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Literature summary for 2.1.1.100 extracted from

  • Diver, M.M.; Long, S.B.
    Mutational analysis of the integral membrane methyltransferase isoprenylcysteine carboxyl methyltransferase (ICMT) reveals potential substrate binding sites (2014), J. Biol. Chem., 289, 26007-26020.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.100

Protein Variants

Protein Variants Comment Organism
E141A biochemically inactive mutant Anopheles gambiae
F216A the mutant shows reduced activity compared to the wild type enzyme Anopheles gambiae
F216R the mutant shows reduced activity compared to the wild type enzyme Anopheles gambiae
F216Y the mutant shows wild type activity Anopheles gambiae
W240A the mutant shows reduced activity compared to the wild type enzyme Anopheles gambiae
Y107A the mutant shows reduced activity compared to the wild type enzyme Anopheles gambiae
Y212A inactive Anopheles gambiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0048
-
 S-adenosyl-L-methionine mutant enzyme F216Y, at pH 7.4 and 25°C Anopheles gambiae
0.0067
-
 S-adenosyl-L-methionine wild type enzyme, at pH 7.4 and 25°C Anopheles gambiae
0.0084
-
 S-adenosyl-L-methionine wild type enzyme, at pH 7.4 and 25°C Homo sapiens
0.0094
-
 S-adenosyl-L-methionine mutant enzyme F216R, at pH 7.4 and 25°C Anopheles gambiae
0.018
-
 S-adenosyl-L-methionine mutant enzyme Y107A, at pH 7.4 and 25°C Anopheles gambiae
0.022
-
 S-adenosyl-L-methionine mutant enzyme F216A, at pH 7.4 and 25°C Anopheles gambiae
0.026
-
 S-adenosyl-L-methionine mutant enzyme W240A, at pH 7.4 and 25°C Anopheles gambiae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral membrane protein Homo sapiens 16020
-
membrane integral membrane protein Anopheles gambiae 16020
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Anopheles gambiae Q7PXA7
-
-
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + biotin-S-farnesyl-L-cysteine
-
 Homo sapiens S-adenosyl-L-homocysteine + biotin-S-farnesyl-L-cysteine methyl ester
-
 ?
S-adenosyl-L-methionine + biotin-S-farnesyl-L-cysteine
-
 Anopheles gambiae S-adenosyl-L-homocysteine + biotin-S-farnesyl-L-cysteine methyl ester
-
 ?
S-adenosyl-L-methionine + Ras protein C-terminal S-farnesyl-L-cysteine
-
 Homo sapiens S-adenosyl-L-homocysteine + Ras protein C-terminal S-farnesyl-L-cysteine methyl ester
-
 ?
S-adenosyl-L-methionine + Ras protein C-terminal S-farnesyl-L-cysteine
-
 Anopheles gambiae S-adenosyl-L-homocysteine + Ras protein C-terminal S-farnesyl-L-cysteine methyl ester
-
 ?

Synonyms

Synonyms Comment Organism
Icmt
-
 Homo sapiens
Icmt
-
 Anopheles gambiae
isoprenylcysteine carboxyl methyltransferase
-
 Homo sapiens
isoprenylcysteine carboxyl methyltransferase
-
 Anopheles gambiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.5
-
 S-adenosyl-L-methionine wild type enzyme, at pH 7.4 and 25°C Anopheles gambiae
0.93
-
 biotin-S-farnesyl-L-cysteine wild type enzyme, at pH 7.4 and 25°C Anopheles gambiae
1.25
-
 S-adenosyl-L-methionine wild type enzyme, at pH 7.4 and 25°C Homo sapiens