Peroxidase Phosphofructokinase

Peroxidase Phosphofructokinase Phosphofructokinase Horseradish Oligoplites mundus Rattail Rattail Rattail... 

Aspartate transcarbamylase catalytic domain 1 Phosphofructokinase domain 1 p-Hydroxybenzoate hydroxylase domain 1 Glucosephosphate isomerase domain 1 Glutathione peroxidase C. Miscellaneous parallel a/j3 Carboxypeptidase Thioredoxin Carbonic anhydrase Phosphofructokinase domain 2 Glucosephosphate isomerase domain 2 III. Antiparallel /3 domains... 

A typical chemical system is the oxidative decarboxylation of malonic acid catalyzed by cerium ions and bromine, the so-called Zhabotinsky reaction this reaction in a given domain leads to the evolution of sustained oscillations and chemical waves. Furthermore, these states have been observed in a number of enzyme systems. The simplest case is the reaction catalyzed by the enzyme peroxidase. The reaction kinetics display either steady states, bistability, or oscillations. A more complex system is the ubiquitous process of glycolysis catalyzed by a sequence of coordinated enzyme reactions. In a given domain the process readily exhibits continuous oscillations of chemical concentrations and fluxes, which can be recorded by spectroscopic and electrometric techniques. The source of the periodicity is the enzyme phosphofructokinase, which catalyzes the phosphorylation of fructose-6-phosphate by ATP, resulting in the formation of fructose-1,6 biphosphate and ADP. The overall activity of the octameric enzyme is described by an allosteric model with fructose-6-phosphate, ATP, and AMP as controlling ligands. 

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