On the Action of Pyrophosphate on 3-phospho- Glyceraldehyde
نویسنده
چکیده
When pyrophosphate has been found to influence an enzymatic reaction, its action is usually indirect, that is as a chelator of free essential metal ions rather than directly on the protein catalyst. However, it appears that the latter situation holds for the action of pyrophosphate in the modification of reduced diphosphopyridine nucleotide’ to the product obtained by the action of 3-phosphoglyceraldehyde dehydrogenase on DPNH (DPNHX) catalyzed by 3-phosphoglyceraldehyde dehydrogenase (1) . The inhibition of succinic dehydrogenase by pyrophosphate (2) appears to be another example of the ion acting on the protein catalyst. The present paper reports on sev\eral additional effects of pyrophosphate on various reactions involving 3-phosphoglyceraldehyde dehydrogenase. Certain of the results suggest that pyrophosphate has an affinity for the phosphatase site of the protein (3).
منابع مشابه
Is nicotinamide adenine dinucleotide phosphate an obligatory intermediate in photosynthesis?
The site of action of the inhibitors disalicylidenepropanediamine and pyrophosphate was more closely defined as acting on ferredoxin. Three inhibitors which act on the electron transport path between ferredoxin and NADP: disalicylidenepropanediamine, pyrophosphate, and phosphoadenosinediphosphate ribose, had no effect on photosynthesis in cell free preparations of Dunaliela parva at concentrati...
متن کاملOn the action of pyrophosphate on 3-phosphoglyceraldehyde dehydrogenase.
When pyrophosphate has been found to influence an enzymatic reaction, its action is usually indirect, that is as a chelator of free essential metal ions rather than directly on the protein catalyst. However, it appears that the latter situation holds for the action of pyrophosphate in the modification of reduced diphosphopyridine nucleotide’ to the product obtained by the action of 3-phosphogly...
متن کاملPhosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins.
Glyceraldehyde-3-phosphate dehydrogenases catalyze key steps in energy and reducing power partitioning in cells of higher plants. Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) present in heterotrophic cells of wheat (Triticum aestivum) was activated up to 3-fold by MgCl2. The effect was not observed with the non-phosphorylated enzyme found in leaves. The div...
متن کاملNAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties.
The hyperthermophilic archaeum Thermoproteus tenax possesses two glyceraldehyde-3-phosphate dehydrogenases differing in cosubstrate specificity and phosphate dependence of the catalyzed reaction. NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase catalyzes the phosphate-independent irreversible oxidation of D-glyceraldehyde 3-phosphate to 3-phosphoglycerate. The coding gene was cloned, seq...
متن کاملNew therapeutic targets for drug design against Trypanosoma cruzi, advances and perspectives.
Chagas disease is one of the most important parasitic diseases in Latin America, affecting 16 to 18 million people. Nifurtimox and Benznidazol are drugs that are commonly used in its treatment; however, these drugs produce several adverse reactions and are not effective in the chronic phase of the disease. Therefore, the design, synthesis, and biological evaluation of new compounds with potenti...
متن کامل