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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hanau, S. Capone, I. D'empaire, L. Proietti Montioli, R. Alberighi, S. Dallocchio, F. |
| Description | Author Affiliation: Hanau S ( Dept. of Biomedical and Specialty Surgical Sciences, Biochemistry Unit, Via Borsari 46, Università di Ferrara, 44121 Ferrara, Italy. Electronic address: hns@unife.it.) |
| Abstract | 6-Phosphogluconate dehydrogenase (6PGDH), the third enzyme of the pentose phosphate pathway (PPP), is essential for biosyntheses and oxidative stress defence. It also has the function of depleting 6PG, whose accumulation induces cell senescence. 6PGDH is a proposed drug target for African trypanosomiasis caused by Trypanosoma brucei and for other microbial infections and cancer. Gel filtration, density gradient sedimentation, cross-linking and dynamic light scattering were used to assay the oligomerization state of T. brucei 6PGDH in the absence and presence of several ligands. The enzyme displays a dimer–tetramer equilibrium and NADPH (but not NADP) reduces the rate of approach to equilibrium, while 6PG is able to antagonize the NADPH effect. The different behaviour of the two forms of coenzyme appears to be related to the differences in Δ $C_{p}$ , with NADP binding Δ $C_{p}$ closer to what is expected of crystallographic structures, while NADPH Δ $C_{p}$ is three times larger. The estimated dimer–tetramer association constant is 1.5 · 10 $^{6}$ M $^{−$ 1 , and the specific activity of the tetramer is about 3 fold higher than the specific activity of the dimer. Thus, cellular conditions promoting tetramer formation could allow an efficient clearing of 6PG. Experiments carried out on sheep liver 6PGDH indicate that tetramerization is a specificity of the parasite enzyme. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 12 |
| Volume Number | 1834 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2013-12-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | NADP Chemistry Phosphogluconate Dehydrogenase Protein Multimerization Physiology Trypanosoma Brucei Brucei Enzymology Animals Metabolism Species Specificity Trypanosomiasis, African Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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