Purification and characterization of phosphofructokinase from rhodotorula glutinis

Phosphofructokinase has been identified and purified from extracts of Rhodotorula glutinius. Kinetic studies of the enzyme indicated high cooperativity with respect to fructose 6-phosphate. The kinetics for ATP shows no cooperativity as indicated by the hyperbolic behavior of the enzyme. The enzyme is inhibited by ADP. Citrate and phosphate have no effect on the enzyme activity. The role of ATB, fructose 6-phosphate, and ADP is discussed.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/24371/1/0000640.pd