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l-Glutamined-Fructose-6-P aminotransferase regulation by glucose-6-P and UDP-N-Acetylglucosamine

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Abstract

l-Glutamined-Fructose-6-P aminotransferase regulates hexosamine synthesis. An affinity purified human fibroblast aminotransferase and specific radioisotope assays developed by us were used to show an independent inhibition of the aminotransferase by Glucose-6-P. More interestingly, at concentration of UDP-N-Acetylglucosamine and glucose-6-P where either sugar has no independent inhibitory effect, there is an allosteric and significant inhibition of the aminotransferase.

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Authors and Affiliations

  1. Neurogenetics and Cell Biology Laboratory Department of Medicine, Duke University Medical Center, 27710, Durham, North Carolina

    A. Tourian, M. Callahan & W. Hung

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  1. A. Tourian
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  2. M. Callahan
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  3. W. Hung
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Tourian, A., Callahan, M. & Hung, W. l-Glutamined-Fructose-6-P aminotransferase regulation by glucose-6-P and UDP-N-Acetylglucosamine. Neurochem Res 8, 1589–1595 (1983). https://doi.org/10.1007/BF00964160

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  • DOI: https://doi.org/10.1007/BF00964160

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