Adenosine diphosphate in the context of "ATP synthase"

Adenosine triphosphate (ATP) is a nucleoside triphosphate that provides energy of approximate 30.5kJ/mol 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.

When consumed in a metabolic process, ATP converts either to adenosine diphosphate (ADP) or to adenosine monophosphate (AMP). Other processes regenerate ATP. It is also a precursor to DNA and RNA, and is used as a coenzyme. An average adult human processes around 50 kilograms (about 100 moles) daily.

A hydrogenosome is a membrane-enclosed organelle found in some anaerobic ciliates, flagellates, fungi, and three species of loriciferans. Hydrogenosomes are highly variable organelles that have presumably evolved from protomitochondria to produce molecular hydrogen and ATP in anaerobic conditions.

Hydrogenosomes were discovered in 1973 by D. G. Lindmark and M. Müller. Because hydrogenosomes hold evolutionary lineage significance for organisms living in anaerobic or oxygen-stressed environments, many research institutions have since documented their findings on how the organelle differs in various sources.

An oxyanion, or oxoanion, is an ion with the generic formula A
_xO
_y (where A represents a chemical element and O represents an oxygen atom). Oxyanions are formed by a large majority of the chemical elements. The corresponding oxyacid of an oxyanion is the compound H
_zA
_xO
_y. The structures of condensed oxyanions can be rationalized in terms of AO_n polyhedral units with sharing of corners or edges between polyhedra. The oxyanions (specifically, phosphate and polyphosphate esters) adenosine monophosphate (AMP), adenosine diphosphate (ADP) and adenosine triphosphate (ATP) are important in biology.

Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that catalyzes the condensation of glutamate and ammonia to form glutamine:Glutamate + ATP + NH₃ → Glutamine + ADP + phosphate

Glutamine synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites.

In the process of photosynthesis, the phosphorylation of ADP to form ATP using the energy of sunlight is called photophosphorylation. Cyclic photophosphorylation occurs in both aerobic and anaerobic conditions, driven by the main source of energy available to living organisms, which is sunlight. All organisms produce ATP, which is the universal energy currency of life. In photophosphorylation, light energy is used to pump protons across a biological membrane, mediated by flow of electrons through an electron transport chain. This stores energy in a proton gradient. As the protons flow back through an enzyme called ATP synthase, ATP is generated from ADP and inorganic phosphate. ATP is essential in the Calvin cycle to assist in the synthesis of carbohydrates from carbon dioxide and NADPH.

The scientist Charles Barnes first used the word 'photosynthesis' in 1893. This word is taken from two Greek words, photos, which means light, and synthesis, which in chemistry means making a substance by combining simpler substances. So, in the presence of light, synthesis of food is called 'photosynthesis'.

In biochemistry, dephosphorylation is the removal of a phosphate (PO3−4) 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. A notable occurrence of dephosphorylation is the conversion of ATP to ADP and inorganic phosphate.

Dephosphorylation employs a type of hydrolytic enzyme, or hydrolase, which cleaves ester bonds. The prominent hydrolase subclass used in dephosphorylation is phosphatase, which removes phosphate groups by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl (–OH) group.

In biochemistry, a kinase (/ˈkaɪneɪs, ˈkɪneɪs, -eɪz/) 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. As a result, kinase produces a phosphorylated substrate and ADP. Conversely, it is referred to as dephosphorylation when the phosphorylated substrate donates a phosphate group and ADP gains a phosphate group (producing a dephosphorylated substrate and the high energy molecule of ATP). These two processes, phosphorylation and dephosphorylation, occur four times during glycolysis.

Kinases are part of the larger family of phosphotransferases. Kinases should not be confused with phosphorylases, which catalyze the addition of inorganic phosphate groups to an acceptor, nor with phosphatases, which remove phosphate groups (dephosphorylation). The phosphorylation state of a molecule, whether it be a protein, lipid or carbohydrate, can affect its activity, reactivity and its ability to bind other molecules. Therefore, kinases are critical in metabolism, cell signalling, protein regulation, cellular transport, secretory processes and many other cellular pathways, which makes them very important to physiology.