Crassulacean acid metabolism (CAM) in Kalancho� daigremontiana: Temperature response of phosphoenolpyruvate (PEP)-carboxylase in relation to allosteric effectors

Planta ◽  
1981 ◽  
Vol 152 (3) ◽  
pp. 181-188 ◽  
Author(s):  
I. C. Buchanan-Bollig ◽  
M. Kluge
Keyword(s):  
Crassulacean Acid Metabolism ◽  
Acid Metabolism ◽  
Temperature Response ◽  
Pep Carboxylase ◽  
Allosteric Effectors

Purification and Properties of Phosphoenolpyruvate Carboxylase From Plants With Crassulacean Acid Metabolism

1982 ◽  
Vol 9 (4) ◽  
pp. 409 ◽  
Author(s):  
DL Nott ◽  
CB Osmond
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Functional Significance ◽  
Crassulacean Acid Metabolism ◽  
Acid Metabolism ◽  
Sodium Dodecyl ◽  
Kinetic Properties ◽  
Cam Plants ◽  
Pep Carboxylase ◽  
Purification And Properties ◽  
Ph Dependent

Phosphoenolpyruvate (PEP) carboxylase was purified from three species of crassulacean acid metabolism (CAM) plants. There was no evidence for isoenzymes of PEP carboxylase in these plants and the purified protein was an active dimer of Mr 220 000-250 000 which dissociated to a monomer of Mr 110 000 after treatment with sodium dodecyl sulfate. Active, higher aggregates could be obtained on Sepharose 6B but the functional significance, if any, of these remains to be assessed. In the absence of effectors, normal Michaelis-Menten kinetics were obtamed with the substrates HCO3- and PEP. The purified enzyme shows a preference for HCO3-, rather than CO2, at pH 6.1 and 8.1, with a Km (HCO3-) of 10-20 �M. The Vmax was relatively independent of pH between pH 5.5 and 8.5, but the Km (PEP) (like most other kinetic properties) was pH dependent with a minimum of about 0.1 mM PEP at pH 6.8. Malate inhibition was more effective at pH 6.2 than at pH 8.2, and the inhibition evidently involved a slow binding of malate which increased the Km (PEP) and resulted in non-hyperbolic kinetics. The Km (PEP) was lowered about 5-10-fold by 1.0 mM glucose 6-phosphate which also overcame malate inhibition and restored hyperbolic kinetic relationships in the presence of malate. Possible roles for these properties in the regulation of CAM are discussed.

Induction of Crassulacean Acid Metabolism in Mesembryanthemum: Mass Increase and De-Novo Synthesis of Pep Carboxylase

1987 ◽  
pp. 669-669
Author(s):  
J. M. Schmitt ◽  
R. Höfner ◽  
C. B. Michalowski ◽  
S. W. Olson ◽  
L. Vazquez-Moreno ◽  
...  
Keyword(s):  
Crassulacean Acid Metabolism ◽  
Acid Metabolism ◽  
De Novo ◽  
De Novo Synthesis ◽  
Pep Carboxylase ◽  
Mass Increase

Glycolysis in CAM Plants

1975 ◽  
Vol 2 (3) ◽  
pp. 389 ◽  
Author(s):  
BG Sutton
Keyword(s):  
Malic Acid ◽  
Crassulacean Acid Metabolism ◽  
Acid Metabolism ◽  
Amylase Activity ◽  
Acid Synthesis ◽  
Glycolytic Enzyme ◽  
Kinetic Characteristics ◽  
Cam Plants ◽  
Pep Carboxylase ◽  
High Level

Enzymes involved in the movement of carbon from glucan to malic acid in the crassulacean acid metabolism (CAM) plant, Kalanchoe daigremontiana were assayed. The kinetic characteristics determined for the enzymes from this plant were similar to those already known for the same enzymes from non-CAM tissue. °-Amylase activity could not be demonstrated in the CAM leaf and glucokinase activity was low. These results, together with a high level of phosphorylase, suggested that the latter enzyme was involved in trasfer of glucan breakdown products to glycolysis. The activity of pyruvate kinase was only 1.7% of the activity of phosphoenolpyruvate (PEP) carboxylase, suggesting that pyruvate production from PEP at night posed little drain on PEP supply for malic acid synthesis. Starch losses and glycolytic enzyme activities of non-CAM plants were sufficient to allow dark acidification comparable to that of CAM plants.

scholarly journals Induction of PEP Carboxylase and Crassulacean Acid Metabolism by Gibberellic Acid in Mesembryanthemum crystallinum

2001 ◽  
Vol 42 (2) ◽  
pp. 236-239 ◽  
Author(s):  
Lonnie J. Guralnick ◽  
Maurice S. B. Ku ◽  
Gerald E. Edwards ◽  
Darren Strand ◽  
Brandon Hockema ◽  
...  
Keyword(s):  
Gibberellic Acid ◽  
Crassulacean Acid Metabolism ◽  
Acid Metabolism ◽  
Mesembryanthemum Crystallinum ◽  
Pep Carboxylase

scholarly journals Differential proteomic analysis by SWATH-MS unravels the most dominant mechanisms underlying yeast adaptation to non-optimal temperatures under anaerobic conditions

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Tânia Pinheiro ◽  
Ka Ying Florence Lip ◽  
Estéfani García-Ríos ◽  
Amparo Querol ◽  
José Teixeira ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Temperature Response ◽  
Laboratory Strain ◽  
Temperature Tolerance ◽  
Anaerobic Conditions ◽  
Cold Response ◽  
Proteomic Data ◽  
Response To Temperature

AbstractElucidation of temperature tolerance mechanisms in yeast is essential for enhancing cellular robustness of strains, providing more economically and sustainable processes. We investigated the differential responses of three distinct Saccharomyces cerevisiae strains, an industrial wine strain, ADY5, a laboratory strain, CEN.PK113-7D and an industrial bioethanol strain, Ethanol Red, grown at sub- and supra-optimal temperatures under chemostat conditions. We employed anaerobic conditions, mimicking the industrial processes. The proteomic profile of these strains in all conditions was performed by sequential window acquisition of all theoretical spectra-mass spectrometry (SWATH-MS), allowing the quantification of 997 proteins, data available via ProteomeXchange (PXD016567). Our analysis demonstrated that temperature responses differ between the strains; however, we also found some common responsive proteins, revealing that the response to temperature involves general stress and specific mechanisms. Overall, sub-optimal temperature conditions involved a higher remodeling of the proteome. The proteomic data evidenced that the cold response involves strong repression of translation-related proteins as well as induction of amino acid metabolism, together with components related to protein folding and degradation while, the high temperature response mainly recruits amino acid metabolism. Our study provides a global and thorough insight into how growth temperature affects the yeast proteome, which can be a step forward in the comprehension and improvement of yeast thermotolerance.

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