Catalytic and regulatory properties of pyruvate kinase isozymes from octopus mantle muscle and liver.

Abstract

The octopus is a relatively slow-moving animal that relies upon burst swimming to power its predatory activities. Pyruvate kinase (EC, 2.7.1.40), as one of the major glycolytic control sites, must be regulated in such a fashion to allow the increased glycolytic rate characteristic of burst metabolism. The mantle enzyme is regulated by the concerted action of ATP, arginine phosphate, and citrate. The Km for ADP was 0.28 mM and that for phosphoenolpyruvate (PEP), 0.25 mM. In contrast to many other invertebrate muscle pyruvate kinases, the enzyme is insensitive to fructose-1,6-diphosphate (FDP) activation.The pyruvate kinase from the liver is kinetically and electrophoretically distinct from the mantle enzyme. The liver isozyme has a considerably lower affinity for PEP (Km = 0.85 mM), is inhibited by ATP, citrate, and arginine phosphate, and is subject to a strong activation by FDP (Ka = 1 × 10−6). These differences between the pyruvate kinases from catabolic and synthetic tissues are reminiscent of the distinctions between mammalian muscle and liver pyruvate kinases.