Аденозин трифосфаты: Жас клеткалардың энергия көзі

Energy carrying molecule in living cells
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| Watchedfields = changed
| verifiedrevid = 477228486
| Name = Adenosine 5' triphosphate
| ImageFile = Adenosintriphosphat protoniert. svg
| ImageSize = 280px
| ImageFileL1 = ATP xtal 3D balls. png
| ImageFileR1 = ATP xtal 3D vdW. png
| OtherNames =
| IUPACName = Adenosine 5′ (tetrahydrogen triphosphate)
| SystematicName = O1 {[(2R,3S,4R,5R) 5 (6 Amino 9H purin 9 yl) 3,4 dihydroxyoxolan 2 yl]methyl} tetrahydrogen triphosphate
| Section1 =
| Section2 = Chembox Properties
| C=10|H=16|N=5|O=13|P=3
| MolarMass = 507.18 g/mol
| MeltingPtC = 187
| MeltingPt notes = disodium salt; decomposes
| Density = 1.04 g/cm3 (disodium salt)
| pKa = 0.9, 1.4, 3.8, 6.5
| LambdaMax = 259 nm
| Absorbance = ε259 = 15.4 mM−1 cm−1 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" of intracellular energy transfer. When consumed in a metabolic processes, 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 human adult processes around 50 kilograms daily. From the perspective of biochemistry, ATP is classified as a nucleoside triphosphate, which indicates that it consists of three components: a nitrogenous base (adenine), the sugar ribose, and the triphosphate.

ATP consists of an adenine attached by the #9 nitrogen atom to the 1′ carbon atom of a sugar (ribose), which in turn is attached at the 5' carbon atom of the sugar to a triphosphate group. In its many reactions related to metabolism, the adenine and sugar groups remain unchanged, but the triphosphate is converted to di and monophosphate, giving respectively the derivatives ADP and AMP. The three phosphoryl groups are labeled as alpha (α), beta (β), and, for the terminal phosphate, gamma (γ). In neutral solution, ionized ATP exists mostly as ATP4−, with a small proportion of ATP3−.

Polyanionic and featuring a potentially chelating polyphosphate group, ATP binds metal cations with high affinity. The binding constant for link=magnesiumMg2+ is The binding of a divalent cation, almost always magnesium, strongly affects the interaction of ATP with various proteins. Due to the strength of the ATP Mg2+ interaction, ATP exists in the cell mostly as a complex with bonded to the phosphate oxygen centers. A second magnesium ion is critical for ATP binding in the kinase domain. The presence of Mg2+ regulates kinase activity. It is interesting from an RNA world perspective that ATP can carry a Mg ion which catalyzes RNA polymerization.

Salts of ATP can be isolated as colorless solids. ATP is stable in aqueous solutions between pH 6.8 and 7.4 (in the absence of catalysts). At more extreme pH levels, it rapidly hydrolyses to ADP and phosphate. Living cells maintain the ratio of ATP to ADP at a point ten orders of magnitude from equilibrium, with ATP concentrations fivefold higher than the concentration of ADP. In the context of biochemical reactions, the P O P bonds are frequently referred to as high energy bonds.

A typical intracellular concentration of ATP may be 1–10 μmol per gram of tissue in a variety of eukaryotes. The dephosphorylation of ATP and rephosphorylation of ADP and AMP occur repeatedly in the course of aerobic metabolism. ATP can be produced by a number of distinct cellular processes; the three main pathways in eukaryotes are (1) glycolysis, (2) the citric acid cycle/oxidative phosphorylation, and (3) beta oxidation. 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. ATP production by a non photosynthetic aerobic eukaryote occurs mainly in the mitochondria, which comprise nearly 25% of the volume of a typical cell.

