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In the glycolytic pathway, 1,3-BPG is the phosphate donor and has a high phosphoryl-transfer potential. The PGK-catalyzed transfer of the phosphate group from 1,3-BPG to ADP to yield ATP can power [clarification needed] the carbon-oxidation reaction of the previous glycolytic step (converting glyceraldehyde 3-phosphate to 3-phosphoglycerate).
Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the "high-energy" exchange medium in the cell. During aerobic respiration, ATP is synthesized in the mitochondrion by addition of a third phosphate group to adenosine diphosphate (ADP) in a ...
In biochemistry, a kinase (/ ˈ k aɪ n eɪ s, ˈ k ɪ n eɪ s,-eɪ z /) [2] is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the high-energy ATP molecule donates a phosphate group to the substrate molecule.
The energy released by this highly exergonic oxidation reaction drives the endergonic second reaction (ΔG°'=+50 kJ/mol (+12kcal/mol)), in which a molecule of inorganic phosphate is transferred to the GAP intermediate to form a product with high phosphoryl-transfer potential: 1,3-bisphosphoglycerate (1,3-BPG).
[2] [3] "Phosphoryl" groups are covalently bonded by a single bond to an organic molecule, phosphate group(s) or another "phosphoryl" group(s), and those groups are sp 3 hybridized at the phosphorus atom. [4] The term "phosphoryl" in the mentioned branches is usually used in the description of catalytic mechanisms in living organisms.
The squiggle notation was invented by Fritz Albert Lipmann, who first proposed ATP as the main energy transfer molecule of the cell, in 1941. [4] Lipmann's notation emphasizes the special nature of these bonds. [5] Stryer states: ATP is often called a high energy compound and its phosphoanhydride bonds are referred to as high-energy bonds.
Phosphoryl transfer only occurs on closing of the 'open lid'. This causes an exclusion of water molecules that brings the substrates in proximity to each other, [ 7 ] lowering the energy barrier for the nucleophilic attack by the α-phosphoryl of AMP on the γ-phosphoryl group of ATP resulting in formation of ADP by transfer of the γ ...
Phosphoryl groups are transferred during PEPCK action, which is likely facilitated by the eclipsed conformation of the phosphoryl groups when ATP is bound to PEPCK. [ 11 ] Since the eclipsed formation is one that is high in energy, phosphoryl group transfer has a decreased energy of activation , meaning that the groups will transfer more readily.