# Adenosine triphosphate

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Energy-carrying molecule in living cells

Adenosine triphosphate Names IUPAC name Adenosine 5′-(tetrahydrogen triphosphate) Systematic IUPAC name O1-{[(2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl} tetrahydrogen triphosphate Identifiers CAS Number 56-65-5 (free acid) Y 34369-07-8 (disodium salt hydrate) N 3D model (JSmol) Interactive image Interactive image ChEBI CHEBI:15422 Y ChEMBL ChEMBL14249 Y ChemSpider 5742 Y DrugBank DB00171 Y ECHA InfoCard 100.000.258 IUPHAR/BPS 1713 KEGG C00002 Y PubChem CID 5957 UNII 8L70Q75FXE Y CompTox Dashboard (EPA) DTXSID6022559 InChI InChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1 Y Key: ZKHQWZAMYRWXGA-KQYNXXCUSA-N Y Key: ZKHQWZAMYRWXGA-KQYNXXCUBG SMILES O=P(O)(O)OP(=O)(O)OP(=O)(O)OC[C@H]3O[C@@H](n2cnc1c(ncnc12)N)[C@H](O)[C@@H]3O c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N Properties Chemical formula C10H16N5O13P3 Molar mass 507.18 g/mol Density 1.04 g/cm3 (disodium salt) Melting point 187 °C (369 °F; 460 K) disodium salt; decomposes Acidity (pKa) 0.9, 1.4, 3.8, 6.5 UV-vis (λmax) 259 nm[1] Absorbance ε259 = 15.4 mM−1 cm−1[1] Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Y verify (what is YN ?) Infobox references

Chemical compound

Interactive animation of the structure of ATP

**Adenosine triphosphate** (**ATP**) is a [nucleoside triphosphate](/source/Nucleoside_triphosphate)[2] that provides [free energy](/source/Gibbs_free_energy) of approximately 58 [kJ](/source/Joule#kilojoule)/[mol](/source/Mole_(unit)) (0.6 [eV](/source/Electronvolt))[3] to drive and support many processes in living [cells](/source/Cell_(biology)), such as [muscle contraction](/source/Muscle_contraction), [nerve impulse](/source/Nerve_impulse) propagation, and [chemical synthesis](/source/Chemical_synthesis). Found in all known forms of [life](/source/Life), it is often referred to as the "molecular unit of [currency](/source/Currency)" for intracellular [energy transfer](/source/Energy_transfer).[4]

When consumed in a [metabolic](/source/Metabolism) process, ATP converts either to [adenosine diphosphate](/source/Adenosine_diphosphate) (ADP) or to [adenosine monophosphate](/source/Adenosine_monophosphate) (AMP). Other processes, such as [oxidative phosphorylation](/source/Oxidative_phosphorylation) or [substrate-level phosphorylation](/source/Substrate-level_phosphorylation), regenerate ATP. ATP is also a [precursor](/source/Precursor_(chemistry)) to [DNA](/source/DNA) and [RNA](/source/RNA), and is used as a [coenzyme](/source/Coenzyme). Daily, an average adult human recycles through synthesis and hydrolysis around 50 kilograms of ATP (about 100 [moles](/source/Mole_(unit))).[5]

From the perspective of [biochemistry](/source/Biochemistry), ATP is classified as a [nucleoside triphosphate](/source/Nucleoside_triphosphate), which indicates that it consists of three components: a nitrogenous base ([adenine](/source/Adenine)), the sugar [ribose](/source/Ribose), and the [triphosphate](/source/Polyphosphate).

## Structure

ATP consists of three parts: a sugar, an amine base, and a phosphate group.[6] More specifically, ATP consists of an [adenine](/source/Adenine) attached by the #9-nitrogen atom to the 1′ [carbon](/source/Carbon) [atom](/source/Atom) of a sugar ([ribose](/source/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](/source/Adenosine_diphosphate) and [AMP](/source/Adenosine_monophosphate). The three phosphoryl groups are labeled as alpha (α), beta (β), and, for the terminal phosphate, gamma (γ).[7]

In neutral solution, ionized ATP exists mostly as ATP4−, with a small proportion of ATP3−.[8]

### Metal cation binding

Polyanionic and featuring a potentially [chelating](/source/Chelation) polyphosphate group, ATP binds metal cations with high affinity. The [binding constant](/source/Binding_constant) for [Mg](/source/Magnesium)2+ is (9554).[9] The binding of a [divalent](/source/Divalent) [cation](/source/Cation), almost always [magnesium](/source/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 Mg2+ bonded to the phosphate [oxygen](/source/Oxygen) centers.[8][10]

A second magnesium ion is critical for ATP binding in the kinase domain.[11] The presence of Mg2+ regulates kinase activity.[12] It is interesting from an RNA world perspective that ATP can carry a Mg ion which catalyzes RNA polymerization.[*[citation needed](https://en.wikipedia.org/wiki/Wikipedia:Citation_needed)*]

## Chemical properties

Salts of ATP can be isolated as colorless solids.[13]

The cycles of synthesis and degradation of ATP; 2 and 1 represent input and output of energy, respectively.

ATP is stable in aqueous solutions between [pH](/source/PH) 6.8 and 7.4 (in the absence of catalysts). At more extreme pH levels, it rapidly [hydrolyses](/source/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.[14][15] In the context of biochemical reactions, the P-O-P bonds are frequently referred to as [*high-energy bonds*](/source/High-energy_phosphate).[16]

## Reactive aspects

The hydrolysis of ATP into ADP and inorganic phosphate:

- ATP4− + H2O ⇌ ADP3− + HPO2−3 + H+

releases Δ*G*°' = −30.5 kJ/mol (−7.3 kcal/mol) of Gibbs free energy under standard conditions when all metabolite concentrations are 1 mol/L. This may differ under physiological conditions if the reactant and products are not exactly in these ionization states.[17] The values of the free energy released by cleaving either a phosphate (Pi) or a pyrophosphate (PPi) unit from ATP at [standard state](/source/Standard_state) concentrations of 1 mol/L at pH 7 are:[18]

- ATP + H2O → ADP + Pi Δ*G*°' = −30.5 kJ/mol (−7.3 kcal/mol)

- ATP + H2O → AMP + PPi Δ*G*°' = −45.6 kJ/mol (−10.9 kcal/mol)

These abbreviated equations at a pH near 7 can be written more explicitly (R = [adenosyl](/source/Adenosine)):

- [RO−P(O)2−O−P(O)2−O−PO3]4− + H2O → [RO−P(O)2−O−PO3]3− + [HPO4]2− + H+

- [RO−P(O)2−O−P(O)2−O−PO3]4− + H2O → [RO−PO3]2− + [HO3P−O−PO3]3− + H+

For ATP hydrolysis that takes place with the physiological concentrations of ATP, ADP, and inorganic phosphate (Pi) within the living cell, the change in Gibbs free energy is given by:[19]

- Δ G = Δ G 0 ′ + R T ln ⁡ ( [ A D P ] [ P i ] [ A T P ] ) {\displaystyle \Delta G=\Delta G^{0'}+RT\ln \left({\frac {[ADP][Pi]}{[ATP]}}\right)}

At cytoplasmic conditions, where the ADP/ATP ratio is 10 orders of magnitude from equilibrium, the Δ*G* is around −57 kJ/mol.[14]

Along with pH, the free energy change of ATP hydrolysis is also associated with Mg2+ concentration, from ΔG°' = −35.7 kJ/mol at a Mg2+ concentration of zero, to ΔG°' = −31 kJ/mol at [Mg2+] = 5 mM. Higher concentrations of Mg2+ decrease free energy released in the reaction due to binding of Mg2+ ions to negatively charged oxygen atoms of ATP at pH 7.[20]

This image shows a 360-degree rotation of a single, gas-phase [magnesium](/source/Magnesium)-ATP chelate with a charge of −2. The anion was optimized at the UB3LYP/6-311++G(d,p) theoretical level and the atomic connectivity modified by the human optimizer to reflect the probable electronic structure.

## Production from AMP and ADP

### Production, aerobic conditions

A typical intracellular [concentration](/source/Concentration) of ATP is 1–10 μmol per gram of muscle tissue in a variety of eukaryotes.[21] The [dephosphorylation](/source/Dephosphorylation) of ATP and rephosphorylation of ADP and AMP occur repeatedly in the course of aerobic metabolism.[22]

ATP can be produced by a number of distinct cellular processes; the three main pathways in [eukaryotes](/source/Eukaryote) are (1) [glycolysis](/source/Glycolysis), (2) the [citric acid cycle](/source/Citric_acid_cycle)/[oxidative phosphorylation](/source/Oxidative_phosphorylation), and (3) [beta-oxidation](/source/Beta-oxidation). The overall process of oxidizing [glucose](/source/Glucose) to [carbon dioxide](/source/Carbon_dioxide), the combination of pathways 1 and 2, known as [cellular respiration](/source/Cellular_respiration), produces about 30 equivalents of ATP from each molecule of glucose.[23]

ATP production by a non-[photosynthetic](/source/Photosynthetic) aerobic eukaryote occurs mainly in the [mitochondria](/source/Mitochondria), which comprise nearly 25% of the volume of a typical cell.[24]

#### Glycolysis

Main article: [Glycolysis](/source/Glycolysis)

