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Oat leaf phosphoglucose isomerase: competitive inhibition by erythrose-4-phosphate

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Abstract

Phosphoglucose isomerase was partially purified from oat leaves and shown to be strongly inhibited by erythrose-4-P. Estimated Ki values were between 0.4 and 4.0 μM. The inhibition was of the competitive type with respect to either of the substrates glucose-6-P and fructose-6-P. Several other plant phosphoglucose isomerases were found to be similarly sensitive to erythrose-4-P.

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Author notes

  1. Erwin Latzko

    Present address: Department of Biochemistry and Nutrition, University of New England, 2351, Armidale, N.S.W., Australia

Authors and Affiliations

  1. Botanisches Institut der Universität, Schlossgarten 3, D-4400, Münster, Federal Republic of Germany

    Grahame J. Kelly & Erwin Latzko

Authors
  1. Grahame J. Kelly
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  2. Erwin Latzko
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Kelly, G.J., Latzko, E. Oat leaf phosphoglucose isomerase: competitive inhibition by erythrose-4-phosphate. Photosynth Res 1, 181–187 (1980). https://doi.org/10.1007/BF00020597

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  • DOI: https://doi.org/10.1007/BF00020597

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