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ICMT
Identifiers
SymbolICMT
Pfam PF04140
Pfam clan CL0115
InterPro IPR007269
OPM superfamily 159
OPM protein 4a2n
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
protein-S-isoprenylcysteine O-methyltransferase
Identifiers
EC no. 2.1.1.100
CAS no. 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 / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

The isoprenylcysteine o-methyltransferase ( EC 2.1.1.100) carries out carboxyl 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

  1. ^ 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. doi: 10.1091/mbc.12.7.1957. PMC  55642. PMID  11451995.
This article incorporates text from the public domain Pfam and InterPro: IPR007269