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Articles

Comparative Studies of Enzymes Related to Serine Metabolism in Higher Plants ¹

Department of Physiological Chemistry, University of Wisconsin Medical School, Madison, Wisconsin 53706

The following enzymes related to serine metabolism in higher plants have been investigated: 1) D-3-phosphoglycerate dehydrogenase, 2) phosphohydroxypyruvate:L-glutamate transaminase, 3) D-glycerate dehydrogenase, and 4) hydroxypyruvate:L-alanine transaminase. Comparative studies on the distribution of the 2 dehydrogenases in seeds and leaves from various plants revealed that D-3-phosphoglycerate dehydrogenase is widely distributed in seeds in contrast to D-glycerate dehydrogenase, which is either absent or present at low levels, and that the reverse pattern is observed in green leaves.

The levels of activity of the 4 enzymes listed above were followed in different tissues of the developing pea (Pisum sativum, var. Alaska). In the leaf, from the tenth to seventeenth day of germination, the specific activity of D-glycerate dehydrogenase increased markedly and was much higher than D-3-phosphoglycerate dehydrogenase which remained relatively constant during this time period. Etiolation resulted in a decrease in D-glycerate dehydrogenase and an increase in D-3-phosphoglycerate dehydrogenase activities. In apical meristem, on the other hand, the level of D-3-phosphoglycerate dehydrogenase exceeded that of D-glycerate dehydrogenase at all time periods studied. Low and decreasing levels of both dehydrogenases were found in epicotyl and cotyledon. The specific activities of the 2 transaminases remained relatively constant during development in both leaf and apical meristem. In general, however, the levels of phosphohydroxypyruvate:L-glutamate transaminase were comparable to those of D-3-phosphoglycerate dehydrogenase in a given tissue as were those for hydroxypyruvate: L-alanine transaminase and D-glycerate dehydrogenase.

³ Predoctoral Fellow of the United States Public Health Service.

¹ This study was supported in part by Grant AM-00922 from the National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, United States Public Health Service and by Research Contract No. AT (11-1)-1631 from the United States Atomic Energy Commission.

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				C.-L. Ho, M. Noji, M. Saito, and K. Saito Regulation of Serine Biosynthesis in Arabidopsis. CRUCIAL ROLE OF PLASTIDIC 3-PHOSPHOGLYCERATE DEHYDROGENASE IN NON-PHOTOSYNTHETIC TISSUES J. Biol. Chem., January 1, 1999; 274(1): 397 - 402. [Abstract] [Full Text] [PDF]