In glycolysis, glucose and glycerol are metabolized to [pyruvate](/source/Pyruvate). Glycolysis generates two equivalents of ATP through [substrate phosphorylation](/source/Substrate-level_phosphorylation) catalyzed by two enzymes, [phosphoglycerate kinase](/source/Phosphoglycerate_kinase) (PGK) and [pyruvate kinase](/source/Pyruvate_kinase). Two equivalents of [nicotinamide adenine dinucleotide](/source/Nicotinamide_adenine_dinucleotide) (NADH) are also produced, which can be oxidized via the [electron transport chain](/source/Electron_transport_chain) and result in the generation of additional ATP by [ATP synthase](/source/ATP_synthase). The pyruvate generated as an end-product of glycolysis is a substrate for the [Krebs Cycle](/source/Citric_acid_cycle).[25]

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.[26]

#### Regulation

In glycolysis, [hexokinase](/source/Hexokinase) is directly inhibited by its product, glucose-6-phosphate, and [pyruvate kinase](/source/Pyruvate_kinase) is inhibited by ATP itself. The main control point for the glycolytic pathway is [phosphofructokinase](/source/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](/source/Tetramer_protein) that exists in two conformations, only one of which binds the second substrate fructose-6-phosphate (F6P). The protein has two [binding sites](/source/Binding_site) for ATP – the [active site](/source/Active_site) is accessible in either protein conformation, but ATP binding to the inhibitor site stabilizes the conformation that binds F6P poorly.[25] A number of other small molecules can compensate for the ATP-induced shift in equilibrium conformation and reactivate PFK, including [cyclic AMP](/source/Cyclic_AMP), [ammonium](/source/Ammonium) ions, inorganic phosphate, and fructose-1,6- and -2,6-biphosphate.[25]

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#### Citric acid cycle

Main articles: [Citric acid cycle](/source/Citric_acid_cycle) and [Oxidative phosphorylation](/source/Oxidative_phosphorylation)

In the [mitochondrion](/source/Mitochondrion), pyruvate is oxidized by the [pyruvate dehydrogenase complex](/source/Pyruvate_dehydrogenase_complex) to the [acetyl](/source/Acetyl) group, which is fully oxidized to carbon dioxide by the [citric acid cycle](/source/Citric_acid_cycle) (also known as the [Krebs](/source/Hans_Krebs_(biochemist)) cycle). Every "turn" of the citric acid cycle produces two molecules of carbon dioxide, one equivalent of ATP [guanosine triphosphate](/source/Guanosine_triphosphate) (GTP) through [substrate-level phosphorylation](/source/Substrate-level_phosphorylation) catalyzed by [succinyl-CoA synthetase](/source/Succinyl-CoA_synthetase), as succinyl-CoA is converted to succinate, three equivalents of NADH, and one equivalent of [FADH2](/source/Flavin_group). NADH and FADH2 are recycled (to NAD+ and [FAD](/source/Flavin_adenine_dinucleotide), respectively) by [oxidative phosphorylation](/source/Oxidative_phosphorylation), generating additional ATP. The oxidation of NADH results in the synthesis of 2–3 equivalents of ATP, and the oxidation of one FADH2 yields between 1–2 equivalents of ATP.[23] The majority of cellular ATP is generated by this process. Although the citric acid cycle itself does not involve molecular [oxygen](/source/Oxygen), it is an obligately [aerobic](/source/Aerobic_glycolysis) process because O2 is used to recycle the NADH and FADH2. In the absence of oxygen, the citric acid cycle ceases.[24]

The generation of ATP by the mitochondrion from cytosolic NADH relies on the [malate-aspartate shuttle](/source/Malate-aspartate_shuttle) (and to a lesser extent, the [glycerol-phosphate shuttle](/source/Glycerol-phosphate_shuttle)) because the inner mitochondrial membrane is impermeable to NADH and NAD+. Instead of transferring the generated NADH, a [malate dehydrogenase](/source/Malate_dehydrogenase) enzyme converts [oxaloacetate](/source/Oxaloacetate) to [malate](/source/Malate), which is translocated to the mitochondrial matrix. Another malate dehydrogenase-catalyzed reaction occurs in the opposite direction, producing oxaloacetate and NADH from the newly transported malate and the mitochondrion's interior store of NAD+. A [transaminase](/source/Transaminase) converts the oxaloacetate to [aspartate](/source/Aspartate) for transport back across the membrane and into the intermembrane space.[24]

In oxidative phosphorylation, the passage of electrons from NADH and FADH2 through the electron transport chain releases the energy to pump [protons](/source/Proton) out of the mitochondrial matrix and into the intermembrane space. This pumping generates a [proton motive force](/source/Proton_motive_force) that is the net effect of a pH gradient and an [electric potential](/source/Electric_potential) gradient across the inner mitochondrial membrane. Flow of protons down this potential gradient – that is, from the intermembrane space to the matrix – yields ATP by ATP synthase.[27] 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](/source/Hypoxia_(medical))), intracellular acidosis (mediated by enhanced glycolytic rates and [ATP hydrolysis](/source/ATP_hydrolysis)), contributes to mitochondrial membrane potential and directly drives ATP synthesis.[28]

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](/source/Antiporter), the ADP/ATP translocase, which is an [integral membrane protein](/source/Integral_membrane_protein) used to exchange newly synthesized ATP in the matrix for ADP in the intermembrane space.[29]

#### Regulation

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](/source/Calcium), inorganic phosphate, ATP, ADP, and AMP. [Citrate](/source/Citrate) – the ion that gives its name to the cycle – is a feedback inhibitor of [citrate synthase](/source/Citrate_synthase) and also inhibits PFK, providing a direct link between the regulation of the citric acid cycle and glycolysis.[25]

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#### Beta oxidation

Main article: [Beta-oxidation](/source/Beta-oxidation)

In the presence of air and various cofactors and enzymes, fatty acids are converted to [acetyl-CoA](/source/Acetyl-CoA). The pathway is called [beta-oxidation](/source/Beta-oxidation). Each cycle of beta-oxidation shortens the fatty acid chain by two carbon atoms and produces one equivalent each of acetyl-CoA, NADH, and FADH2. The acetyl-CoA is metabolized by the citric acid cycle to generate ATP, while the NADH and FADH2 are used by oxidative phosphorylation to generate ATP. Dozens of ATP equivalents are generated by the beta-oxidation of a single long acyl chain.[30]

#### Regulation

In oxidative phosphorylation, the key control point is the reaction catalyzed by [cytochrome c oxidase](/source/Cytochrome_c_oxidase), which is regulated by the availability of its substrate – the reduced form of [cytochrome c](/source/Cytochrome_c). The amount of reduced cytochrome c available is directly related to the amounts of other substrates:

- 1 2 NADH + cyt c ox + ADP + P i ⇌ 1 2 NAD + + cyt c red + ATP {\displaystyle {\frac {1}{2}}{\ce {NADH}}+{\ce {cyt}}\ {\ce {c_{ox}}}+{\ce {ADP}}+{\ce {P_{i}}}\rightleftharpoons {\frac {1}{2}}{\ce {NAD^+}}+{\ce {cyt}}\ {\ce {c_{red}}}+{\ce {ATP}}}

which directly implies this equation:

- [ c y t c r e d ] [ c y t c o x ] = ( [ N A D H ] [ N A D ] + ) 1 2 ( [ A D P ] [ P i ] [ A T P ] ) K e q {\displaystyle {\frac {[\mathrm {cyt~c_{red}} ]}{[\mathrm {cyt~c_{ox}} ]}}=\left({\frac {[\mathrm {NADH} ]}{[\mathrm {NAD} ]^{+}}}\right)^{\frac {1}{2}}\left({\frac {[\mathrm {ADP} ][\mathrm {P_{i}} ]}{[\mathrm {ATP} ]}}\right)K_{\mathrm {eq} }}

Thus, a high ratio of [NADH] to [NAD+] or a high ratio of [ADP] [Pi] to [ATP] imply a high amount of reduced cytochrome c and a high level of cytochrome c oxidase activity.[25] An additional level of regulation is introduced by the transport rates of ATP and NADH between the mitochondrial matrix and the cytoplasm.[29]

#### Ketosis

Main article: [Ketone bodies](/source/Ketone_bodies)

Ketone bodies can be used as fuels, yielding 22 ATP and 2 [GTP](/source/Guanosine_triphosphate) molecules per acetoacetate molecule when oxidized in the mitochondria. Ketone bodies are transported from the [liver](/source/Liver) to other tissues, where [acetoacetate](/source/Acetoacetate) and [*beta*-hydroxybutyrate](/source/Beta-Hydroxybutyric_acid) can be reconverted to acetyl-CoA to produce reducing equivalents (NADH and FADH2), via the citric acid cycle. Ketone bodies cannot be used as fuel by the liver, because the liver lacks the enzyme β-ketoacyl-CoA transferase, also called [thiolase](/source/Thiolase). [Acetoacetate](/source/Acetoacetate) in low concentrations is taken up by the liver and undergoes detoxification through the methylglyoxal pathway which ends with lactate. Acetoacetate in high concentrations is absorbed by cells other than those in the liver and enters a different pathway via [1,2-propanediol](/source/1%2C2-propanediol). Though the pathway follows a different series of steps requiring ATP, 1,2-propanediol can be turned into pyruvate.[31]

### Production, anaerobic conditions

[Fermentation](/source/Fermentation_(biochemistry)) is the metabolism of organic compounds in the absence of air. It involves [substrate-level phosphorylation](/source/Substrate-level_phosphorylation) in the absence of a respiratory [electron transport chain](/source/Electron_transport_chain).

