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2.1.1.100: protein-S-isoprenylcysteine O-methyltransferase

This is an abbreviated version!
For detailed information about protein-S-isoprenylcysteine O-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.100

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

Synonyms

EC 2.1.1.24, farnesyl cysteine C-terminal methyltransferase, farnesyl-protein carboxymethyltransferase, farnesylated protein C-terminal O-methyltransferase, Icmt, isoprenylated protein methyltransferase, isoprenylcysteine carboxyl methyltransferase, isoprenylcysteine carboxylmethyltransferase, isoprenylcysteine carboxylmethyltransferase Ste14p, isoprenylcysteine methylesterase, methyltransferase, protein C-terminal farnesylcysteine O-, prenylated protein methyltransferase, protein S-farnesylcysteine C-terminal methyltransferase, S-farnesylcysteine methyltransferase, STE14A, STE14B, Ste14p

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.100 protein-S-isoprenylcysteine O-methyltransferase

Engineering

Engineering on EC 2.1.1.100 - protein-S-isoprenylcysteine O-methyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E141A
biochemically inactive mutant
F216A
the mutant shows reduced activity compared to the wild type enzyme
F216R
the mutant shows reduced activity compared to the wild type enzyme
F216Y
the mutant shows wild type activity
W240A
the mutant shows reduced activity compared to the wild type enzyme
Y107A
the mutant shows reduced activity compared to the wild type enzyme
D122A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
E107A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
E142A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
E146A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
E251A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
E252A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
F124A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
F124R
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
F258A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
F72A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
P275A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
R209A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme, comparison of membrane topology
R63A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
RH209/210A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
S123A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
W241A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme, comparison of membrane topology
Y266A
-
site-directed mutagenesis, the mutant shows increased activity comapred to the wild-type enzyme, comparison of membrane topology
E167A
-
the mutation leads to strongly reduced activity compared to the wild type enzyme
H113A
-
the mutation leads to strongly reduced activity compared to the wild type enzyme
H126A
-
the mutation leads to strongly reduced activity compared to the wild type enzyme
R163A
-
the mutation leads to strongly reduced activity compared to the wild type enzyme
E213Q
-
the mutant is enzymatically almost inactive (5% activity compared to the wild type)
L81F
-
the mutant shows little to no in vitro methyltransferase activity
additional information