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Information on EC 2.1.1.100 - protein-S-isoprenylcysteine O-methyltransferase and Organism(s) Mus musculus and UniProt Accession Q9EQK7

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IUBMB Comments
C-terminal S-geranylgeranylcysteine and S-geranylcysteine residues are also methylated, but more slowly.
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This record set is specific for:
Mus musculus
UNIPROT: Q9EQK7
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
ste14p, isoprenylcysteine carboxyl methyltransferase, isoprenylcysteine carboxylmethyltransferase, prenylated protein methyltransferase, isoprenylated protein methyltransferase, protein-s-isoprenylcysteine o-methyltransferase, isoprenylcysteine methylesterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isoprenylcysteine carboxyl methyltransferase
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farnesyl cysteine C-terminal methyltransferase
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-
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farnesyl-protein carboxymethyltransferase
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-
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farnesylated protein C-terminal O-methyltransferase
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-
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Icmt
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isoprenylated protein methyltransferase
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isoprenylcysteine carboxyl methyltransferase
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methyltransferase, protein C-terminal farnesylcysteine O-
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-
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prenylated protein methyltransferase
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protein S-farnesylcysteine C-terminal methyltransferase
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S-farnesylcysteine methyltransferase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:protein-C-terminal-S-farnesyl-L-cysteine O-methyltransferase
C-terminal S-geranylgeranylcysteine and S-geranylcysteine residues are also methylated, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
130731-20-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine
S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + N-acetyl-S-geranylgeranyl-L-cysteine
S-adenosyl-L-homocysteine + N-acetyl-S-geranylgeranyl-L-cysteine methyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine
S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester
show the reaction diagram
-
-
-
?
S-adenosylmethionine + N-acetyl-S-(E,E)-farnesyl-L-cysteine
S-adenosylhomocysteine + N-acetyl-S-(E,E)-farnesyl-L-cysteine methyl ester
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine
S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-acetyl-S-farnesyl-L-cysteine
competitive inhibitor
n-octyl beta-glucoside
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0.2%, 55-75% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0115
N-acetyl-S-(E,E)-farnesyl-L-cysteine
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native enzyme
0.0116
N-acetyl-S-geranylgeranyl-L-cysteine
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native enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
malfunction
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reduced enzyme activity does not affect levels of prelamin A, but instead causes mislocalization of prelamin A away fromthe nuclear rim and triggers prelamin A-dependent activation of AKT-mTOR, which decreases premature senescence of zinc metallopeptidase STE24-deficient fibroblasts
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ICMT_MOUSE
283
4
31790
Swiss-Prot
Secretory Pathway (Reliability: 3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
targeting the enzyme is an effective strategy for treating HGPS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Buckner, F.S.; Kateete, D.P.; Lubega, G.W.; Van Voorhis, W.C.; Yokoyama, K.
Trypanosoma brucei prenylated-protein carboxyl methyltransferase prefers farnesylated substrates
Biochem. J.
367
809-816
2002
Mus musculus, Trypanosoma brucei
Manually annotated by BRENDA team
Grams, D.; Lockey, R.; Kolliputi, N.
Is isoprenylcysteine carboxyl methyltransferase the key to reverse ageing?
Front. Aging Neurosci.
5
40
2013
Mus musculus
Manually annotated by BRENDA team
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
Science
340
1330-1333
2013
Mus musculus (Q9EQK7), Mus musculus
Manually annotated by BRENDA team