encodes famesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export., Mol Cell. Biol, 1994, 14, 1438-1449. 

MURFITT, L. M., KOLOSOVA, N., MANN, C. J., DUDAREVA, N Purification and characterization of S-adenosyl-L-methionine Benzoic acid carboxyl methyltransferase, the enzyme responsible for biosynthesis of the volatile ester methyl benzoate in flowers of Antirrhinum majus., Arch Biochem. Biophys., 2000, 382,145-151. 

A number of proteins such as histones, cytochrome c and certain flagellar proteins are found to contain methylated amino acids (19). Three different methylases have been characterized and all require S-adenosylmethionine (SAM) as the methyl donor (20-23). Protein methylase I (SAM-protein arginine methyl transferase) methylates the guanidine side chain of arginine residue protein methylase II (SAM-protein carboxyl methyltransferase) transfers methyl groups only to 8- and y-carboxyl groups in the peptide chain. Carboxyl groups in the a position cannot serve as acceptors. Protein methylase III (SAM-protein lysine... 

Romano, J.D., Schmidt, W.K., and Michaelis, S. (1998). The Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Stel4p is in the endoplasmic reticulum membrane. Mol Biol Cell 9 2231-2247. 

Griggs, A.M., Hahne, K., and Hrycyna, C.A. (2010). Functional oligomerization of the Saccharomyces cerevisiae isoprenylcysteine carboxyl methyltransferase, Stel4p. J Biol Chem 285 13380-13387. 

Biochemical and Biological Functions of IsoprenyIcysteine Carboxyl Methyltransferase... 

Stephenson, R.C., and Clarke, S. (1990). Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic farnesyl cysteine-containing peptide substrate. J Biol Chem 265 16248-16254. 

Pillinger, M.H., Volker, C., Stock, J.B., Weissmann, G., and Philips, M.R. (1994). Characterization of a plasma membrane-associated prenylcysteine-directed alpha carboxyl methyltransferase in human neutrophils. J Biol Chem 269 1486-1492. 

Wright, L.P., Court, H., Mor, A., Ahearn, I.M., Casey, P.J., and Philips, M.R. (2009). Topology of mammalian isoprenylcysteine carboxyl methyltransferase determined in live cells with a fluorescent probe. Mol Cell Biol 29 1826-1833. 

Bergo, M.O., Leung, G.K., Ambroziak, P., Otto, J.C., Casey, P.J., and Young, S.G. (2000). Targeted inactivation of the isoprenylcysteine carboxyl methyltransferase gene causes mislocalization of K-Ras in mammalian cells. J Biol Chem 275 17605-17610. 

Ahmad, M., Zhang, Y., Papharalambus, C., and Alexander, R.W. (2002). Role of isoprenylcysteine carboxyl methyltransferase in tumor necrosis factor-alpha stimulation of expression of vascular cell adhesion molecule-1 in endothelial cells. Arterioscler Thromb Vase Biol 22 759-764. 

Lu, Q., et al. (2004). Isoprenylcysteine carboxyl methyltransferase modulates endothelial monolayer permeabihty involvement of Rho A carboxyl methylation. Circ Res 94 306-315. 

Kramer, K., et al. (2003). Isoprenylcysteine carboxyl methyltransferase activity modulates endothelial cell apoptosis. Mol Biol Cell 14 848-857. 

Bergo, M.O., et at (2001). Isoprenylcysteine carboxyl methyltransferase deficiency in mice. J Biol Chem 276 5841-5845. 

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