The Enzyme Database

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EC 2.1.1.100     
Accepted name: protein-S-isoprenylcysteine O-methyltransferase
Reaction: S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester
Other name(s): farnesyl cysteine C-terminal methyltransferase; farnesyl-protein carboxymethyltransferase; protein C-terminal farnesylcysteine O-methyltransferase; farnesylated protein C-terminal O-methyltransferase; isoprenylated protein methyltransferase; prenylated protein methyltransferase; protein S-farnesylcysteine C-terminal methyltransferase; S-farnesylcysteine methyltransferase; prenylcysteine carboxylmethyltransferase [misleading]; prenylcysteine carboxymethyltransferase [misleading]; prenylcysteine methyltransferase
Systematic name: S-adenosyl-L-methionine:protein-C-terminal-S-farnesyl-L-cysteine O-methyltransferase
Comments: C-terminal S-geranylgeranylcysteine and S-geranylcysteine residues are also methylated, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 130731-20-3
References:
1.  Clarke, S., Vogel, J.P., Deschenes, R.J. and Stock, J. Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases. Proc. Natl. Acad. Sci. USA 85 (1988) 4643–4647. [PMID: 3290900]
2.  Ota, I.M. and Clarke, S. Enzymatic methylation of 23-29-kDa bovine retinal rod outer segment membrane proteins. Evidence for methyl ester formation at carboxyl-terminal cysteinyl residues. J. Biol. Chem. 264 (1989) 12879–12884. [PMID: 2753892]
3.  Stephenson, R.C. and Clarke, S. Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic farnesyl cysteine-containing peptide substrate. J. Biol. Chem. 265 (1990) 16248–16254. [PMID: 2398053]
[EC 2.1.1.100 created 1992 (EC 2.1.1.24 created 1972, modified 1983, modified 1989, part incorporated 1992)]
 
 


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