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PLANT PHYSIOLOGY , Vol 110, Issue 3 753-758, Copyright © 1996 by American Society of Plant Biologists
Adenylosuccinate Synthetase: Site of Action of Hydantocidin, a Microbial Phytotoxin
D. L. Siehl, M. V. Subramanian, E. W. Walters, S. F. Lee, R. J. Anderson and A. G. Toschi
Sandoz Agro, Inc., Research Division, 975 California Avenue, Palo Alto, California 94304-1104
The site of action of hydantocidin was probed using Arabidopsis thaliana
plants growing on agar plates. Herbicidal effects were reversed when the
agar medium was supplemented with AMP, but not IMP or GMP, suggesting that
hydantocidin blocked the two-step conversion of IMP to AMP in the de novo
purine biosynthesis pathway. Hydantocidin itself did not inhibit
adenylosuccinate synthetase or adenylosuccinate lyase isolated from Zea
mays. However, a phosphorylated derivative of hydantocidin,
N-acetyl-5[prime]-phosphohydantocidin, was a potent inhibitor of the
synthetase but not of the lyase. These results identify the site of action
of hydantocidin and establish adenylosuccinate synthetase as an herbicide
target of commercial potential.
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