
TY  - JOUR
A1  - Burnell, JN 
T1  - Purification and Properties of Phospho<I>enol</I>pyruvate Carboxykinase from C<sub>4</sub> Plants
JF  - Functional Plant Biology
JO  - Functional Plant Biol.
Y1  - 1986
VL  - 13
IS  - 5
SP  - 577
EP  - 587
KW  - 
UR  - https://doi.org/10.1071/PP9860577 
N2  - Phosphoenolpyruvate (PEP) carboxykinase (EC 4.1.1.49) from the leaves of Urochloa panicoides, Chloris gayana and Panicum maximum has been purified to homogeneity and its properties determined. The enzyme from all three PEP carboxykinase-type C4 plants have similar physical and kinetic properties. The native enzyme has a molecular weight of 380 000 and its monomeric molecular weight is about 64 000, suggesting the enzyme is hexameric. It is active over a wide pH range and has a pH optimum between 7.4 and 8.2, has a wide nucleotide specificity, has an absolute requirement for Mn2+ and is stimulated by C-. The enzyme is inhibited by 3-phosphoglyceric acid, fructose 6-phosphate and fructose 1,6-bisphosphate; the mechanism of inhibition is discussed. The purified PEP carboxykinase is unable to catalyse the conversion of oxaloacetate to pyruvate, nor does it possess pyruvate kinase activity. These findings are discussed in relation to the C4 photosynthetic pathway operating in PEP carboxykinase-type C4 plants. 
ER  -

