Interaction of ATP with Erythroblast Glucose-6-phosphate Dehydrogenase

Paolino Ninfali, Luciano Baronciani

Research output: Contribution to journalArticlepeer-review


ATP, complexed with magnesium and as free anion, binds to rabbit erythroblasts glucose-6-phosphate dehydrogenase (G6PD) inducing significant structural transitions in the enzyme, revealed by a different heat stability. ATP4- facilitates the process of thermal inactivation by inducing the presence of thermolable forms. On the contrary, ATP-Mg protects the enzyme from thermal inactivation. The protection is significant but less marked than that shown by NADP. Kinetic studies indicate a different type of binding between ATP-Mg and ATP4-. Uncomplexed ATP is a competitive inhibitor vs NADP or G6P and it shows a positive cooperative effect. ATP-Mg is an uncompetitive inhibitor vs G6P and competitive vs NADP and it shows a negative cooperativity. A similar behaviour is also shown by complexed and free CTP and GTP.

Original languageEnglish
Pages (from-to)377-385
Number of pages9
JournalBiochemistry and Molecular Biology International
Issue number2
Publication statusPublished - 1996


  • Adenine nucleotides
  • Erythroid cells
  • G6PD
  • Post-translational modifications

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology


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