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Chloroplast and Cytoplasmic Enzymes

VI. Pea Leaf 3-Phosphoglycerate Kinases ¹

^a Department of Biological Sciences, University of Illinois at Chicago Circle, Chicago, Illinois 60680

Pea (Pisum sativum) leaf chloroplastic and cytoplasmic 3-phosphoglycerate kinases (ATP: D-3-phosphoglycerate 1-phosphotransferase, EC 2.7.2.3) have similar Michaelis constants for ATP, 0.7 and 0.55 mM, for ADP, 0.18 and 0.22, and for 3-P-glycerate, 0.59 and 0.54 mM at low substrate concentrations, and 1.6 and 1.25 mM at high substrate concentrations. Both enzymes are inhibited by ADP and AMP in the ATP-utilizing direction and by ATP and AMP in the ATP-generating direction and are controlled by energy charge. Apparently, whether the cytoplasmic and chloroplastic kinases in the plant cell will participate in the reductive pentose phosphate cycle and gluconeogenesis or in glycolysis will be determined by the environment in the cell compartment and not by the differential properties of the enzymes themselves.

¹ This research was supported by grants from the National Science Foundation (GB 28160) and University of Illinois, Chicago Circle, Research Board to L. E. A. and Sigma Xi to I. P. This study is included in a thesis submitted by Ivan Pacold to the Graduate School, University of Illinois at Chicago Circle, in partial fulfillment of the requirements for the degree of Master of Science.