The equation for the reaction of glucose to form [lactic acid](/source/Lactic_acid) is:

- C6H12O6 + 2 ADP + 2 Pi → 2 CH3CH(OH)COOH + 2 ATP + 2 H2O

[Anaerobic respiration](/source/Anaerobic_respiration) is respiration in the absence of [O2](/source/Oxygen). Prokaryotes can utilize a variety of electron acceptors. These include [nitrate](/source/Nitrate), [sulfate](/source/Sulfate), and carbon dioxide. In anaerobic organisms and prokaryotes, different pathways result in ATP. ATP is produced in the chloroplasts of green plants in a process similar to oxidative phosphorylation, called photophosphorylation.[6]

#### ATP replenishment by nucleoside diphosphate kinases

ATP can also be synthesized through several so-called "replenishment" reactions catalyzed by the enzyme families of [nucleoside diphosphate kinases](/source/Nucleoside_diphosphate_kinase) (NDKs), which use other nucleoside triphosphates as a high-energy phosphate donor, and the [ATP:guanido-phosphotransferase](/source/ATP%3Aguanido_phosphotransferase_family) family.[*[citation needed](https://en.wikipedia.org/wiki/Wikipedia:Citation_needed)*]

### ATP production during photosynthesis

In plants, ATP is synthesized in the [thylakoid membrane](/source/Thylakoid_membrane) of the [chloroplast](/source/Chloroplast). The process is called [photophosphorylation](/source/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.[32] Some of the ATP produced in the chloroplasts is consumed in the [Calvin cycle](/source/Calvin_cycle), which produces [triose](/source/Triose) sugars.

### ATP recycling

The total quantity of ATP in the human body is about 0.1 [mol/L](/source/Molar_concentration).[33] 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.[34] Each equivalent of ATP is recycled 1000–1500 times during a single day (150 / 0.1 = 1500),[33] at approximately 9×1020 molecules/s.[33]

An example of the Rossmann fold, a [structural domain](/source/Structural_domain) of a [decarboxylase](/source/Decarboxylase) enzyme from the bacterium *[Staphylococcus epidermidis](/source/Staphylococcus_epidermidis)* ([PDB](/source/Protein_Data_Bank): [1G5Q](https://www.rcsb.org/structure/1G5Q)​) with a bound [flavin mononucleotide](/source/Flavin_mononucleotide) cofactor

## Biochemical functions

### Cellular energy production

The conversion of ATP to ADP is the principal mechanism for energy supply in biological processes.[6] Energy is produced in cells when the terminal phosphate group in an ATP molecule is removed from the chain to produce adenosine diphosphate (ADP) when water hydrolyzes ATP:[6]

ATP + H2O → ADP + HPO42- + H+ + energy

However, removing a phosphate group from ADP to produce adenosine monophosphate (AMP) also produces extra energy.[6]

### Intracellular signaling

ATP is involved in [signal transduction](/source/Signal_transduction) by serving as substrate for kinases, enzymes that transfer phosphate groups. Kinases are the most common ATP-binding proteins. They share a small number of common folds.[35] [Phosphorylation](/source/Phosphorylation) of a protein by a kinase can activate a cascade such as the [mitogen-activated protein kinase](/source/Mitogen-activated_protein_kinase) cascade.[36]

ATP is also a substrate of [adenylate cyclase](/source/Adenylate_cyclase), most commonly in [G protein-coupled receptor](/source/G_protein%E2%80%93coupled_receptor) signal transduction pathways and is transformed to [second messenger](/source/Second_messenger), cyclic AMP, which is involved in triggering calcium signals by the release of calcium from intracellular stores.[37] 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.[38]

### DNA and RNA synthesis

ATP is one of four monomers required in the synthesis of [RNA](/source/RNA). The process is promoted by [RNA polymerases](/source/RNA_polymerase).[39] A similar process occurs in the formation of DNA, except that ATP is first converted to the [deoxyribonucleotide](/source/Deoxyribonucleotide) dATP. Like many condensation reactions in nature, [DNA replication](/source/DNA_replication) and [DNA transcription](/source/DNA_transcription) also consume ATP.

### Amino acid activation in protein synthesis

Main article: [Amino acid activation](/source/Amino_acid_activation)

[Aminoacyl-tRNA synthetase](/source/Aminoacyl-tRNA_synthetase) enzymes consume ATP in the attachment tRNA to amino acids, forming aminoacyl-tRNA complexes. Aminoacyl transferase binds AMP-amino acid to tRNA. The coupling reaction proceeds in two steps:

1. aa + ATP ⟶ aa-AMP + [PPi](/source/Pyrophosphate)

1. aa-AMP + tRNA ⟶ aa-tRNA + AMP

The amino acid is coupled to the penultimate nucleotide at the 3′-end of the tRNA (the A in the sequence CCA) via an ester bond (roll over in illustration).

### ATP binding cassette transporter

Transporting chemicals out of a cell against a gradient is often associated with ATP hydrolysis. Transport is mediated by [ATP binding cassette transporters](/source/ATP_binding_cassette_transporter). The human genome encodes 48 ABC transporters, that are used for exporting drugs, lipids, and other compounds.[40]

### Extracellular signalling and neurotransmission

Cells secrete ATP to communicate with other cells in a process called [purinergic signalling](/source/Purinergic_signalling). ATP serves as a [neurotransmitter](/source/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[41][42] or is pumped into vesicles[43] which then [fuse](/source/Exocytosis) with the membrane. Cells detect ATP using the [purinergic receptor](/source/Purinergic_receptor) proteins [P2X](/source/P2X_purinoreceptor) and [P2Y](/source/P2Y_receptor).[44] ATP has been shown to be a critically important signalling molecule for [microglia](/source/Microglia) - [neuron](/source/Neuron) interactions in the adult brain,[45] as well as during brain development.[46] Furthermore, tissue-injury induced ATP-signalling is a major factor in rapid microglial phenotype changes.[47]

### Muscle contraction

ATP fuels [muscle contractions](/source/Muscle_contraction).[48] Muscle contractions are regulated by signaling pathways, although different [muscle](/source/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](/source/Actin) and [myosin](/source/Myosin).[49]

ATP is initially bound to myosin. When [ATPase](/source/ATPase) hydrolyzes the bound ATP into [ADP](/source/Adenosine_diphosphate) and inorganic [phosphate](/source/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.[49][50]

### Protein solubility

ATP has recently been proposed to act as a biological [hydrotrope](/source/Hydrotrope)[51] and has been shown to affect proteome-wide solubility.[52]

## Abiogenic origins

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.[53] 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.[54]

## ATP analogues

Biochemistry laboratories often use *[in vitro](/source/In_vitro)* studies to explore ATP-dependent molecular processes. ATP analogs are also used in [X-ray crystallography](/source/X-ray_crystallography) to determine a [protein structure](/source/Protein_structure) in complex with ATP, often together with other substrates.[*[citation needed](https://en.wikipedia.org/wiki/Wikipedia:Citation_needed)*]

[Enzyme inhibitors](/source/Enzyme_inhibitor) of ATP-dependent enzymes such as [kinases](/source/Kinase) are needed to examine the [binding sites](/source/Binding_site) and [transition states](/source/Transition_state) involved in ATP-dependent reactions.[*[citation needed](https://en.wikipedia.org/wiki/Wikipedia:Citation_needed)*]

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](/source/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](/source/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.[55]

## Medical use

ATP is used intravenously for some heart-related conditions.[56]

## History

ATP was discovered in 1929 from muscle tissue by [Karl Lohmann](https://en.wikipedia.org/w/index.php?title=Karl_Lohmann_(biochemist)&action=edit&redlink=1) [[de](https://de.wikipedia.org/wiki/Karl_Lohmann_(Biochemiker))][6][57] and Jendrassik[58] and, independently, by Cyrus Fiske and [Yellapragada Subba Rao](/source/Yellapragada_Subba_Rao) of [Harvard Medical School](/source/Harvard_Medical_School),[59] 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](/source/Fritz_Albert_Lipmann) in 1941.[60] He played a major role in establishing that ATP is the energy [currency](/source/Currency) of a cell.[6]

It was first synthesized in the laboratory by [Alexander Todd](/source/Alexander_R._Todd%2C_Baron_Todd) in 1948,[61] and he was awarded the [Nobel Prize in Chemistry](/source/Nobel_Prize_in_Chemistry) in 1957 partly for this work.

The 1978 [Nobel Prize in Chemistry](/source/Nobel_Prize_in_Chemistry) was awarded to [Peter Dennis Mitchell](/source/Peter_D._Mitchell) for the discovery of the [chemiosmotic](/source/Chemiosmosis) mechanism of ATP synthesis.

The 1997 Nobel Prize in Chemistry was divided, one half jointly to [Paul D. Boyer](/source/Paul_D._Boyer) and [John E. Walker](/source/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](/source/Jens_C._Skou) "for the first discovery of an ion-transporting enzyme, Na+, K+ -ATPase."[62]

## See also

- [Adenosine-tetraphosphatase](/source/Adenosine-tetraphosphatase)

- [Adenosine methylene triphosphate](/source/NDPCP)

- [ATPases](/source/ATPases)

- [ATP test](/source/ATP_test)

- [Creatine](/source/Creatine)

- [Cyclic adenosine monophosphate](/source/Cyclic_adenosine_monophosphate) (cAMP)

- [Nucleotide exchange factor](/source/Nucleotide_exchange_factor)

- [Phosphagen](/source/Phosphagen)

## References

1. ^ [***a***](#cite_ref-lamda_source_1_1-0) [***b***](#cite_ref-lamda_source_1_1-1) ["Adenosine 5'-triphosphate disodium salt Product Information"](https://www.sigmaaldrich.com/content/dam/sigma-aldrich/docs/Sigma/Product_Information_Sheet/a7699pis.pdf) (PDF). Sigma. [Archived](https://web.archive.org/web/20190323054630/https://www.sigmaaldrich.com/content/dam/sigma-aldrich/docs/Sigma/Product_Information_Sheet/a7699pis.pdf) (PDF) from the original on 2019-03-23. Retrieved 2019-03-22.

