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The values of the free energy released by cleaving either a phosphate (P i) or a pyrophosphate (PP i) unit from ATP at standard state concentrations of 1 mol/L at pH 7 are: [16] ATP + H 2 O → ADP + P i Δ G °' = −30.5 kJ/mol (−7.3 kcal/mol)
See Amino acid for the pK a values of all amino acid side chains inferred in such a way. There are also numerous experimental studies that have yielded such values, for example by use of NMR spectroscopy. The table below lists the model pK a values that are often used in a protein pK a calculation, and contains a third column based on protein ...
In cell biology, protein kinase A (PKA) is a family of serine-threonine kinase [1] whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (EC 2.7.11.11). PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism.
AMP can be produced from ADP by the myokinase (adenylate kinase) reaction when the ATP reservoir in the cell is low: [5] [6] 2 ADP → ATP + AMP. Or AMP may be produced by the hydrolysis of one high energy phosphate bond of ADP: ADP + H 2 O → AMP + P i. AMP can also be formed by hydrolysis of ATP into AMP and pyrophosphate: ATP + H 2 O → ...
At pH 1 or lower, the phosphoric acid is practically undissociated. Around pH 4.7 (mid-way between the first two pK a values) the dihydrogen phosphate ion, [H 2 PO 4] −, is practically the only species present. Around pH 9.8 (mid-way between the second and third pK a values) the monohydrogen phosphate ion, [HPO 4] 2−, is the only species ...
Structure of ATP Structure of ADP Four possible resonance structures for inorganic phosphate. ATP hydrolysis is the catabolic reaction process by which chemical energy that has been stored in the high-energy phosphoanhydride bonds in adenosine triphosphate (ATP) is released after splitting these bonds, for example in muscles, by producing work in the form of mechanical energy.
The G s alpha subunit, in turn, activates adenylyl cyclase, which quickly converts ATP into cAMP. This leads to the activation of the cAMP-dependent pathway. This pathway can also be activated downstream by directly activating adenylyl cyclase or PKA. Molecules that activate cAMP pathway include: cholera toxin - increases cAMP levels
TNP-ATP is a fluorescent molecule that is able to determine whether a protein binds to ATP, and the constants associated with that binding.It is primarily used in fluorescence spectroscopy, but is also very useful as an acceptor molecule in FRET, and as a fluorescent probe in fluorescence microscopy and X-ray crystallography.