In glycolysis, glucose and glycerol are metabolized to pyruvate. Glycolysis generates two equivalents of ATP through substrate phosphorylation catalyzed by two enzymes, phosphoglycerate kinase (PGK) and pyruvate kinase. Two equivalents of nicotinamide adenine dinucleotide (NADH) are also produced, which can be oxidized via the electron transport chain and result in the generation of additional ATP by ATP synthase. The pyruvate generated as an end product of glycolysis is a substrate for the Krebs Cycle. Glycolysis is viewed as consisting of two phases with five steps each. In phase 1, "the preparatory phase", glucose is converted to 2 d glyceraldehyde 3 phosphate (g3p). One ATP is invested in Step 1, and another ATP is invested in Step 3. Steps 1 and 3 of glycolysis are referred to as "Priming Steps". In Phase 2, two equivalents of g3p are converted to two pyruvates. In Step 7, two ATP are produced. Also, in Step 10, two further equivalents of ATP are produced. In Steps 7 and 10, ATP is generated from ADP. A net of two ATPs is formed in the glycolysis cycle. The glycolysis pathway is later associated with the Citric Acid Cycle which produces additional equivalents of ATP.

In glycolysis, hexokinase is directly inhibited by its product, glucose 6 phosphate, and pyruvate kinase is inhibited by ATP itself. The main control point for the glycolytic pathway is phosphofructokinase (PFK), which is allosterically inhibited by high concentrations of ATP and activated by high concentrations of AMP. The inhibition of PFK by ATP is unusual since ATP is also a substrate in the reaction catalyzed by PFK; the active form of the enzyme is a tetramer that exists in two conformations, only one of which binds the second substrate fructose 6 phosphate (F6P). The protein has two binding sites for ATP – the active site is accessible in either protein conformation, but ATP binding to the inhibitor site stabilizes the conformation that binds F6P poorly. Three ATP are produced per turn. Although oxygen consumption appears fundamental for the maintenance of the proton motive force, in the event of oxygen shortage (hypoxia), intracellular acidosis (mediated by enhanced glycolytic rates and ATP hydrolysis), contributes to mitochondrial membrane potential and directly drives ATP synthesis. Most of the ATP synthesized in the mitochondria will be used for cellular processes in the cytosol; thus it must be exported from its site of synthesis in the mitochondrial matrix. ATP outward movement is favored by the membrane's electrochemical potential because the cytosol has a relatively positive charge compared to the relatively negative matrix. For every ATP transported out, it costs 1 H+. Producing one ATP costs about 3 H+. Therefore, making and exporting one ATP requires 4H+. The inner membrane contains an antiporter, the ADP/ATP translocase, which is an integral membrane protein used to exchange newly synthesized ATP in the matrix for ADP in the intermembrane space.

The citric acid cycle is regulated mainly by the availability of key substrates, particularly the ratio of NAD+ to NADH and the concentrations of calcium, inorganic phosphate, ATP, ADP, and AMP. Citrate – the ion that gives its name to the cycle – is a feedback inhibitor of citrate synthase and also inhibits PFK, providing a direct link between the regulation of the citric acid cycle and glycolysis.

ATP can also be synthesized through several so called "replenishment" reactions catalyzed by the enzyme families of nucleoside diphosphate kinases (NDKs), which use other nucleoside triphosphates as a high energy phosphate donor, and the ATP:guanido phosphotransferase family.

In plants, ATP is synthesized in the thylakoid membrane of the chloroplast. The process is called photophosphorylation. The "machinery" is similar to that in mitochondria except that light energy is used to pump protons across a membrane to produce a proton motive force. ATP synthase then ensues exactly as in oxidative phosphorylation. Some of the ATP produced in the chloroplasts is consumed in the Calvin cycle, which produces triose sugars.

The total quantity of ATP in the human body is about 0.1 mol/L. The majority of ATP is recycled from ADP by the aforementioned processes. Thus, at any given time, the total amount of ATP + ADP remains fairly constant. The energy used by human cells in an adult requires the hydrolysis of 100 to 150 mol/L of ATP daily, which means a human will typically use their body weight worth of ATP over the course of the day. Each equivalent of ATP is recycled 1000–1500 times during a single day , Phosphorylation of a protein by a kinase can activate a cascade such as the mitogen activated protein kinase cascade. ATP is also a substrate of adenylate cyclase, most commonly in G protein coupled receptor signal transduction pathways and is transformed to second messenger, cyclic AMP, which is involved in triggering calcium signals by the release of calcium from intracellular stores. This form of signal transduction is particularly important in brain function, although it is involved in the regulation of a multitude of other cellular processes.

