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Literature summary for 2.1.1.100 extracted from

  • Baron, R.A.; Peterson, Y.K.; Otto, J.C.; Rudolph, J.; Casey, P.J.
    Time-dependent inhibition of isoprenylcysteine carboxyl methyltransferase by indole-based small molecules (2007), Biochemistry, 46, 554-560.
    View publication on PubMed

Application

Application Comment Organism
medicine target in anticancer drug design Spodoptera frugiperda

Inhibitors

Inhibitors Comment Organism Structure
cysmethynil time-dependent inhibitor, competitive inhibitor with respect to the isoprenylated cysteine substrate and a noncompetitive inhibitor with respect to S-adenosyl-L-methionine Spodoptera frugiperda
additional information decrease in the length versus hydrophobicity of the indole nitrogen substituent is accompanied by loss of the time-dependent properties of this indole class of Icmt inhibitors Spodoptera frugiperda

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0029
-
farnesylated and Rce1-proteolyzed K-Ras protein
-
Spodoptera frugiperda
0.0071
-
S-adenosyl-L-methionine
-
Spodoptera frugiperda

Organism

Organism UniProt Comment Textmining
Spodoptera frugiperda
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
SF-9 cell
-
Spodoptera frugiperda
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + farnesylated and Rce1-proteolyzed K-Ras protein
-
Spodoptera frugiperda ?
-
?

Synonyms

Synonyms Comment Organism
Icmt
-
Spodoptera frugiperda
isoprenylcysteine carboxyl methyltransferase
-
Spodoptera frugiperda

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0022
-
cysmethynil with respect to farnesylated and Rce1-proteolyzed K-Ras protein as substrate Spodoptera frugiperda
0.00239
-
cysmethynil with respect to S-adenosyl-L-methionine as substrate Spodoptera frugiperda