1. **[^](#cite_ref-2)** Dunn, Jacob; Grider, Michael H. (2023). ["Physiology, Adenosine Triphosphate"](https://www.ncbi.nlm.nih.gov/books/NBK553175/). *StatPearls*. StatPearls Publishing. [PMID](/source/PMID_(identifier)) [31985968](https://pubmed.ncbi.nlm.nih.gov/31985968). Retrieved 13 November 2023.

1. **[^](#cite_ref-Georgiev2026_3-0)** Georgiev, Danko D.; Tasinov, Oskan B.; Pavlov, Danail V.; Hrusafov, Deyan S. (2026). ["Reduced Gibbs free energy supply hinders brain information processing during mental fatigue"](https://www.tandfonline.com/doi/full/10.1080/21641846.2026.2636450). *Fatigue: Biomedicine, Health & Behavior*. [doi](/source/Doi_(identifier)):[10.1080/21641846.2026.2636450](https://doi.org/10.1080%2F21641846.2026.2636450).

1. **[^](#cite_ref-4)** [Knowles, Jeremy Randall](/source/Jeremy_R._Knowles) (1980). "Enzyme-catalyzed phosphoryl transfer reactions". *Annual Review of Biochemistry*. **49** (1): 877–919. [Bibcode](/source/Bibcode_(identifier)):[1980ARBio..49..877K](https://ui.adsabs.harvard.edu/abs/1980ARBio..49..877K). [doi](/source/Doi_(identifier)):[10.1146/annurev.bi.49.070180.004305](https://doi.org/10.1146%2Fannurev.bi.49.070180.004305). [PMID](/source/PMID_(identifier)) [6250450](https://pubmed.ncbi.nlm.nih.gov/6250450).

1. **[^](#cite_ref-5)** "An average individual with a daily diet of 8000 kJ and a 30% efficiency of turning foodstuffs into chemical energy will synthesize (and hydrolyze) about 50 kg of ATP during 1 day." Wilkens, Stephan (2008). "ATP Synthesis, Chemistry of". *Wiley Encyclopedia of Chemical Biology*. [doi](/source/Doi_(identifier)):[10.1002/9780470048672.wecb648](https://doi.org/10.1002%2F9780470048672.wecb648). [ISBN](/source/ISBN_(identifier)) [978-0-471-75477-0](https://en.wikipedia.org/wiki/Special:BookSources/978-0-471-75477-0).

1. ^ [***a***](#cite_ref-Myers_6-0) [***b***](#cite_ref-Myers_6-1) [***c***](#cite_ref-Myers_6-2) [***d***](#cite_ref-Myers_6-3) [***e***](#cite_ref-Myers_6-4) [***f***](#cite_ref-Myers_6-5) [***g***](#cite_ref-Myers_6-6) Myers, Richard L. (2007). [*The 100 Most Important Chemical Compounds: A Reference Guide*](https://books.google.com/books?id=0AnJU-hralEC). ABC-CLIO. pp. 18–19. [ISBN](/source/ISBN_(identifier)) [978-0-313-33758-1](https://en.wikipedia.org/wiki/Special:BookSources/978-0-313-33758-1). [Archived](https://web.archive.org/web/20160617093705/https://books.google.com/books?id=0AnJU-hralEC) from the original on 17 June 2016. Retrieved 21 November 2015.

1. **[^](#cite_ref-7)** Dunn, Jacob; Grider, Michael H. (2023), ["Physiology, Adenosine Triphosphate"](https://www.ncbi.nlm.nih.gov/books/NBK553175/), *StatPearls*, Treasure Island (FL): StatPearls Publishing, [PMID](/source/PMID_(identifier)) [31985968](https://pubmed.ncbi.nlm.nih.gov/31985968), retrieved 2023-09-28

1. ^ [***a***](#cite_ref-Storer_8-0) [***b***](#cite_ref-Storer_8-1) Storer, A.; [Cornish-Bowden, A.](/source/Athel_Cornish-Bowden) (1976). ["Concentration of MgATP2− and other ions in solution. Calculation of the true concentrations of species present in mixtures of associating ions"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1164030). *Biochemical Journal*. **159** (1): 1–5. [doi](/source/Doi_(identifier)):[10.1042/bj1590001](https://doi.org/10.1042%2Fbj1590001). [PMC](/source/PMC_(identifier)) [1164030](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1164030). [PMID](/source/PMID_(identifier)) [11772](https://pubmed.ncbi.nlm.nih.gov/11772).

1. **[^](#cite_ref-9)** Wilson, J.; Chin, A. (1991). "Chelation of divalent cations by ATP, studied by titration calorimetry". *Anal. Biochem*. **193** (1): 16–19. [doi](/source/Doi_(identifier)):[10.1016/0003-2697(91)90036-S](https://doi.org/10.1016%2F0003-2697%2891%2990036-S). [PMID](/source/PMID_(identifier)) [1645933](https://pubmed.ncbi.nlm.nih.gov/1645933).

1. **[^](#cite_ref-10)** Garfinkel, Lillian; Altschuld, Ruth A.; Garfinkel, David (1986). "Magnesium in cardiac energy metabolism". *Journal of Molecular and Cellular Cardiology*. **18** (10): 1003–1013. [doi](/source/Doi_(identifier)):[10.1016/S0022-2828(86)80289-9](https://doi.org/10.1016%2FS0022-2828%2886%2980289-9). [PMID](/source/PMID_(identifier)) [3537318](https://pubmed.ncbi.nlm.nih.gov/3537318).

1. **[^](#cite_ref-Saylor_11-0)** Saylor, P.; Wang, C.; Hirai, T.; Adams, J. (1998). "A second magnesium ion is critical for ATP binding in the kinase domain of the oncoprotein v-Fps". *Biochemistry*. **37** (36): 12624–12630. [doi](/source/Doi_(identifier)):[10.1021/bi9812672](https://doi.org/10.1021%2Fbi9812672). [PMID](/source/PMID_(identifier)) [9730835](https://pubmed.ncbi.nlm.nih.gov/9730835).

1. **[^](#cite_ref-Lin_12-0)** Lin, X.; Ayrapetov, M; Sun, G. (2005). ["Characterization of the interactions between the active site of a protein tyrosine kinase and a divalent metal activator"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1316873). *BMC Biochem*. **6** 25. [doi](/source/Doi_(identifier)):[10.1186/1471-2091-6-25](https://doi.org/10.1186%2F1471-2091-6-25). [PMC](/source/PMC_(identifier)) [1316873](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1316873). [PMID](/source/PMID_(identifier)) [16305747](https://pubmed.ncbi.nlm.nih.gov/16305747).

1. **[^](#cite_ref-13)** Budavari, Susan, ed. (2001). *[The Merck Index: An Encyclopedia of Chemicals, Drugs, and Biologicals](/source/Merck_Index)* (13th ed.). Merck. [ISBN](/source/ISBN_(identifier)) [0911910131](https://en.wikipedia.org/wiki/Special:BookSources/0911910131).

1. ^ [***a***](#cite_ref-Nicholls_14-0) [***b***](#cite_ref-Nicholls_14-1) Ferguson, S. J.; Nicholls, David; Ferguson, Stuart (2002). *Bioenergetics 3* (3rd ed.). San Diego, CA: Academic. [ISBN](/source/ISBN_(identifier)) [978-0-12-518121-1](https://en.wikipedia.org/wiki/Special:BookSources/978-0-12-518121-1).

1. **[^](#cite_ref-Stryer_p376_15-0)** Berg, J. M.; Tymoczko, J. L.; Stryer, L. (2003). [*Biochemistry*](https://archive.org/details/biochemistry200100jere). New York, NY: W. H. Freeman. p. [376](https://archive.org/details/biochemistry200100jere/page/376). [ISBN](/source/ISBN_(identifier)) [978-0-7167-4684-3](https://en.wikipedia.org/wiki/Special:BookSources/978-0-7167-4684-3).

1. **[^](#cite_ref-16)** Chance, B.; Lees, H.; Postgate, J. G. (1972). "The Meaning of "Reversed Electron Flow" and "High Energy Electron" in Biochemistry". *Nature*. **238** (5363): 330–331. [Bibcode](/source/Bibcode_(identifier)):[1972Natur.238..330C](https://ui.adsabs.harvard.edu/abs/1972Natur.238..330C). [doi](/source/Doi_(identifier)):[10.1038/238330a0](https://doi.org/10.1038%2F238330a0). [PMID](/source/PMID_(identifier)) [4561837](https://pubmed.ncbi.nlm.nih.gov/4561837). [S2CID](/source/S2CID_(identifier)) [4298762](https://api.semanticscholar.org/CorpusID:4298762).

1. **[^](#cite_ref-17)** Gajewski, E.; Steckler, D.; Goldberg, R. (1986). ["Thermodynamics of the hydrolysis of adenosine 5′-triphosphate to adenosine 5′-diphosphate"](https://doi.org/10.1016%2FS0021-9258%2818%2967153-4). *J. Biol. Chem*. **261** (27): 12733–12737. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(18)67153-4](https://doi.org/10.1016%2FS0021-9258%2818%2967153-4). [PMID](/source/PMID_(identifier)) [3528161](https://pubmed.ncbi.nlm.nih.gov/3528161).

1. **[^](#cite_ref-18)** Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert (2007). *Biochemistry* (6th ed.). New York, NY: W. H. Freeman. p. 413. [ISBN](/source/ISBN_(identifier)) [978-0-7167-8724-2](https://en.wikipedia.org/wiki/Special:BookSources/978-0-7167-8724-2).

