Oat leaf phosphoglucose isomerase: competitive inhibition by erythrose-4-phosphate.
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.
Botanisches Institut der Universität, Schlossgarten 3, D-4400, Münster, Federal Republic of Germany.
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GJ
Kelly
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Latzko