Abstract
1. 1. Pyruvate kinase of mussel foot shows positive cooperativity with respect to phosphoenolpyruvate as substrate. 2. 2. The enzyme is subject to allosteric regulation by fructose-1,6-biphosphate (FbP), alanine and adenosine triphosphate (ATP). 3. 3. The activation of the enzyme by fructose-1,6-biphosphate as well as its inhibition by alanine and ATP are pH-dependent.
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