| Autor: |
Senoo, Satoshi, Iida, Tetsuji, Shouda, Kou, Sato, Yukiharu, Nicolaus, Beate, Böger, Peter, Wakabayashi, Ko |
| Zdroj: |
Zeitschrift für Naturforschung C; August 1996, Vol. 51 Issue: 7-8 p518-526, 9p |
| Abstrakt: |
A simple model thiadiazolidine, 5-(4-methoxycarbonylmethylthio-phenylimino)-3,4-tetra-methylene-1,3,4-thiadiazolidin-2-one, was synthesized and its structural modification investigated using glutathione S-transferase (GST) and an esterase preparation isolated from Echinochloa utilis. The objective is a better understanding of the metabolic activation of peroxidizing thiadiazolidine compounds. The model thiadiazolidine with an ester group (thiadiazolidine ester) was isomerized by GST to a more phytotoxic triazolidine structure (triazolidine ester). Both the thiadiazolidine and the more active triazolidine ester were hydrolyzed by Echinochloa esterase to less active free acid compounds. 5-(4-carboxymethylthiophenylimino)-3,4-tetramethylene-1,3,4-thiadiazolidin-2-one (thiadiazolidine acid) and 4-(4-carboxy-methylthiophenyl)-1,2-tetramethylene-1,2,4-triazolidin-3-one-5-thione (triazolidine acid), respectively. The thiadiazolidine acid, however, was only slightly converted into the triazolidine acid in the presence of GST. It is concluded that the thiadiazolidine ester was isomerized in Echinochloa to give the triazolidine acid through the triazolidine ester. Since the triazolidine ester exhibited the highest phytotoxic peroxidizing activity GST is considered as an activating enzyme for phytotoxicity and esterase as a detoxifying enzyme to reduce phytotoxic activity. Accordingly, phytotoxic thiadiazolidine-ester type herbicides may be produced by an interplay of isomerizing GST and esterase activity contributing to herbicide selectivity among plant species. |
| Databáze: |
Supplemental Index |
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