In-situ evidence for the involvement of calcium and bundle-sheath-derived photosynthetic metabolites in the C4 phosphoenolpyruvate-carboxylase kinase signal-transduction chain

Planta ◽  
1996 ◽  
Vol 199 (3) ◽  
Author(s):  
StephenM.G. Duff ◽  
Nathalie Giglioli-Guivarc'h ◽  
Jean-No�l Pierre ◽  
Jean Vidal ◽  
ShirleyA. Condon ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Phosphoenolpyruvate Carboxylase ◽  
Bundle Sheath ◽  
Phosphoenolpyruvate Carboxylase Kinase

The unique phosphoenolpyruvate carboxylase kinase

2003 ◽  
Vol 41 (6-7) ◽  
pp. 541-547 ◽  
Author(s):  
Cristina Echevarria ◽  
Jean Vidal
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Phosphoenolpyruvate Carboxylase Kinase

scholarly journals Malate content of picoliter samples of Raphanus sativus cytoplasm.

1991 ◽  
Vol 39 (4) ◽  
pp. 435-440 ◽  
Author(s):  
M J Bodson ◽  
W H Outlaw ◽  
S H Silvers
Keyword(s):  
Root Hair ◽  
Phosphoenolpyruvate Carboxylase ◽  
Raphanus Sativus ◽  
Organic Anion ◽  
Root Hairs ◽  
Interactive Effects ◽  
Plant Metabolism ◽  
Individual Root

Malate, which plays many essential roles in plant metabolism, is a potent in vitro inhibitor of the cytosolic enzyme phosphoenolpyruvate carboxylase (PEPC). Because PEPC activity leads to malate biosynthesis, malate is assumed to attenuate its own synthesis in situ. To test this hypothesis, we measured directly the malate content of picoliter samples of Raphanus root-hair cytoplasm using quantitative histochemical techniques. We also obtained an estimate for malate accumulation in these cells. These values were compared with the PEPC activity of individual root hairs (less than 2 ng). The results indicate that high cytoplasmic malate concentration does not severely inhibit PEPC in situ. We suggest that the focus for studies on the regulation of organic anion accumulation be on the interactive effects of malate and other PEPC effectors.

Factors involved in the rise of phosphoenolpyruvate carboxylase-kinase activity caused by salinity in sorghum leaves

Planta ◽  
2013 ◽  
Vol 237 (5) ◽  
pp. 1401-1413 ◽  
Author(s):  
José A. Monreal ◽  
Cirenia Arias-Baldrich ◽  
Francisco Pérez-Montaño ◽  
Jacinto Gandullo ◽  
Cristina Echevarría ◽  
...  
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Kinase Activity ◽  
Phosphoenolpyruvate Carboxylase Kinase

How to tell the time: the regulation of phosphoenolpyruvate carboxylase in Crassulacean acid metabolism (CAM) plants

2003 ◽  
Vol 31 (3) ◽  
pp. 728-730 ◽  
Author(s):  
H.G. Nimmo
Keyword(s):  
Circadian Rhythms ◽  
Phosphoenolpyruvate Carboxylase ◽  
Crassulacean Acid Metabolism ◽  
Acid Metabolism ◽  
Circadian Oscillator ◽  
Cam Plants ◽  
Reversible Phosphorylation ◽  
Circadian Expression ◽  
Phosphoenolpyruvate Carboxylase Kinase ◽  
Co2 Metabolism

Crassulacean acid metabolism (CAM) plants exhibit persistent circadian rhythms of CO2 metabolism. These rhythms are driven by changes in the flux through phosphoenolpyruvate carboxylase, which is regulated by reversible phosphorylation in response to a circadian oscillator. This article reviews progress in our understanding of the circadian expression of phosphoenolpyruvate carboxylase kinase.

scholarly journals Arabidopsis thaliana contains two phosphoenolpyruvate carboxylase kinase genes with different expression patterns

2002 ◽  
Vol 25 (1) ◽  
pp. 115-122 ◽  
Author(s):  
V. Fontaine ◽  
J. Hartwell ◽  
G. I. Jenkins ◽  
H. G. Nimmo
Keyword(s):  
Arabidopsis Thaliana ◽  
Phosphoenolpyruvate Carboxylase ◽  
Expression Patterns ◽  
Phosphoenolpyruvate Carboxylase Kinase

Regulation of phosphoenolpyruvate carboxylase: an example of signal transduction via protein phosphorylation in higher plants

1990 ◽  
Vol 30 ◽  
pp. 121-131 ◽  
Author(s):  
Hugh G. Nimmo ◽  
Pamela J. Carter ◽  
Charles A. Fewson ◽  
Gavin A.L. McNaughton ◽  
Gillian A. Nimmo ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Phosphorylation ◽  
Phosphoenolpyruvate Carboxylase ◽  
Higher Plants

A fundamental thermostable cyanide-sensitive phosphoenolpyruvate acid carboxylase in photosynthetic and other organisms

1971 ◽  
Vol 49 (4) ◽  
pp. 631-643 ◽  
Author(s):  
David Pan ◽  
E. Roy Waygood
Keyword(s):  
Heat Treatment ◽  
Zea Mays ◽  
Acid Phosphatase ◽  
Plant Species ◽  
Phosphoenolpyruvate Carboxylase ◽  
Deae Cellulose ◽  
Bundle Sheath ◽  
Evolutionary Significance ◽  
Optimum Temperature ◽  
Optimum Ph

A thermostable 'phosphoenolpyruvate carboxylase' has been isolated from leaves of Zea mays different from phosphoenolpyruvate carboxylase (EC. 4.1.1.31) in that its optimum pH is 5.4, it does not liberate orthophosphate during the reaction, and it is inhibited by cyanide. The enzymic reaction has an optimum temperature of 70–75C and has been purified through steps including acidification to pH 4.6, heat treatment to 50C, and DEAE-cellulose and Sephadex G-200 column chromatography. Three fractions were active in the Sephadex eluate, but only fraction III was free from a thermostable acid phosphatase which catalyzes the liberation of orthophosphate from the substrate and the end product which is suggested to be a C4 phosphocarbonyl compound, although phosphohydroxypyruvate appears by either spontaneous or enzymic decarboxylation. The enzyme is assayed by the formation of a phenyl-hydrazone at 325 nm. The enzyme is localized and tightly bound in both the parenchyma bundle sheath and mesophyll chloroplasts, which are free from the thermostable acid phosphatase. Similar concentrations of the enzyme have been found in all plant species tested including C3 plants, ferns, bryophytes, algae, fungi, and even in calf liver. The enzyme must have considerable evolutionary significance.

Sign in / Sign up

Export Citation Format

Share Document