Protein-S-isoprenylcysteine O-methyltransferase

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]

ICMT
Identifiers
SymbolICMT
PfamPF04140
Pfam clanCL0115
InterProIPR007269
OPM superfamily159
OPM protein4a2n
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
protein-S-isoprenylcysteine O-methyltransferase
Identifiers
EC no.2.1.1.100
CAS no.130731-20-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

This article incorporates text from the public domain Pfam and InterPro: IPR007269


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