Adenylosuccinate synthetase: site of action of hydantocidin, a microbial phytotoxin

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 purin...

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Published in:	Plant physiology (Bethesda) Vol. 110; no. 3; pp. 753 - 758
Main Authors:	Siehl, D.L. (Sandoz Agro, Inc., Palo Alto, CA.), Subramanian, M.V, Walters, E.W, Lee, S.F, Anderson, R.J, Toschi, A.G
Format:	Journal Article
Language:	English
Published:	Rockville, MD American Society of Plant Physiologists 01-03-1996
Subjects:	ACIDE SUCCINIQUE ACIDO SUCCINICO ACTIVIDAD CATALITICA ACTIVITE CATALYTIQUE ADENOSINE MONOPHOSPHATE Adenosine Monophosphate - biosynthesis ADENOSINMONOFOSFATO Adenylosuccinate Lyase - drug effects Adenylosuccinate Synthase - drug effects Antidotes Arabidopsis - drug effects Arabidopsis - enzymology Arabidopsis - growth & development ARABIDOPSIS THALIANA Biological and medical sciences Biosynthesis Chemical control Corn CULTIVO DE CELULAS CULTURE DE CELLULE DESHERBAGE ENZIMAS ENZYME Enzyme Inhibitors - pharmacology Enzymes ESCARDA ESTRUCTURA QUIMICA FITOTOXINAS Fundamental and applied biological sciences. Psychology Glycine - analogs & derivatives Glycine - pharmacology HERBICIDAS HERBICIDE Herbicides Herbicides - chemistry Herbicides - pharmacology Hydantoins - chemistry Hydantoins - pharmacology INHIBIDORES DEL CRECIMIENTO INHIBITEUR DE CROISSANCE Inosine Monophosphate - metabolism MEDIO DE CULTIVO MILIEU DE CULTURE Mode of action NUCLEOTIDE NUCLEOTIDOS Parasitic plants. Weeds Pentosephosphates - pharmacology Phytopathology. Animal pests. Plant and forest protection PHYTOTOXINE Plant growth Plants Purines Rapid Communication REACCIONES QUIMICAS REACTION CHIMIQUE Seedlings STREPTOMYCES STRUCTURE CHIMIQUE VIA BIOQUIMICA DEL METABOLISMO VOIE BIOCHIMIQUE DU METABOLISME Weeds Zea mays - enzymology Amidine-lyases Carbon-nitrogen ligases Phytotoxin Enzyme Lyases Biosynthesis Herbicide Site of action Carbon-nitrogen lyases Arabidopsis thaliana Regulation(control) Enzymatic activity Microbial origin Cruciferae Ligases Dicotyledones Angiospermae Spermatophyta Adenylosuccinate synthase Purine Adenylosuccinate lyase Mechanism of action Experimental plant
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Summary:	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'-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
Bibliography:	F60 H60 9632495 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23
ISSN:	0032-0889 1532-2548
DOI:	10.1104/pp.110.3.753