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Hydrolysis of the phosphate groups in ATP is especially exergonic, because the resulting inorganic phosphate molecular ion is greatly stabilized by multiple resonance structures, making the products (ADP and P i) lower in energy than the reactant (ATP). The high negative charge density associated with the three adjacent phosphate units of ATP ...
In biochemistry, dephosphorylation is the removal of a phosphate (PO 3− 4) group from an organic compound by hydrolysis. It is a reversible post-translational modification. Dephosphorylation and its counterpart, phosphorylation, activate and deactivate enzymes by detaching or attaching phosphoric esters and anhydrides.
Phosphatases catalyze the hydrolysis of a phosphomonoester, removing a phosphate moiety from the substrate. Water is split in the reaction, with the -OH group attaching to the phosphate ion, and the H+ protonating the hydroxyl group of the other product. The net result of the reaction is the destruction of a phosphomonoester and the creation of ...
Since orthophosphoric acid has three −OH groups, it can esterify with one, two, or three alcohol molecules to form a mono-, di-, or triester. See the general structure image of an ortho- (or mono-) phosphate ester below on the left, where any of the R groups can be a hydrogen or an organic radical. Di- and tripoly- (or tri-) phosphate esters ...
The hydrolysis of ATP into ADP and inorganic phosphate ATP 4-(aq) + H 2 O (l) = ADP 3-(aq) + HPO 2-(aq) + H + (aq) releases 20.5 kilojoules per mole (4.9 kcal/mol) of enthalpy. This may differ under physiological conditions if the reactant and products are not exactly in these ionization states. [15]
In chemistry, a phosphate is an anion, salt, functional group or ester derived from a phosphoric acid. It most commonly means orthophosphate, a derivative of orthophosphoric acid, a.k.a. phosphoric acid H 3 PO 4. The phosphate or orthophosphate ion [PO 4] 3− is derived from phosphoric acid by the removal of three protons H +.
A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (), with up to 30% of all proteins being phosphorylated at any given time.
Glucose-6-phosphate Glucose. The enzyme glucose 6-phosphatase (EC 3.1.3.9, G6Pase; systematic name D-glucose-6-phosphate phosphohydrolase) catalyzes the hydrolysis of glucose 6-phosphate, resulting in the creation of a phosphate group and free glucose: