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Plant Physiology 71:658-661 (1983)
© 1983 American Society of Plant Biologists

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Articles

Phosphoglycerate Dehydrogenase from Soybean Nodules 1

Partial Purification and Some Kinetic Properties

Michael J. Boland2 and Karel R. Schubert3

Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824-1319

Phosphoglycerate dehydrogenase (EC 1.1.1.95), an enzyme believed to be involved in the synthesis of serine, an intermediate in ureide biosynthesis, has been purified about 200-fold from nodules of soybean (Glycine max L. Merr. cv Amsoy 71). The reaction was reversible and exhibited a strong pH dependence with optima of 9.4 and 6.1 for the forward and reverse reactions. The Km values for the forward reaction were 0.25 millimolar for NAD+ and 0.29 millimolar for D-3-phosphoglycerate at pH 9.4, while those for the reverse reaction were 12 µM for NADH and 0.15 millimolar for 3-phosphohydroxypyruvate at pH 7.5. NADPH functioned as an alternate reductant with a Km of 0.15 millimolar. Product inhibition for the reverse reaction was competitive for NAD+ with respect to NADH and noncompetitive for phosphoglycerate with respect to phosphohydroxypyruvate. Phosphoglycerate dehydrogenase activity was dependent on inorganic ions and was not inhibited by serine.

2 On leave from the Applied Biochemistry Division, D.S.I.R., Palmerston North, New Zealand (current address) and was supported in part by a New Zealand Public Service Study Award.

3 To whom requests for reprints should be sent.

1 This work was supported by Grants 5901-0410-9-0248-0 and 82-CRCR-1-116 from the United States Department of Agriculture-Science and Education Administration Competitive Research Grants Office. This is Journal Article 10289 of the Michigan Agricultural Experiment Station.






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Copyright © 1983 by the American Society of Plant Biologists