1. **[^](#cite_ref-Nelson-2021_19-0)** Nelson, David L.; Cox, Michael M. (2021). *Lehninger Principles of Biochemistry* (4th ed.). New York: W. H. Freeman and Company.

1. **[^](#cite_ref-20)** Garrett, Reginald H.; Grisham, Charles M. (2016). *Biochemistry* (6th ed.). Cengage Learning. p. 68. [ISBN](/source/ISBN_(identifier)) [978-1-305-57720-6](https://en.wikipedia.org/wiki/Special:BookSources/978-1-305-57720-6).

1. **[^](#cite_ref-21)** Beis, I.; Newsholme, E. A. (October 1, 1975). ["The Contents of Adenine Nucleotides, Phosphagens and some glycolytic intermediates in resting muscles from vertebrates and invertebrates"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1172435). *Biochemical Journal*. **152** (1): 23–32. [doi](/source/Doi_(identifier)):[10.1042/bj1520023](https://doi.org/10.1042%2Fbj1520023). [PMC](/source/PMC_(identifier)) [1172435](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1172435). [PMID](/source/PMID_(identifier)) [1212224](https://pubmed.ncbi.nlm.nih.gov/1212224).

1. **[^](#cite_ref-brit_22-0)** ["Adenosine triphosphate"](https://www.britannica.com/science/adenosine-triphosphate). Britannica. 11 November 2023. Retrieved 1 December 2023.

1. ^ [***a***](#cite_ref-Rich_23-0) [***b***](#cite_ref-Rich_23-1) Rich, P. R. (2003). "The molecular machinery of Keilin's respiratory chain". *Biochem. Soc. Trans*. **31** (6): 1095–1105. [doi](/source/Doi_(identifier)):[10.1042/BST0311095](https://doi.org/10.1042%2FBST0311095). [PMID](/source/PMID_(identifier)) [14641005](https://pubmed.ncbi.nlm.nih.gov/14641005).

1. ^ [***a***](#cite_ref-Lodish_24-0) [***b***](#cite_ref-Lodish_24-1) [***c***](#cite_ref-Lodish_24-2) Lodish, H.; Berk, A.; Matsudaira, P.; Kaiser, C. A.; Krieger, M.; Scott, M. P.; Zipursky, S. L.; Darnell, J. (2004). [*Molecular Cell Biology*](https://archive.org/details/molecularcellbio00harv) (5th ed.). New York, NY: W. H. Freeman. [ISBN](/source/ISBN_(identifier)) [978-0-7167-4366-8](https://en.wikipedia.org/wiki/Special:BookSources/978-0-7167-4366-8).

1. ^ [***a***](#cite_ref-Voet_25-0) [***b***](#cite_ref-Voet_25-1) [***c***](#cite_ref-Voet_25-2) [***d***](#cite_ref-Voet_25-3) [***e***](#cite_ref-Voet_25-4) Voet, D.; Voet, J. G. (2004). *Biochemistry*. Vol. 1 (3rd ed.). Hoboken, NJ: Wiley. [ISBN](/source/ISBN_(identifier)) [978-0-471-19350-0](https://en.wikipedia.org/wiki/Special:BookSources/978-0-471-19350-0).

1. **[^](#cite_ref-glycolysis_animation_26-0)** Mehta S (20 September 2011). ["Glycolysis – Animation and Notes"](https://web.archive.org/web/20120325151810/http://pharmaxchange.info/press/2011/09/glycolysis-animation-and-notes/). *PharmaXchange*. Archived from [the original](http://pharmaxchange.info/press/2011/09/glycolysis-animation-and-notes/) on 25 March 2012. Retrieved 22 September 2011.

1. **[^](#cite_ref-27)** Abrahams, J.; Leslie, A.; Lutter, R.; Walker, J. (1994). "Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria". *Nature*. **370** (6491): 621–628. [Bibcode](/source/Bibcode_(identifier)):[1994Natur.370..621A](https://ui.adsabs.harvard.edu/abs/1994Natur.370..621A). [doi](/source/Doi_(identifier)):[10.1038/370621a0](https://doi.org/10.1038%2F370621a0). [PMID](/source/PMID_(identifier)) [8065448](https://pubmed.ncbi.nlm.nih.gov/8065448). [S2CID](/source/S2CID_(identifier)) [4275221](https://api.semanticscholar.org/CorpusID:4275221).

1. **[^](#cite_ref-28)** Devaux, JBL; Hedges, CP; Hickey, AJR (January 2019). ["Acidosis Maintains the Function of Brain Mitochondria in Hypoxia-Tolerant Triplefin Fish: A Strategy to Survive Acute Hypoxic Exposure?"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6346031). *Front Physiol*. 9, 1914 1941. [doi](/source/Doi_(identifier)):[10.3389/fphys.2018.01941](https://doi.org/10.3389%2Ffphys.2018.01941). [PMC](/source/PMC_(identifier)) [6346031](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6346031). [PMID](/source/PMID_(identifier)) [30713504](https://pubmed.ncbi.nlm.nih.gov/30713504).

1. ^ [***a***](#cite_ref-Brandolin_29-0) [***b***](#cite_ref-Brandolin_29-1) Dahout-Gonzalez, C.; Nury, H.; Trézéguet, V.; Lauquin, G.; Pebay-Peyroula, E.; Brandolin, G. (2006). "Molecular, functional, and pathological aspects of the mitochondrial ADP/ATP carrier". *Physiology*. **21** (4): 242–249. [doi](/source/Doi_(identifier)):[10.1152/physiol.00005.2006](https://doi.org/10.1152%2Fphysiol.00005.2006). [PMID](/source/PMID_(identifier)) [16868313](https://pubmed.ncbi.nlm.nih.gov/16868313).

1. **[^](#cite_ref-30)** Ronnett, G.; Kim, E.; Landree, L.; Tu, Y. (2005). "Fatty acid metabolism as a target for obesity treatment". *Physiol. Behav*. **85** (1): 25–35. [doi](/source/Doi_(identifier)):[10.1016/j.physbeh.2005.04.014](https://doi.org/10.1016%2Fj.physbeh.2005.04.014). [PMID](/source/PMID_(identifier)) [15878185](https://pubmed.ncbi.nlm.nih.gov/15878185). [S2CID](/source/S2CID_(identifier)) [24865576](https://api.semanticscholar.org/CorpusID:24865576).

1. **[^](#cite_ref-Environmental_Protection_Agency;_TOXICOLOGICAL_REVIEW_OF_ACETONE_(CAS_No._67-64-1)_31-0)** ["Integrated Risk Information System"](https://web.archive.org/web/20150924074331/http://www.epa.gov/iris/toxreviews/0128tr.pdf) (PDF). 2013-03-15. Archived from [the original](http://www.epa.gov/iris/toxreviews/0128tr.pdf) (PDF) on 2015-09-24. Retrieved 2019-02-01.

1. **[^](#cite_ref-32)** Allen, J. (2002). ["Photosynthesis of ATP-electrons, proton pumps, rotors, and poise"](https://doi.org/10.1016%2FS0092-8674%2802%2900870-X). *Cell*. **110** (3): 273–276. [doi](/source/Doi_(identifier)):[10.1016/S0092-8674(02)00870-X](https://doi.org/10.1016%2FS0092-8674%2802%2900870-X). [PMID](/source/PMID_(identifier)) [12176312](https://pubmed.ncbi.nlm.nih.gov/12176312). [S2CID](/source/S2CID_(identifier)) [1754660](https://api.semanticscholar.org/CorpusID:1754660).

1. ^ [***a***](#cite_ref-Fuhrman-1061_33-0) [***b***](#cite_ref-Fuhrman-1061_33-1) [***c***](#cite_ref-Fuhrman-1061_33-2) Fuhrman, Bradley P.; Zimmerman, Jerry J. (2011). [*Pediatric Critical Care*](https://www.sciencedirect.com/science/article/pii/B9780323073073100746#s0025). Elsevier. p. 1061. [ISBN](/source/ISBN_(identifier)) [978-0-323-07307-3](https://en.wikipedia.org/wiki/Special:BookSources/978-0-323-07307-3). Retrieved 16 May 2020.

1. **[^](#cite_ref-Fuhrman_34-0)** Fuhrman, Bradley P.; Zimmerman, Jerry J. (2011). [*Pediatric Critical Care*](https://www.sciencedirect.com/science/article/pii/B9780323073073100746#s0025). Elsevier. pp. 1058–1072. [ISBN](/source/ISBN_(identifier)) [978-0-323-07307-3](https://en.wikipedia.org/wiki/Special:BookSources/978-0-323-07307-3). Retrieved 16 May 2020.

1. **[^](#cite_ref-Scheeff_35-0)** Scheeff, E.; Bourne, P. (2005). ["Structural evolution of the protein kinase-like superfamily"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1261164). *PLOS Comput. Biol*. **1** (5) e49. [Bibcode](/source/Bibcode_(identifier)):[2005PLSCB...1...49S](https://ui.adsabs.harvard.edu/abs/2005PLSCB...1...49S). [doi](/source/Doi_(identifier)):[10.1371/journal.pcbi.0010049](https://doi.org/10.1371%2Fjournal.pcbi.0010049). [PMC](/source/PMC_(identifier)) [1261164](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1261164). [PMID](/source/PMID_(identifier)) [16244704](https://pubmed.ncbi.nlm.nih.gov/16244704).

