[Possible regulatory role of 5'-methylthioadenosine on enzymatic methyl esterification of membrane protein].
In the present study the effect of 5'methylthioadenosine (MTA), a natural metabolite of S-adenosylmethionine (AdoMet), on the enzymatic methyl esterification of intact erythrocyte membrane proteins has been investigated. The thioether significantly affects the methylation process :50% inhibition being observable at 100 microM MTA. This inhibition is due to the action of MTA on the enzyme protein methylase II. Since MTA is present in micromolar amounts in the cells, the reported effect could be of physiological interest and suggests a new regulatory role of this AdoMet metabolite.
D000225:Adenine / Q000494:pharmacology; D000241:Adenosine / Q000031:analogs & derivatives* / Q000494:pharmacology; D003839:Deoxyadenosines; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D008565:Membrane Proteins / Q000097:blood*; D008745:Methylation; D011497:Protein O-Methyltransferase / Q000037:antagonists & inhibitors; D012436:S-Adenosylmethionine / Q000097:blood; D013872:Thionucleosides / Q000494:pharmacology*
D003839:Deoxyadenosines; D008565:Membrane Proteins; D013872:Thionucleosides; C008500:5'-methylthioadenosine; D012436:S-Adenosylmethionine; D011497:Protein O-Methyltransferase; D000225:Adenine; D000241:Adenosine
Possibile ruolo regolatorio della 5'-metiltioadenosina sulla metil esterificazione enzimatica delle proteine di membrana.