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Light activation of pyruvate orthophosphate dikinase in maize mesophyll chloroplasts a role for adenylate energy charge



Light activation of pyruvate orthophosphate dikinase in maize mesophyll chloroplasts a role for adenylate energy charge



Plant and Cell Physiology 31(1): 1-6



Pyruvate, orthophosphate dikinase (EC 2.7.9.1) was activated in the light and inactivated following a dark treatment in intact maize mesophyll chloroplasts. Addition of catalase (100-250 units/ml) to the assay medium was necessary to obtain good activation and to keep the enzyme in an active state during illumination. Arsenate and carbonyl cyanide m-chlorophenyl-hydrazone, uncouplers of photophosphorylation, inhibited the activation. Pyruvate, which has been proposed to have a critical role in supporting the light activation of pyruvate, orthophosphate dikinase, actually inhibited the activation. The pyruvate level in the chloroplast suspension decreased when the enzyme was light-activated. Measurements of adenylates and pyruvate in the chloroplasts indicated that the energy state of the chloroplasts was more important for the light activation than was the level of pyruvate.

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