1. **[^](#cite_ref-36)** Mishra, N.; Tuteja, R.; Tuteja, N. (2006). "Signaling through MAP kinase networks in plants". *Arch. Biochem. Biophys*. **452** (1): 55–68. [doi](/source/Doi_(identifier)):[10.1016/j.abb.2006.05.001](https://doi.org/10.1016%2Fj.abb.2006.05.001). [PMID](/source/PMID_(identifier)) [16806044](https://pubmed.ncbi.nlm.nih.gov/16806044).

1. **[^](#cite_ref-37)** Kamenetsky, M.; Middelhaufe, S.; Bank, E.; Levin, L.; Buck, J.; Steegborn, C. (2006). ["Molecular details of cAMP generation in mammalian cells: a tale of two systems"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3662476). *J. Mol. Biol*. **362** (4): 623–639. [doi](/source/Doi_(identifier)):[10.1016/j.jmb.2006.07.045](https://doi.org/10.1016%2Fj.jmb.2006.07.045). [PMC](/source/PMC_(identifier)) [3662476](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3662476). [PMID](/source/PMID_(identifier)) [16934836](https://pubmed.ncbi.nlm.nih.gov/16934836).

1. **[^](#cite_ref-38)** Hanoune, J.; Defer, N. (2001). "Regulation and role of adenylyl cyclase isoforms". *Annu. Rev. Pharmacol. Toxicol*. **41** (1): 145–174. [doi](/source/Doi_(identifier)):[10.1146/annurev.pharmtox.41.1.145](https://doi.org/10.1146%2Fannurev.pharmtox.41.1.145). [PMID](/source/PMID_(identifier)) [11264454](https://pubmed.ncbi.nlm.nih.gov/11264454).

1. **[^](#cite_ref-39)** Joyce, C. M.; Steitz, T. A. (1995). ["Polymerase structures and function: variations on a theme?"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC177480). *J. Bacteriol*. **177** (22): 6321–6329. [doi](/source/Doi_(identifier)):[10.1128/jb.177.22.6321-6329.1995](https://doi.org/10.1128%2Fjb.177.22.6321-6329.1995). [PMC](/source/PMC_(identifier)) [177480](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC177480). [PMID](/source/PMID_(identifier)) [7592405](https://pubmed.ncbi.nlm.nih.gov/7592405).

1. **[^](#cite_ref-40)** Borst, P.; Elferink, R. Oude (2002). ["Mammalian ABC transporters in health and disease"](https://pure.uva.nl/ws/files/3499814/42885_202387y.pdf) (PDF). *Annual Review of Biochemistry*. **71** (1): 537–592. [Bibcode](/source/Bibcode_(identifier)):[2002ARBio..71..537B](https://ui.adsabs.harvard.edu/abs/2002ARBio..71..537B). [doi](/source/Doi_(identifier)):[10.1146/annurev.biochem.71.102301.093055](https://doi.org/10.1146%2Fannurev.biochem.71.102301.093055). [PMID](/source/PMID_(identifier)) [12045106](https://pubmed.ncbi.nlm.nih.gov/12045106). [S2CID](/source/S2CID_(identifier)) [34707074](https://api.semanticscholar.org/CorpusID:34707074). [Archived](https://web.archive.org/web/20180421032744/https://pure.uva.nl/ws/files/3499814/42885_202387y.pdf) (PDF) from the original on 2018-04-21. Retrieved 2018-04-20.

1. **[^](#cite_ref-RomanovLasher2018_41-0)** Romanov, Roman A.; Lasher, Robert S.; High, Brigit; Savidge, Logan E.; Lawson, Adam; Rogachevskaja, Olga A.; Zhao, Haitian; Rogachevsky, Vadim V.; Bystrova, Marina F.; Churbanov, Gleb D.; Adameyko, Igor; Harkany, Tibor; Yang, Ruibiao; Kidd, Grahame J.; Marambaud, Philippe; Kinnamon, John C.; Kolesnikov, Stanislav S.; Finger, Thomas E. (2018). ["Chemical synapses without synaptic vesicles: Purinergic neurotransmission through a CALHM1 channel-mitochondrial signaling complex"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5966022). *Science Signaling*. **11** (529) eaao1815. [doi](/source/Doi_(identifier)):[10.1126/scisignal.aao1815](https://doi.org/10.1126%2Fscisignal.aao1815). [ISSN](/source/ISSN_(identifier)) [1945-0877](https://search.worldcat.org/issn/1945-0877). [PMC](/source/PMC_(identifier)) [5966022](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5966022). [PMID](/source/PMID_(identifier)) [29739879](https://pubmed.ncbi.nlm.nih.gov/29739879).

1. **[^](#cite_ref-Dahl2015_42-0)** Dahl, Gerhard (2015). ["ATP release through pannexon channels"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4455760). *Philosophical Transactions of the Royal Society B: Biological Sciences*. **370** (1672) 20140191. [doi](/source/Doi_(identifier)):[10.1098/rstb.2014.0191](https://doi.org/10.1098%2Frstb.2014.0191). [ISSN](/source/ISSN_(identifier)) [0962-8436](https://search.worldcat.org/issn/0962-8436). [PMC](/source/PMC_(identifier)) [4455760](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4455760). [PMID](/source/PMID_(identifier)) [26009770](https://pubmed.ncbi.nlm.nih.gov/26009770).

1. **[^](#cite_ref-LarssonSawada2012_43-0)** Larsson, Max; Sawada, Keisuke; Morland, Cecilie; Hiasa, Miki; Ormel, Lasse; Moriyama, Yoshinori; Gundersen, Vidar (2012). ["Functional and Anatomical Identification of a Vesicular Transporter Mediating Neuronal ATP Release"](https://doi.org/10.1093%2Fcercor%2Fbhr203). *Cerebral Cortex*. **22** (5): 1203–1214. [doi](/source/Doi_(identifier)):[10.1093/cercor/bhr203](https://doi.org/10.1093%2Fcercor%2Fbhr203). [ISSN](/source/ISSN_(identifier)) [1460-2199](https://search.worldcat.org/issn/1460-2199). [PMID](/source/PMID_(identifier)) [21810784](https://pubmed.ncbi.nlm.nih.gov/21810784).

1. **[^](#cite_ref-44)** Puchałowicz, Kamila; Tarnowski, Maciej; Baranowska-Bosiacka, Irena; Chlubek, Dariusz; Dziedziejko, Violetta (2014-12-18). ["P2X and P2Y Receptors—Role in the Pathophysiology of the Nervous System"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4284787). *International Journal of Molecular Sciences*. **15** (12): 23672–23704. [doi](/source/Doi_(identifier)):[10.3390/ijms151223672](https://doi.org/10.3390%2Fijms151223672). [ISSN](/source/ISSN_(identifier)) [1422-0067](https://search.worldcat.org/issn/1422-0067). [PMC](/source/PMC_(identifier)) [4284787](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4284787). [PMID](/source/PMID_(identifier)) [25530618](https://pubmed.ncbi.nlm.nih.gov/25530618).

1. **[^](#cite_ref-45)** Csaba, Cserep; Balazs, Pósfai (2020). ["Microglia monitor and protect neuronal function through specialized somatic purinergic junctions"](https://www.science.org/doi/10.1126/science.aax6752). *Science*. **367** (6477): 528–537. [Bibcode](/source/Bibcode_(identifier)):[2020Sci...367..528C](https://ui.adsabs.harvard.edu/abs/2020Sci...367..528C). [doi](/source/Doi_(identifier)):[10.1126/science.aax6752](https://doi.org/10.1126%2Fscience.aax6752). [PMID](/source/PMID_(identifier)) [31831638](https://pubmed.ncbi.nlm.nih.gov/31831638).

1. **[^](#cite_ref-46)** Csaba, Cserep; Anett, Schwarcz D (2022). ["Microglial control of neuronal development via somatic purinergic junctions"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9513806). *Cell Reports*. **40** (12) 111369. [doi](/source/Doi_(identifier)):[10.1016/j.celrep.2022.111369](https://doi.org/10.1016%2Fj.celrep.2022.111369). [PMC](/source/PMC_(identifier)) [9513806](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9513806). [PMID](/source/PMID_(identifier)) [36130488](https://pubmed.ncbi.nlm.nih.gov/36130488).

1. **[^](#cite_ref-47)** Peter, Berki; Csaba, Cserep; Zsuzsanna, Környei (2024). ["Microglia contribute to neuronal synchrony despite endogenous ATP-related phenotypic transformation in acute mouse brain slices"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11208608). *Nature Communications*. **15** (1): 5402. [Bibcode](/source/Bibcode_(identifier)):[2024NatCo..15.5402B](https://ui.adsabs.harvard.edu/abs/2024NatCo..15.5402B). [doi](/source/Doi_(identifier)):[10.1038/s41467-024-49773-1](https://doi.org/10.1038%2Fs41467-024-49773-1). [PMC](/source/PMC_(identifier)) [11208608](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11208608). [PMID](/source/PMID_(identifier)) [38926390](https://pubmed.ncbi.nlm.nih.gov/38926390).

1. **[^](#cite_ref-48)** Hultman, E.; Greenhaff, P. L. (1991). "Skeletal muscle energy metabolism and fatigue during intense exercise in man". *Science Progress*. **75** (298 Pt 3-4): 361–370. [ISSN](/source/ISSN_(identifier)) [0036-8504](https://search.worldcat.org/issn/0036-8504). [PMID](/source/PMID_(identifier)) [1842855](https://pubmed.ncbi.nlm.nih.gov/1842855).

