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. 1972 Jun;128(1):89-97.
doi: 10.1042/bj1280089.

The activities of fructose diphosphatase in flight muscles from the bumble-bee and the role of this enzyme in heat generation

E A Newsholme, B Crabtree, S J Higgins, S D Thornton, C Start

The activities of fructose diphosphatase in flight muscles from the bumble-bee and the role of this enzyme in heat generation

E A Newsholme et al. Biochem J. 1972 Jun.

Abstract

1. The maximum catalytic activities of fructose diphosphatase from flight muscles of bumble-bees (Bombus spp.) are at least 30-fold those reported for the enzyme from other tissues. The maximum activity of fructose diphosphatase in the flight muscle of any particular bee is similar to that of phosphofructokinase in the same muscle, and the activity of hexokinase is similar to or greater than the activity of phosphofructokinase. There is no detectable activity of glucose 6-phosphatase and only a very low activity of glucose 6-phosphate dehydrogenase in these muscles. The activities of both fructose diphosphatase and phosphofructokinase vary inversely with the body weight of the bee, whereas that of hexokinase is relatively constant. 2. There is no significant hydrolysis of fructose 1-phosphate, fructose 6-phosphate, glucose 1,6-diphosphate and glycerol 3-phosphate by extracts of bumble-bee flight muscle. 3. Fructose 1,6-diphosphatase from bumble-bee flight muscle and from other muscles is inhibited by Mn(2+) and univalent cations; the potency of inhibition by the latter varies in the order Li(+)>Na(+)>K(+). However, the fructose diphosphatase from bumble-bee flight muscle is different from the enzyme from other tissues in that it is not inhibited by AMP. 4. The contents of ATP, hexose monophosphates, fructose diphosphate and triose phosphates in bumble-bee flight muscle showed no significant changes between rest and flight. 5. It is proposed that both fructose diphosphatase and phosphofructokinase are simultaneously active and catalyse a cycle between fructose 6-phosphate and fructose diphosphate in resting bumble-bee flight muscle. Such a cycle would produce continuous hydrolysis of ATP, with the release of energy as heat, which would help to maintain the thoracic temperature during rest periods at a level adequate for flight.

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References

    1. J Biol Chem. 1966 Feb 10;241(3):632-4 - PubMed
    1. Biochem J. 1965 Jun;95:767-74 - PubMed
    1. Biochem J. 1965 Feb;94:436-45 - PubMed
    1. Biochem J. 1972 Jan;126(1):49-58 - PubMed
    1. Pflugers Arch Gesamte Physiol Menschen Tiere. 1960;270:399-412 - PubMed
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