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ARS Home » Pacific West Area » Albany, California » Western Regional Research Center » Crop Improvement and Genetics Research » Research » Publications at this Location » Publication #169892
Title: PROTEIN FARNESYLTRANSFERASE INHIBITORS INTERFERE WITH FARNESYL DIPHOSPHATE BINDING BY RUBBER TRANSFERASE

Author
item Mau, Christopher
item GARNEAU, SYLVIE - DEPT OF CHEMISTRY
item SCHOLTE, ANDREW - DEPT OF CHEMISTRY
item Van Fleet, Jennifer
item VEDERAS, JOHN - DEPT OF CHEMISTRY
item Cornish, Katrina

Submitted to: European Journal of Biochemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 1/1/2003
Publication Date: 10/1/2003
Citation: Mau, C.J., Garneau, S., Scholte, A., Van Fleet, J.E., Vederas, J., Cornish, K. Protein farnesyltransferase inhibitors interfere with farnesyl diphosphate binding by rubber transferase. 2003. European Journal of Biochemistry. 270(19):3939-3945.

Interpretive Summary:

Technical Abstract: Rubber transferase, a cis -prenyltransferase, catalyzes the addition of thousands of isopentenyl diphosphate (IPP) molecules to an allylic diphosphate initiator, such as farnesyl diphosphate (FPP, 1 ), in the presence of a divalent metal cofactor. In an effort to characterize the catalytic site of rubber transferase, the effects of two types of protein farnesyltransferase inhibitors, several chaetomellic acid A analogs (2 , 4'7 ) and -hydroxyfarnesylphosphonic acid (3 ), on the ability of rubber transferase to add IPP to the allylic diphosphate initiator were determined. Both types of compounds inhibited the activity of rubber transferases from Hevea brasiliensis and Parthenium argentatum , but there were species'specific differences in the inhibition of rubber transferases by these compounds. Several shorter analogs of chaetomellic acid A did not inhibit rubber transferase activity, even though the analogs contained chemical features that are present in an elongating rubber molecule. These results indicate that the initiator-binding site in rubber transferase shares similar features to FPP binding sites in other enzymes.