Phosphoenolpyruvate carboxylase from pennywort (Umbilicus rupestris). Changes in properties after exposure to water stress
- 1 March 1984
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 218 (2) , 387-393
- https://doi.org/10.1042/bj2180387
Abstract
Umbilicus rupestris (pennywort) switches from C3 photosynthesis to an incomplete form of crassulacean acid metabolism (referred to as ‘CAM-idling’) when exposed to water stress (drought). This switch is accompanied by an increase in the activity of phosphoenolpyruvate carboxylase. This enzyme also shows several changes in properties, including a marked decrease in sensitivity to acid pH, a lower Km for phosphoenolpyruvate, very much decreased sensitivity to the allosteric inhibitor malate, and increased responsiveness to the allosteric effector glucose 6-phosphate. The Mr of the enzyme remains unchanged, at approx. 185 000. These changes in properties of phosphoenolpyruvate carboxylase are discussed in relation to the roles of the enzyme in C3 and in CAM plants.This publication has 8 references indexed in Scilit:
- Intracellular Localization of Enzymes of Carbon Metabolism in Mesembryanthemum crystallinum Exhibiting C3 Photosynthetic Characteristics or Performing Crassulacean Acid MetabolismPlant Physiology, 1982
- Purification and Properties of Phosphoenolpyruvate Carboxylase From Plants With Crassulacean Acid MetabolismFunctional Plant Biology, 1982
- Carbon Metabolism in Two Species of Pereskia (Cactaceae)Plant Physiology, 1981
- Day/Night Changes in the Sensitivity of Phosphoenolpyruvate Carboxylase to Malate during Crassulacean Acid MetabolismPlant Physiology, 1980
- Responses of Succulents to Plant Water StressPlant Physiology, 1978
- Regulation of phosphoenolpyruvate carboxylase of Zea mays by metabolitesBiochemical Journal, 1973
- A procedure for the electrophoretic analysis of phosphoenolpyruvate carboxylaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1973
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951