Protein-S-isoprenylcysteine O-methyltransferase
| ICMT | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | ICMT | ||||||||
| Pfam | PF04140 | ||||||||
| Pfam clan | CL0115 | ||||||||
| InterPro | IPR007269 | ||||||||
| OPM superfamily | 344 | ||||||||
| OPM protein | 4a2n | ||||||||
| |||||||||
| protein-S-isoprenylcysteine O-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.100 | ||||||||
| CAS number | 130731-20-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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The isoprenylcysteine o-methyltransferase (EC 2.1.1.100) carries out carboyxl methylation of cleaved eukaryotic proteins that terminate in a CaaX motif. In Saccharomyces cerevisiae (Baker's yeast) this methylation is carried out by Ste14p, an integral endoplasmic reticulum membrane protein. Ste14p is the founding member of the isoprenylcysteine carboxyl methyltransferase (ICMT) family, whose members share significant sequence homology.[1]
The enzyme catalyzes the chemical 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
Thus, the two substrates of this enzyme are S-adenosyl methionine and protein C-terminal S-farnesyl-L-cysteine, whereas its two products are S-adenosylhomocysteine and protein C-terminal S-farnesyl-L-cysteine methyl ester.
References
- ↑ Romano JD, Michaelis S (July 2001). "Topological and mutational analysis of Saccharomyces cerevisiae Ste14p, founding member of the isoprenylcysteine carboxyl methyltransferase family". Mol. Biol. Cell 12 (7): 1957–71. PMC 55642. PMID 11451995.
- Clarke S, Vogel JP, Deschenes RJ, Stock J (1988). "Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases". Proc. Natl. Acad. Sci. U.S.A. 85 (13): 4643–7. doi:10.1073/pnas.85.13.4643. PMC 280491. PMID 3290900.
- Ota IM, Clarke S (1989). "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 (22): 12879–84. PMID 2753892.
- Stephenson RC, 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 (27): 16248–54. PMID 2398053.
This article incorporates text from the public domain Pfam and InterPro IPR007269