1. ^ [***a***](#cite_ref-:0_49-0) [***b***](#cite_ref-:0_49-1) Kuo, Ivana Y.; Ehrlich, Barbara E. (February 2015). ["Signaling in Muscle Contraction"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4315934). *Cold Spring Harbor Perspectives in Biology*. **7** (2) a006023. [Bibcode](/source/Bibcode_(identifier)):[2015CSHPB...706023K](https://ui.adsabs.harvard.edu/abs/2015CSHPB...706023K). [doi](/source/Doi_(identifier)):[10.1101/cshperspect.a006023](https://doi.org/10.1101%2Fcshperspect.a006023). [ISSN](/source/ISSN_(identifier)) [1943-0264](https://search.worldcat.org/issn/1943-0264). [PMC](/source/PMC_(identifier)) [4315934](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4315934). [PMID](/source/PMID_(identifier)) [25646377](https://pubmed.ncbi.nlm.nih.gov/25646377).

1. **[^](#cite_ref-50)** ["38.17: Muscle Contraction and Locomotion - ATP and Muscle Contraction"](https://bio.libretexts.org/Bookshelves/Introductory_and_General_Biology/Book%3A_General_Biology_(Boundless)/38%3A_The_Musculoskeletal_System/38.17%3A_Muscle_Contraction_and_Locomotion_-_ATP_and_Muscle_Contraction). *Biology LibreTexts*. 2018-07-16. Retrieved 2024-05-01.

1. **[^](#cite_ref-51)** Hyman, Anthony A.; Krishnan, Yamuna; Alberti, Simon; Wang, Jie; Saha, Shambaditya; Malinovska, Liliana; Patel, Avinash (2017-05-19). "ATP as a biological hydrotrope". *Science*. **356** (6339): 753–756. [Bibcode](/source/Bibcode_(identifier)):[2017Sci...356..753P](https://ui.adsabs.harvard.edu/abs/2017Sci...356..753P). [doi](/source/Doi_(identifier)):[10.1126/science.aaf6846](https://doi.org/10.1126%2Fscience.aaf6846). [ISSN](/source/ISSN_(identifier)) [0036-8075](https://search.worldcat.org/issn/0036-8075). [PMID](/source/PMID_(identifier)) [28522535](https://pubmed.ncbi.nlm.nih.gov/28522535). [S2CID](/source/S2CID_(identifier)) [24622983](https://api.semanticscholar.org/CorpusID:24622983).

1. **[^](#cite_ref-52)** Savitski, Mikhail M.; Bantscheff, Marcus; Huber, Wolfgang; Dominic Helm; Günthner, Ina; Werner, Thilo; Kurzawa, Nils; Sridharan, Sindhuja (2019-03-11). ["Proteome-wide solubility and thermal stability profiling reveals distinct regulatory roles for ATP"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6411743). *Nature Communications*. **10** (1): 1155. [Bibcode](/source/Bibcode_(identifier)):[2019NatCo..10.1155S](https://ui.adsabs.harvard.edu/abs/2019NatCo..10.1155S). [doi](/source/Doi_(identifier)):[10.1038/s41467-019-09107-y](https://doi.org/10.1038%2Fs41467-019-09107-y). [ISSN](/source/ISSN_(identifier)) [2041-1723](https://search.worldcat.org/issn/2041-1723). [PMC](/source/PMC_(identifier)) [6411743](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6411743). [PMID](/source/PMID_(identifier)) [30858367](https://pubmed.ncbi.nlm.nih.gov/30858367).

1. **[^](#cite_ref-53)** Whicher, Alexandra; Camprubi, Eloi; Pinna, Silvana; Herschy, Barry; Lane, Nick (2018-06-01). ["Acetyl Phosphate as a Primordial Energy Currency at the Origin of Life"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6061221). *Origins of Life and Evolution of Biospheres*. **48** (2): 159–179. [Bibcode](/source/Bibcode_(identifier)):[2018OLEB...48..159W](https://ui.adsabs.harvard.edu/abs/2018OLEB...48..159W). [doi](/source/Doi_(identifier)):[10.1007/s11084-018-9555-8](https://doi.org/10.1007%2Fs11084-018-9555-8). [ISSN](/source/ISSN_(identifier)) [1573-0875](https://search.worldcat.org/issn/1573-0875). [PMC](/source/PMC_(identifier)) [6061221](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6061221). [PMID](/source/PMID_(identifier)) [29502283](https://pubmed.ncbi.nlm.nih.gov/29502283).

1. **[^](#cite_ref-54)** ["Ancient chemistry may explain why living things use ATP as the universal energy currency: An early step in metabolic evolution set the stage for emergence of ATP as the universal energy carrier"](https://www.sciencedaily.com/releases/2022/10/221004151228.htm). *ScienceDaily*. Retrieved 2023-08-27.

1. **[^](#cite_ref-Resetar_55-0)** Resetar, A. M.; Chalovich, J. M. (1995). "Adenosine 5′-(gamma-thiotriphosphate): an ATP analog that should be used with caution in muscle contraction studies". *Biochemistry*. **34** (49): 16039–16045. [doi](/source/Doi_(identifier)):[10.1021/bi00049a018](https://doi.org/10.1021%2Fbi00049a018). [PMID](/source/PMID_(identifier)) [8519760](https://pubmed.ncbi.nlm.nih.gov/8519760).

1. **[^](#cite_ref-56)** Pelleg, Amir; Kutalek, Steven P.; Flammang, Daniel; Benditt, David (February 2012). ["ATPace: injectable adenosine 5′-triphosphate"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3265710). *Purinergic Signalling*. **8** (Suppl 1): 57–60. [doi](/source/Doi_(identifier)):[10.1007/s11302-011-9268-1](https://doi.org/10.1007%2Fs11302-011-9268-1). [ISSN](/source/ISSN_(identifier)) [1573-9538](https://search.worldcat.org/issn/1573-9538). [PMC](/source/PMC_(identifier)) [3265710](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3265710). [PMID](/source/PMID_(identifier)) [22057692](https://pubmed.ncbi.nlm.nih.gov/22057692).

1. **[^](#cite_ref-57)** Lohmann, K. (August 1929). "Über die Pyrophosphatfraktion im Muskel" [On the pyrophosphate fraction in muscle]. *Naturwissenschaften* (in German). **17** (31): 624–625. [Bibcode](/source/Bibcode_(identifier)):[1929NW.....17..624.](https://ui.adsabs.harvard.edu/abs/1929NW.....17..624.). [doi](/source/Doi_(identifier)):[10.1007/BF01506215](https://doi.org/10.1007%2FBF01506215). [S2CID](/source/S2CID_(identifier)) [20328411](https://api.semanticscholar.org/CorpusID:20328411).

1. **[^](#cite_ref-58)** Vaughan, Martha; Hill, Robert L.; Simoni, Robert D. (2002). ["The Determination of Phosphorus and the Discovery of Phosphocreatine and ATP: the Work of Fiske and SubbaRow"](http://www.jbc.org/content/277/32/e21). *Journal of Biological Chemistry*. **277** (32): e21. [PMID](/source/PMID_(identifier)) [12161449](https://pubmed.ncbi.nlm.nih.gov/12161449). [Archived](https://web.archive.org/web/20170808062708/http://www.jbc.org/content/277/32/e21) from the original on 2017-08-08. Retrieved 2017-10-24.

1. **[^](#cite_ref-59)** Maruyama, K. (March 1991). "The discovery of adenosine triphosphate and the establishment of its structure". *J. Hist. Biol*. **24** (1): 145–154. [doi](/source/Doi_(identifier)):[10.1007/BF00130477](https://doi.org/10.1007%2FBF00130477). [S2CID](/source/S2CID_(identifier)) [87425890](https://api.semanticscholar.org/CorpusID:87425890).

1. **[^](#cite_ref-60)** Lipmann, F. (1941). "Metabolic generation and utilization of phosphate bond energy". *Adv. Enzymol*. **1**: 99–162. [ISSN](/source/ISSN_(identifier)) [0196-7398](https://search.worldcat.org/issn/0196-7398).

1. **[^](#cite_ref-61)** ["History: ATP first discovered in 1929"](http://nobelprize.org/nobel_prizes/chemistry/laureates/1997/illpres/history.html). *The Nobel Prize in Chemistry 1997*. [Nobel Foundation](/source/Nobel_Foundation). [Archived](https://web.archive.org/web/20100123061355/http://nobelprize.org/nobel_prizes/chemistry/laureates/1997/illpres/history.html) from the original on 2010-01-23. Retrieved 2010-05-26.

1. **[^](#cite_ref-62)** ["The Nobel Prize in Chemistry 1997"](https://www.nobelprize.org/nobel_prizes/chemistry/laureates/1997/). *Nobel Prize*. [Archived](https://web.archive.org/web/20171024205633/https://www.nobelprize.org/nobel_prizes/chemistry/laureates/1997/) from the original on 24 October 2017. Retrieved 21 January 2018.

## External links

Wikimedia Commons has media related to [Adenosine triphosphate](https://commons.wikimedia.org/wiki/Category:Adenosine_triphosphate).

