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- Title
Comparative analysis of two glyceraldehyde-3-phosphate dehydrogenases from a thermoacidophilic archaeon, Sulfolobus tokodaii
- Authors
Ito, Fumiaki; Chishiki, Hidehiro; Fushinobu, Shinya; Wakagi, Takayoshi
- Abstract
Abstract: Sulfolobus tokodaii, a thermoacidophilic archaeon, possesses two structurally and functionally different enzymes that catalyze the oxidation of glyceraldehyde-3-phosphate (GAP): non-phosphorylating GAP dehydrogenase (St-GAPN) and phosphorylating GAP dehydrogenase (St-GAPDH). In contrast to previously characterized GAPN from Sulfolobus solfataricus, which exhibits V-type allosterism, St-GAPN showed K-type allosterism in which the positive cooperativity was abolished with concomitant activation by glucose 1-phosphate (G1P). St-GAPDH catalyzed the reversible oxidation of GAP to 1,3-bisphosphoglycerate (1,3-BPG) with high gluconeogenic activity, which was specific for NADPH, while both NAD+ and NADP+ were utilized in the glycolytic direction. Structured summary of protein interactions: GAPDH and GAPDH bind by molecular sieving (View interaction) GAPN and GAPN bind by 2.2molecular sieving (View interaction).
- Subjects
GLYCERALDEHYDEPHOSPHATE dehydrogenase; COMPARATIVE studies; SULFOLOBUS; ACIDOPHILIC bacteria; ALLOSTERIC regulation; OXIDATION
- Publication
FEBS Letters, 2012, Vol 586, Issue 19, p3097
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.07.059