6-Phosphogluconate dehydrogenase: Structural symmetry and functional asymmetry

Title:6-Phosphogluconate dehydrogenase: Structural symmetry and functional asymmetry

Volume: 7 Issue: 5

Author(s): Mario Rippa, Stefania Hanau, Carlo Cervellati and Franco Dallocchio*

Affiliation:

• Department of Biochemistry and Molecular Biology; University of Ferrara, Via L. Borsari 46, 44100 Ferrara, Italy

Abstract: 6-Phosphogluconate dehydrogenase catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate through an oxidation, a decarboxylation and a tautomerization. The two subunits in the crystals of the dimeric sheep liver enzyme have the same conformation, as the apoenzyme and with the substrate or coenzyme. An hypothesis is now advanced that in solution, during catalysis, the two subunits have a different alternating role and thus a functional asymmetry.

Cite this article as:

Rippa Mario, Hanau Stefania, Cervellati Carlo and Dallocchio Franco*, 6-Phosphogluconate dehydrogenase: Structural symmetry and functional asymmetry, Protein & Peptide Letters 2000; 7 (5) . https://dx.doi.org/10.2174/092986650705221207143705