- [ATP bound to proteins](http://www.ebi.ac.uk/pdbe-srv/PDBeXplore/ligand/?ligand=ATP) in the [PDB](/source/Protein_Data_Bank)

- [ScienceAid: Energy ATP and Exercise](https://web.archive.org/web/20160310134410/http://www.scienceaid.co.uk/biology/biochemistry/atp.html)

- [PubChem entry for Adenosine Triphosphate](https://pubchem.ncbi.nlm.nih.gov/compound/5957)

- [KEGG entry for Adenosine Triphosphate](http://www.genome.jp/dbget-bin/www_bget?cpd:C00002)

- [ATP 3D model](https://www.molecules3d.com/?model=ATP)

v t e Nucleic acid constituents Nucleobase Purine Adenine Guanine Hypoxanthine Xanthine Purine analogue Pyrimidine Uracil Thymine Cytosine Pyrimidine analogue Unnatural base pair (UBP) Nucleoside Ribonucleoside Adenosine Guanosine 5-Methyluridine Uridine 5-Methylcytidine Cytidine Pseudouridine Inosine N6-Methyladenosine Xanthosine Wybutosine Deoxyribonucleoside Deoxyadenosine Deoxyguanosine Thymidine Deoxyuridine Deoxycytidine Deoxyinosine Deoxyxanthosine Nucleotide (Nucleoside monophosphate) Ribonucleotide AMP GMP m5UMP UMP CMP IMP XMP Deoxyribonucleotide dAMP dGMP dTMP dUMP dCMP dIMP dXMP Cyclic nucleotide cAMP cGMP c-di-GMP c-di-AMP cADPR cGAMP Nucleoside diphosphate ADP GDP m5UDP UDP CDP Xanthosine diphosphate dADP dGDP dTDP dUDP dCDP Nucleoside triphosphate ATP GTP m5UTP UTP CTP ITP XTP dATP dGTP dTTP dUTP dCTP dITP dXTP

v t e Enzyme cofactors Active forms vitamins TPP / ThDP (B1) FMN, FAD (B2) NAD+, NADH, NADP+, NADPH (B3) Coenzyme A (B5) PLP / P5P (B6) Biotin (B7) THFA / H4FA, DHFA / H2FA, MTHF (B9) AdoCbl, MeCbl (B12) Ascorbic acid (C) Phylloquinone (K1), Menaquinone (K2) Coenzyme F420 non-vitamins ATP CTP SAMe PAPS GSH Coenzyme B Cofactor F430 Coenzyme M Coenzyme Q Heme / Haem (A, B, C, O) Lipoic Acid Methanofuran Molybdopterin Mycofactocin PQQ THB / BH4 THMPT / H4MPT metal ions Ca2+ Cu2+ Fe2+, Fe3+ Mg2+ Mn2+ Mo Ni2+ Zn2+ Base forms vitamins: see vitamins

v t e Neurotransmitters Amino acid-derived Major excitatory / inhibitory systems Glutamate system Agmatine Aspartic acid (aspartate) Glutamic acid (glutamate) Glutathione Glycine GSNO GSSG Kynurenic acid NAA NAAG Proline Serine GABA system GABA GABOB GHB Glycine system α-Alanine β-Alanine Glycine Hypotaurine Proline Sarcosine Serine Taurine GHB system GHB T-HCA (GHC) Biogenic amines Monoamines 6-OHM Dopamine Epinephrine (adrenaline) NAS (normelatonin) Norepinephrine (noradrenaline) Serotonin (5-HT) Trace amines 3-Iodothyronamine N-Methylphenethylamine N-Methyltryptamine m-Octopamine p-Octopamine Phenylethanolamine Phenethylamine Synephrine Tryptamine m-Tyramine p-Tyramine Others Histamine Neuropeptides See here instead. Lipid-derived Endocannabinoids 2-AG 2-AGE (noladin ether) 2-ALPI 2-OG AA-5-HT Anandamide (AEA) DEA LPI NADA NAGly OEA Oleamide PEA RVD-Hpα SEA Virodhamine (O-AEA) Neurosteroids See here instead. Nucleobase-derived Nucleosides Adenosine system ADP AMP ATP Vitamin-derived Miscellaneous Cholinergic system Acetylcholine Gasotransmitters Carbon monoxide (CO) Hydrogen sulfide (H2S) Nitric oxide (NO) Candidates Acetaldehyde Ammonia (NH3) Carbonyl sulfide (COS) Nitrous oxide (N2O) Sulfur dioxide (SO2)

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Formaldehyde HGH controversies Lead poisoning Melamine Mercury in fish Sudan I Food additives Flavorings Monosodium glutamate (MSG) Salt Sugar High-fructose corn syrup Vegetable oil controversy Intestinal parasites, parasitic disease Amoebiasis Anisakiasis Cryptosporidiosis Cyclosporiasis Diphyllobothriasis Enterobiasis Fasciolopsiasis Fasciolosis Giardiasis Gnathostomiasis Paragonimiasis Toxocariasis Toxoplasmosis Trichinosis Trichuriasis Microorganisms Botulism Campylobacter jejuni Clostridium perfringens Cronobacter Enterovirus Escherichia coli O104:H4 Escherichia coli O157:H7 Hepatitis A Hepatitis E Listeria Norovirus Rotavirus Salmonella Shigatoxigenic and verotoxigenic E. coli Vibrio cholerae Pesticides Chlorpyrifos DDT Lindane Malathion Methamidophos Preservatives Benzoic acid Ethylenediaminetetraacetic acid (EDTA) Sodium benzoate Sugar substitutes Acesulfame potassium Aspartame controversy Saccharin Sodium cyclamate Sorbitol Sucralose Toxins, poisons, environment pollution 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v t e Metabolism, catabolism, anabolism General Metabolic pathway Metabolic network Primary nutritional groups Energy metabolism Aerobic respiration Glycolysis → Pyruvate decarboxylation → Citric acid cycle → Oxidative phosphorylation (electron transport chain + ATP synthase) Anaerobic respiration Electron acceptors other than oxygen Fermentation Glycolysis → Substrate-level phosphorylation ABE Ethanol Lactic acid Specific paths Protein metabolism Protein synthesis Catabolism (protein→peptide→amino acid) Amino acid Amino acid synthesis Amino acid degradation (amino acid→pyruvate, acetyl CoA, or TCA intermediate) Urea cycle Nucleotide metabolism Purine metabolism Nucleotide salvage Pyrimidine metabolism Purine nucleotide cycle Carbohydrate metabolism (carbohydrate catabolism and anabolism) Human Glycolysis ⇄ Gluconeogenesis Glycogenolysis ⇄ Glycogenesis Pentose phosphate pathway Fructolysis Polyol pathway Galactolysis Leloir pathway Glycosylation N-linked O-linked Nonhuman Photosynthesis Anoxygenic photosynthesis Chemosynthesis Carbon fixation DeLey-Doudoroff pathway Entner-Doudoroff pathway Radiosynthesis Xylose metabolism Lipid metabolism (lipolysis, lipogenesis) Fatty acid metabolism Fatty acid degradation (Beta oxidation) Fatty acid synthesis Other Steroid metabolism Sphingolipid metabolism Eicosanoid metabolism Ketosis Reverse cholesterol transport Other Metal metabolism Iron metabolism Ethanol metabolism Phospagen system (ATP-PCr) Chlororespiration

v t e Metabolism map Carbon fixation Photo- respiration Pentose phosphate pathway Citric acid cycle Glyoxylate cycle Urea cycle Fatty acid synthesis Fatty acid elongation Beta oxidation Peroxisomal beta oxidation Glyco- genolysis Glyco- genesis Glyco- lysis Gluconeo- genesis Pyruvate decarb- oxylation Fermentation Keto- lysis Keto- genesis feeders to gluconeo- genesis Direct / C4 / CAM carbon intake Light reaction Oxidative phosphorylation Amino acid deamination Citrate shuttle Lipogenesis Lipolysis Steroidogenesis MVA pathway MEP pathway Shikimate pathway Transcription & replication Translation Proteolysis Glycosyl- ation Sugar acids Double/multiple sugars & glycans Simple sugars Inositol-P Amino sugars & sialic acids Nucleotide sugars Hexose-P Triose-P Glycerol P-glycerates Pentose-P Tetrose-P Propionyl -CoA Succinate Acetyl -CoA Pentose-P P-glycerates Glyoxylate Photosystems Pyruvate Lactate Acetyl -CoA Citrate Oxalo- acetate Malate Succinyl -CoA α-Keto- glutarate Ketone bodies Respiratory chain Serine group Alanine Branched-chain amino acids Aspartate group Homoserine group & lysine Glutamate group & proline Arginine Creatine & polyamines Ketogenic & glucogenic amino acids Amino acids Shikimate Aromatic amino acids & histidine Ascorbate (vitamin C) δ-ALA Bile pigments Hemes Cobalamins (vitamin B12) Various vitamin Bs Calciferols (vitamin D) Retinoids (vitamin A) Quinones (vitamin K) & tocopherols (vitamin E) Cofactors Vitamins & minerals Antioxidants PRPP Nucleotides Nucleic acids Proteins Glycoproteins & proteoglycans Chlorophylls MEP MVA Acetyl -CoA Polyketides Terpenoid backbones Terpenoids & carotenoids (vitamin A) Cholesterol Bile acids Glycero- phospholipids Glycerolipids Acyl-CoA Fatty acids Glyco- sphingolipids Sphingolipids Waxes Polyunsaturated fatty acids Neurotransmitters & thyroid hormones Steroids Endo- cannabinoids Eicosanoids Major metabolic pathways in metro-style map. Click any text (name of pathway or metabolites) to link to the corresponding article. Single lines: pathways common to most lifeforms. Double lines: pathways not in humans (occurs in e.g. plants, fungi, prokaryotes). Orange nodes: carbohydrate metabolism. Violet nodes: photosynthesis. Red nodes: cellular respiration. Pink nodes: cell signaling. Blue nodes: amino acid metabolism. Grey nodes: vitamin and cofactor metabolism. Brown nodes: nucleotide and protein metabolism. Green nodes: lipid metabolism.

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Adapted from the Wikipedia article [Adenosine triphosphate](https://en.wikipedia.org/wiki/Adenosine_triphosphate) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Adenosine_triphosphate?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.