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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.
Adenosine triphosphate (ATP) is a nucleoside triphosphate [2] that provides energy to drive and support many processes in living cells, such as muscle contraction, nerve impulse propagation, and chemical synthesis. Found in all known forms of life, it is often referred to as the "molecular unit of currency" for intracellular energy transfer. [3]
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.
Oxidative phosphorylation (UK / ɒ k ˈ s ɪ d. ə. t ɪ v /, US / ˈ ɑː k. s ɪ ˌ d eɪ. t ɪ v / [1]) or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP).
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.
In the field of enzymology, a proton ATPase, or H +-ATPase, is an enzyme that catalyzes the following chemical reaction: ATP + H 2 O + H + in ADP + phosphate + H + out. The 3 substrates of this enzyme are ATP, H 2 O, and H +, whereas its 3 products are ADP, phosphate, and H +.
Subunit C (also called subunit 9, or proteolipid in F-ATPases, or the 16 kDa proteolipid in V-ATPases) was found in the Fo or Vo complex of F- and V-ATPases, respectively. The subunits form an oligomeric c ring that make up the Fo/Vo/Ao rotor, where the actual number of subunits vary greatly among specific enzymes.