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Evolution of the functional properties of pyruvate kinase isozymes: pyruvate kinase L fromRana pipiens

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Summary

The regulatory properties of type L pyruvate kinase fromRana pipiens are intermediate between those of the mammalian K and L isozymes. As with mammalian type L, the levels of the frog isozyme are affected by the animal's nutritional state. The mammalian and amphibian isozymes show similar sensitivities to fructose 1,6-bisphosphate activation and amino acid inhibition. By contrast, the frog L isozyme shares several properties of the K class: ie. irreversible inactivation by oxidized glutathione and lack of response to a cyclic AMP stimulated phosphorylation. Furthermore, as for some mammalian K isozymes, frog type L shows a high PEP affinity and a low cooperativity of PEP binding.

Insofar as the properties of this present day enzyme reflect those of its counterpart in the amphibian ancestor of higher vertebrates, our results suggest that at its first expression, the type L resembled the type K. Many important regulatory properties of the L isozyme, especially the sensitivity to phosphorylation, were acquired more recently perhaps in association with an increased importance of constant blood glucose.

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Abbreviations

DTT :

dithiothreitol

EDTA :

ethylenediamine tetraacetic acid

EGTA :

ethyleneglycol-bis(2-aminoethylether)-N,N′-tetraacetic acid

FB :

fructose-1,6-bisphosphate

PEP :

phosphoenolpyruvate

PK :

pyruvate kinase

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  1. Départment de Biologie, Université Laval, P.Q., Québec, Canada, G1K 7P4

    Paul Fournier & Helga Guderley

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  1. Paul Fournier
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  2. Helga Guderley
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Fournier, P., Guderley, H. Evolution of the functional properties of pyruvate kinase isozymes: pyruvate kinase L fromRana pipiens . J Comp Physiol B 156, 691–699 (1986). https://doi.org/10.1007/BF00692747

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