Oreganic Acid, a Potent Inhibitor of Ras Farnesyl-Protein Transferase
| Autor: | Sheo B. Singh, Keith C. Silverman, Dolores Vilella, Rosalind G. Jenkins, Hiranthi Jayasuriya, Russell B. Lingham, Gerald F. Bills, Carmen Cascales |
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| Rok vydání: | 1997 |
| Předmět: |
Farnesyl Protein Transferase
Stereochemistry Biophysics Peptide Oncogene Protein p21(ras) environment and public health Biochemistry Substrate Specificity Sulfation Transferases Humans Transferase Molecular Biology chemistry.chemical_classification Alkyl and Aryl Transferases biology Chemistry organic chemicals Fungi Tricarboxylic Acids Active site Cell Biology Tricarboxylic acid Enzyme Oreganic acid biology.protein lipids (amino acids peptides and proteins) |
| Zdroj: | Biochemical and Biophysical Research Communications. 232:478-481 |
| ISSN: | 0006-291X |
| Popis: | A sulfated tricarboxylic acid fungal metabolite is an inhibitor of human farnesyl-protein transferase (FPTase). The compound, designated as oreganic acid, has a molecular weight of 494, an empirical formula of C22H38O10S and inhibits FPTase with an IC50value of 14 nM. Oreganic acid is a selective inhibitor of FPTase because it does not inhibit human geranylgeranyl-protein transferase type I (GGPTase-I). It is not a time-dependent inhibitor, reversibly inhibits FPTase, is competitive with respect to farnesyl diphosphate and non-competitive with respect to the Ras acceptor peptide. The structure of oreganic acid resembles that of farnesyl diphosphate and most likely inhibits FPTase by mimicking farnesyl diphosphate at the active site of the enzyme. |
| Databáze: | OpenAIRE |
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