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Plant Physiology 64:706-711 (1979)
© 1979 American Society of Plant Biologists

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Inhibition of Glycine Decarboxylation and Serine Formation in Tobacco by Glycine Hydroxamate and Its Effect on Photorespiratory Carbon Flow 1

Arthur L. Lawyer2 and Israel Zelitch

a Department of Molecular Biophysics and Biochemistry, Yale University, and Department of Biochemistry, The Connecticut Agricultural Experiment Station, New Haven, Connecticut 065043

Glycine hydroxamate is a competitive inhibitor of glycine decarboxylation and serine formation (referred to as glycine decarboxylase activity) in particulate preparations obtained from both callus and leaf tissue of tobacco. In preparations from tobacco callus tissues, the Ki for glycine hydroxamate was 0.24 ± 0.03 millimolar and the Km for glycine was 5.0 ± 0.5 millimolar. The inhibitor was chemically stable during assays of glycine decarboxylase activity, but reacted strongly when incubated with glyoxylate. Glycine hydroxamate blocked the conversion of glycine to serine and CO2in vivo when callus tissue incorporated and metabolized [1-14C]glycine, [1-14C]glycolate, or [1-14C]glyoxylate. The hydroxamate had no effect on glyoxylate aminotransferase activities in vivo, and the nonenzymic reaction between glycine hydroxamate and glyoxylate did not affect the flow of carbon in the glycolate pathway in vivo. Glycine hydroxamate is the first known reversible inhibitor of the photorespiratory conversion of glycine to serine and CO2.

2 Present address: Laboratory of Chemical Biodynamics, Lawrence Berkeley Laboratory, University of California, Berkeley, California 94720.

1 This investigation was supported in part by a National Institutes of Health National Research Service Award 5T32-GM-07223 from the Institute of General Medical Sciences to A. L. L.

3 Reprint requests should be sent to the latter address.






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ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1979 by the American Society of Plant Biologists