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Literature summary for 2.1.1.100 extracted from

  • Ibrahim, M.X.; Sayin, V.I.; Akula, M.K.; Liu, M.; Fong, L.G.; Young, S.G.; Bergo, M.O.
    Targeting isoprenylcysteine methylation ameliorates disease in a mouse model of progeria (2013), Science, 340, 1330-1333.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.100

Application

Application Comment Organism
medicine targeting the enzyme is an effective strategy for treating HGPS Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
N-acetyl-S-farnesyl-L-cysteine competitive inhibitor Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine Mus musculus
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 S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester
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 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q9EQK7
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine
-
 Mus musculus S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester
-
 ?

Synonyms

Synonyms Comment Organism
Icmt
-
 Mus musculus
isoprenylcysteine carboxyl methyltransferase
-
 Mus musculus

General Information

General Information Comment Organism
malfunction reduced enzyme activity causes prelamin A mislocalization within the nucleus and triggers prelamin A-dependent activation of AKT-mammalian target of rapamycin signaling, which abolishes the premature senescence of Zmpste24-deficient fibroblasts. Enzyme inhibition increases AKT-mammalian target of rapamycin signaling and proliferation and delays senescence in Hutchinson-Gilford progeria syndrome fibroblasts Mus musculus