Kinetic Properties of Phosphorylase and 6-Phosphofructokinase of Kalanchoe daigremontiana and Atriplex spongiosa

1975 ◽  
Vol 2 (3) ◽  
pp. 403 ◽  
Author(s):  
G Sutton
Keyword(s):  
Carbohydrate Metabolism ◽  
Crassulacean Acid Metabolism ◽  
Acid Metabolism ◽  
Kinetic Properties ◽  
C4 Plant ◽  
Cam Plants ◽  
Regulation Of Carbohydrate Metabolism ◽  
Cam Plant ◽  
Kalanchoë Daigremontiana ◽  
Kalanchoe Daigremontiana

The kinetic properties of phosphorylase (EC 2.4.1.1) and 6-phosphofructokinase (EC 2.7.1.11) extracted from a crassulacean acid metabolism (CAM) plant, Kalanchoe daigremontiana Hamet et Perrier, and a C4 plant, Atriplex spongiosa F. Muell., were compared. The phosphorylase from the CAM plant was strongly inhibited by P1 (1 mM), phosphoenolpyruvate (PEP) (2 mM) and glucose (4 mM). The C4 phosphorylase was less strongly inhibited by P1, and not at all by PEP or glucose. The C4 6-phosphofructokinase was, at Km levels of substrate, about 100 times more sensitive to inhibition by PEP than the CAM enzyme. These results are discussed as the basis for a biochemical regulation of carbohydrate metabolism in CAM plants at night.

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.

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