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The overall process of oxidizing glucose to carbon dioxide, the combination of pathways 1 and 2, known as cellular respiration, produces about 30 equivalents of ATP from each molecule of glucose. [20] ATP production by a non-photosynthetic aerobic eukaryote occurs mainly in the mitochondria, which comprise nearly 25% of the volume of a typical ...
The alpha/A and beta/B subunits can each be divided into three regions, or domains, centred on the ATP-binding pocket, and based on structure and function. The central domain contains the nucleotide-binding residues that make direct contact with the ADP/ATP molecule. [8]
Molecular structure of adenosine triphosphate (ATP) An ATP-binding motif is a 250-residue sequence within an ATP-binding protein’s primary structure. The binding motif is associated with a protein’s structure and/or function. [1] ATP is a molecule of energy, and can be a coenzyme, involved in a number of biological reactions.
The molecular formula C 10 H 16 N 5 O 13 P 3 ... Adenosine triphosphate (ATP) Deoxyguanosine triphosphate (dGTP) This page was last edited on 28 August 2022, at 16: ...
The chemical energy stored in ATP (the bond of its third phosphate group to the rest of the molecule can be broken allowing more stable products to form, thereby releasing energy for use by the cell) can then be used to drive processes requiring energy, including biosynthesis, locomotion or transportation of molecules across cell membranes.
The P-loop main chain is shown in red, the Mg 2+ ion as green sphere and the side chains of the amino acids K16 and S17 are shown as sticks. Walker A motif , also known as the Walker loop , or P-loop , or phosphate-binding loop , is a motif in proteins that is associated with phosphate binding.
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The protein then closes up around the molecules and binds them loosely – the "loose" state (shown in red). The enzyme then changes shape again and forces these molecules together, with the active site in the resulting "tight" state (shown in pink) binding the newly produced ATP molecule with very high affinity. Finally, the active site cycles ...