Substrate Phosphorylation

Substrate Phosphorylation

 

in biochemistry, the synthesis of energy-rich phosphorus compounds using the energy of the oxidation-reduction reactions of glycolysis, which are catalyzed by phosphoglyceraldehyde dehydrogenase and enolase. It also takes place upon oxidation of α-ketoglutaric acid in the Krebs cycle (under the action of a-ketoglutarate dehydrogenase and succinate thiokinase). For bacteria, cases of substrate phosphorylation upon oxidation of pyruvic acid have been described.

Substrate phosphorylation, in contrast to phosphorylation in an electron transport system (seeOXIDATIVE PHOSPHORYLATION), is not inhibited by general poisons, such as dinitrophenol, and is not related to the fixation of enzymes in mitochondrial membranes. The contribution of substrate phosphorylation to the cellular supply of adenosine triphosphate under aerobic conditions is significantly less than the contribution of phosphorylation in an electron transport system.

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In order to elucidate the ostensibly contradictory findings of MEK1 /2 hyperphosphorylation and decrease in substrate phosphorylation, the influence of 7-epi-nemorosone on the kinase activity of MEK1 /2 was studied in a cell-free system.
Therefore, similar allosteric regulation of substrate phosphorylation may have a more general meaning and play a significant role in various 'decision-making' steps of the cell cycle.
Cellular substrate phosphorylation studies targeting the inhibition of PI3K and functional cellular assays of tumor cell proliferation have been performed.
Insulin-receptor autophosphorylation and endogenous substrate phosphorylation in human adipocytes from control, obese, and NIDDM subjects.