ATP is one of four monomers required in the synthesis of RNA. The process is promoted by RNA polymerases. A similar process occurs in the formation of DNA, except that ATP is first converted to the deoxyribonucleotide dATP. Like many condensation reactions in nature, DNA replication and DNA transcription also consume ATP.

Transporting chemicals out of a cell against a gradient is often associated with ATP hydrolysis. Transport is mediated by ATP binding cassette transporters. The human genome encodes 48 ABC transporters, that are used for exporting drugs, lipids, and other compounds.

Cells secrete ATP to communicate with other cells in a process called purinergic signalling. ATP serves as a neurotransmitter in many parts of the nervous system, modulates ciliary beating, affects vascular oxygen supply etc. ATP is either secreted directly across the cell membrane through channel proteins or is pumped into vesicles which then fuse with the membrane. Cells detect ATP using the purinergic receptor proteins P2X and P2Y.

ATP fuels muscle contractions. Muscle contractions are regulated by signaling pathways, although different muscle types being regulated by specific pathways and stimuli based on their particular function. However, in all muscle types, contraction is performed by the proteins actin and myosin. ATP is initially bound to myosin. When ATPase hydrolyzes the bound ATP into ADP and inorganic phosphate, myosin is positioned in a way that it can bind to actin. Myosin bound by ADP and Pi forms cross bridges with actin and the subsequent release of ADP and Pi releases energy as the power stroke. The power stroke causes actin filament to slide past the myosin filament, shortening the muscle and causing a contraction. Another ATP molecule can then bind to myosin, releasing it from actin and allowing this process to repeat.

ATP has recently been proposed to act as a biological hydrotrope and has been shown to affect proteome wide solubility.

Acetyl phosphate (AcP), a precursor to ATP, can readily be synthesized at modest yields from thioacetate in pH 7 and 20 °C and pH 8 and 50 °C, although acetyl phosphate is less stable in warmer temperatures and alkaline conditions than in cooler and acidic to neutral conditions. It is unable to promote polymerization of ribonucleotides and amino acids and was only capable of phosphorylation of organic compounds. It was shown that it can promote aggregation and stabilization of AMP in the presence of Na+, aggregation of nucleotides could promote polymerization above 75 °C in the absence of Na+. It is possible that polymerization promoted by AcP could occur at mineral surfaces. It was shown that ADP can only be phosphorylated to ATP by AcP and other nucleoside triphosphates were not phosphorylated by AcP. This might explain why all lifeforms use ATP to drive biochemical reactions.

Biochemistry laboratories often use in vitro studies to explore ATP dependent molecular processes. ATP analogs are also used in X ray crystallography to determine a protein structure in complex with ATP, often together with other substrates. Enzyme inhibitors of ATP dependent enzymes such as kinases are needed to examine the binding sites and transition states involved in ATP dependent reactions. Most useful ATP analogs cannot be hydrolyzed as ATP would be; instead, they trap the enzyme in a structure closely related to the ATP bound state. Adenosine 5′ (γ thiotriphosphate) is an extremely common ATP analog in which one of the gamma phosphate oxygens is replaced by a sulfur atom; this anion is hydrolyzed at a dramatically slower rate than ATP itself and functions as an inhibitor of ATP dependent processes. In crystallographic studies, hydrolysis transition states are modeled by the bound vanadate ion. Caution is warranted in interpreting the results of experiments using ATP analogs, since some enzymes can hydrolyze them at appreciable rates at high concentration.

ATP is used intravenously for some heart related conditions.

ATP was discovered in 1929 by Karl Lohmann and Jendrassik and, independently, by Cyrus Fiske and Yellapragada Subba Rao of Harvard Medical School, both teams competing against each other to find an assay for phosphorus. It was proposed to be the intermediary between energy yielding and energy requiring reactions in cells by Fritz Albert Lipmann in 1941. It was first synthesized in the laboratory by Alexander Todd in 1948, and he was awarded the Nobel Prize in Chemistry in 1957 partly for this work. The 1978 Nobel Prize in Chemistry was awarded to Peter Dennis Mitchell for the discovery of the chemiosmotic mechanism of ATP synthesis. The 1997 Nobel Prize in Chemistry was divided, one half jointly to Paul D. Boyer and John E. Walker "for their elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP)" and the other half to Jens C. Skou "for the first discovery of an ion transporting enzyme, Na+, K+ ATPase."