title: Inhibition of protein prenylation by patulin.
abstract: The antibiotic patulin was found to inhibit protein prenylation in mouse FM3A cells. Thus, the agent reduced incorporation of [3H]mevalonate into proteins by 50% at a concentration of 7 microM. In a cell-free assay, patulin inhibited rat brain farnesyl:protein transferase, one of the enzymes responsible for protein prenylation. The inhibition was 50% at a concentration of 290 microM.
authors.affiliation: Department of Applied Biological Science, Tokyo Noko University, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Miura
authors.forename: K
authors.initials: K
authors.lastname: Hasumi
authors.forename: A
authors.initials: A
authors.lastname: Endo
mesh_terms: D019883:Alkyl and Aryl Transferases; D000818:Animals; D001921:Brain / Q000201:enzymology; D002478:Cells, Cultured; D003513:Cycloheximide / Q000494:pharmacology; D007930:Leucine / Q000378:metabolism; D008798:Mevalonic Acid / Q000378:metabolism; D051379:Mice; D010365:Patulin / Q000494:pharmacology*; D017368:Protein Prenylation / Q000187:drug effects*; D051381:Rats; D014166:Transferases / Q000037:antagonists & inhibitors; D014255:Trichothecenes / Q000494:pharmacology
chemical_list: D014255:Trichothecenes; D010365:Patulin; D003513:Cycloheximide; C003797:roridin E; D014166:Transferases; D019883:Alkyl and Aryl Transferases; C064911:p21(ras) farnesyl-protein transferase; D007930:Leucine; D008798:Mevalonic Acid