Inhibition of phosphomannose isomerase by fructose 1-phosphate: an explanation for defective N-glycosylation in hereditary fructose intolerance.

Jaeken, J;Pirard, M;Adamowicz, M;Pronicka, E;Van Schaftingen, Emile
(1996) Pediatric Research : international journal of human developmental biology — Vol. 40, n° 5, p. 764-766 (1996)

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  • Jaeken, J
    Author
  • Pirard, M
    Author
  • Adamowicz, M
    Author
  • Pronicka, E
    Author
  • Van Schaftingen, EmileUCLouvain
    Author
Abstract
Isoelectrofocusing of serum sialotransferrins from patients with untreated hereditary fructose intolerance (HFI) shows a cathodal shift similar to that in carbohydrate-deficient glycoprotein (CDG) syndrome type I and in untreated galactosemia. This report is on serum lysosomal enzyme abnormalities in untreated HFI that are identical to those found in CDG syndrome type I but different from those in untreated galactosemia. CDG syndrome type I is due to phosphomannomutase deficiency, a defect in the early glycosylation pathway. It was found that fructose 1-phosphate is a potent competitive inhibitor (Ki congruent to 40 microM) of phosphomannose isomerase (EC 5.3.1.8), the first enzyme of the N-glycosylation pathway thus explaining the N-glycosylation disturbances in HFI.
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Jaeken, J., Pirard, M., Adamowicz, M., Pronicka, E., & Van Schaftingen, E. (1996). Inhibition of phosphomannose isomerase by fructose 1-phosphate: an explanation for defective N-glycosylation in hereditary fructose intolerance. Pediatric Research : international journal of human developmental biology, 40(5), 764-766. https://doi.org/10.1203/00006450-199611000-00017 (Original work published 1996)