Abstract

Glyphosine [N, N-bis-(phosphonomethyl) glycine] inhibited maize leaf P-enolpyruvate carboxylase competitively with respect to P-enolpyruvate. The inhibition was dependent on glyphosine concentration and pH. Glycine, but not glucose-6-phosphate, protected the enzyme from the effect of glyphosine. A related compound, glyphosate [N-(phosphonomethyl) glycine], produced little or no inhibition. P-enolpyruvate carboxylase could be one of the targets of glyphosine action, causing growth inhibition as reported (Croft, S. M., C. J. Arntzen, L. N. Vanderhoef and C. S. Zettinger (1974) Biochim. Biophys. Acta 335: 211-217).

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