Regulation of C4-phosphoenolpyruvate carboxylase activity by ambient CO2
β Scribed by Y. Samaras; Y. Manetas
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 354 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0166-8595
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β¦ Synopsis
A~tract. Light activation of phosphoenolpyruvate carboxylase from the leaves of the C4 plant Setaria verticillata (L.) is more pronounced at low CO, levels. The 2-fold activation observed at physiological ambient CO2 becomes 3.64-fold at 5 #L/L and completely abolished above 700/~L/L. When the stomata close under the influence of abscisic acid at 330/~L/L CO 2, the extent of light activation is high (3.59-fold), probably because the increased diffusive resistance keeps the internal CO2 at much lower levels. Under darkness, CO2 and absicisic acid do not affect the extractable phosphoenolpyruvate carboxylase activity. Internal CO2 levels may determine phosphoenolpyruvate concentration in the cytoplasm through the control of its utilization by phosphoenolpyruvate carboxylase. We have recently proposed ) that photosynthetically produced phosphoenolpyruvate could be an activator of the enzyme. It is therefore suggested that CO, indirectly affects the activation state of phosphoenolpyruvate carboxylase by controlling the levels of phosphoenolpyruvate which may act as an activator.
π SIMILAR VOLUMES
The rate and extent of light activation of PEPC may be used as another criterion to distinguish C 3 and C 4 plants. Light stimulated phosphoenolypyruvate carboxylase (PEPC) in leaf discs of C4 plants, the activity being three times greater than that in the dark but stimulation of PEPC was limited ab
The phosphorylation state and the malate sensitivity of phosphoenolpyruvate carboxylase (PEPCase, EC 4.1.1.31) in Bryophyllumfedtschenkoi Hamet et Perrier are altered by changes in the ambient temperature. These effects, in turn alter the in-vivo activity of the enzyme. Low temperature (3 ~ or less)