56-65-5

Basic information

• Product Name: Adenosine triphosphate
• Synonyms: ADENOSINE-5?TRIPHOSPHORIC ACID (ATP) pure;Adenosine 5'-triphosphate;Adenosine 5'-(tetrahydrogen triphosphate);Adenosine triphosphate;Adenosine-5'-triphosphoric acid;ATP;5'-ATP;Adenylpyrophosphoric acid;Adenphos;Adetol;Atipi;Atriphos;Striadyne;Striphos;Triadenyl;Triphosaden ;Adenphos;Striphos;ADENOSINE TRIPHOSPHATE, DISODIUM SALT (ATP);5'-Adenyldiphosphoric acid;Adenosine-5;[[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxyphosphonic acid
• CAS NO: 56-65-5
• Molecular Formula: C₁₀H₁₆N₅O₁₃P₃
• Molecular Weight: 507.18
• EINECS: 200-283-2
• Product Categories: Pharmaceutical Intermediates;Nucleic acids
• Mol File: 56-65-5.mol
• Article Data: 68

Chemical Properties

• Melting Point: 144°C (rough estimate)
• Boiling Point: 951.429 °C at 760 mmHg
• Flash Point: 529.205 °C
• Appearance: /lyophilized powder
• Density: 1.0 g/mL at 20 °C
• Storage Temp.: −20°C
• PKA: pK2: 4.00(-1);pK3: 6.48(-2) (25°C)
• CAS DataBase Reference: Adenosine triphosphate(CAS DataBase Reference)
• NIST Chemistry Reference: Adenosine triphosphate(56-65-5)
• EPA Substance Registry System: Adenosine triphosphate(56-65-5)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• Hazardous Substances Data: 56-65-5(Hazardous Substances Data)

Usage

Description

Adenosine triphosphate, also known as ATP, is a molecule that carries energy within cells. It is one of the most important biological compounds because of its role in supplying energy for life. ATP is the universal energy carrier used by all organisms to supply energy for biological functions. It is often referred to as the energy currency of cells.ATP also functions as a neurotransmitter that is stored and secreted with other neurotransmitters from the pancreas. ATP is a nucleotide consisting of the nucleoside adenosine with three attached phosphate groups (see Adenine). Like other nucleotides, ATP consists of three parts: a sugar, an amine base, and a phosphate group. The central part of the molecule in ATP is the sugar ribose. The amine base adenine is attached to the ribose, forming adenosine. Opposite the adenine on the ribose is attached a chain of three phosphate groups.

Chemical Properties

The structure of Adenosine triphosphate has an ordered carbon compound as a backbone, but the part that is really critical is the phosphorous part - the triphosphate. Three phosphorous groups are connected by oxygens to each other, and there are also side oxygens connected to the phosphorous atoms. Under the normal conditions in the body, each of these oxygens has a negative charge, and therefore repel each other. These bunched up negative charges want to escape - to get away from each other, so there is a lot of potential energy here.If you remove just one of these phosphate groups from the end, so that there are just two phosphate groups, the molecule is much happier. This conversion from ATP to ADP is an extremely crucial reaction for the supplying of energy for life processes. Just the cutting of one bond with the accompanying rearrangement is sufficient to liberate about 7.3 kilocalories per mole = 30.6 kJ/mol. This is about the same as the energy in a single peanut.hyperphysics.phy-astr.gsu.edu

Originator

Atepodin ,Medix ,Spain

History

ATP was first isolated by the German chemist Karl Lohmann (1898–1978) from muscle tissue extracts in 1929. Alexander Todd’s (1907–1997) research helped to clarify ATP’s structure, and it was first synthesized by Todd in 1948.

Uses

Adenosine triphosphate (ATP) plays a critical role in the transport of macromolecules such as proteins and lipids into and out of the cell.? The hydrolysis of ATP provides the required energy for active transport mechanisms to carry such molecules across a concentration gradient.

Synthesis

ATP is synthesized in organisms by several related mechanisms. Oxidative phosphorylation is the main process that aerobic organisms use to produce ATP. Oxidative phosphorylation produces ATP from ADP and inorganic phosphate (Pi) from the oxidation of nicotinamide adenine dinucleotide (NADH) by molecular oxygen in the cell’s mitochondria. Glycolysis is another process that generates ATP. Glycolysis converts glucose into pyruvate and in the process also forms NADH and ATP. The process can be represented as: Glucose + 2ADP + 2NAD+ + 2Pi → 2 pyruvate + 2ATP + 2NADH + 2H+. In this reaction Pi represents free inorganic phosphate. The rate of glycolysis in the body is inversely related to the amount of available ATP. Pyruvate produced by glycolysis can enter the Krebs cycle, producing more ATP.

Definition

Adenosine triphosphate (ATP) is the source of energy for use and storage at the cellular level.?It is an adenosine 5'-phosphate in which the 5'-phosphate is a triphosphate group. It is involved in the transportation of chemical energy during metabolic pathways.

Manufacturing Process

With a solution of 0.29 part by weight of well dried 1,3- dicyclohexylguanidinium adenosine 5'-phosphoramidate in 5 parts by volume of ortho-chlorophenol is admixed a solution of 0.95 part by weight of bistriethylammonium pyrophosphate in a mixed solvent composed of 1 part by volume of ortho-chlorophenol and 2 parts by volume of acetonitrile. The mixture is left standing at 20°C for 2 days. Then 30 parts by volume of water is added to the mixture. After washing with three 15 parts by weight volumeportions of diethyl ether, the aqueous layer is separated, and the remaining diethyl ether in the aqueous layer is removed under reduced pressure. Five parts by weight of activated charcoal is added to the aqueous layer and the mixture is stirred for 30 minutes. The activated charcoal is filtered and further 1 part by weight of activated charcoal is added to the filtrate. After 20 minutes agitation, the activated charcoal is taken out by filtration. The combined activated charcoal is washed with a little water, and eluted twice with respective 300 and 200 parts by volume-portions of 50% (volume) ethanol containing 2% (volume) of concentrated aqueous ammonia. The eluate is concentrated to 40 parts by volume, then is passed through a column packed with 20 parts by volume of a strongly basic anion exchange resin in bead form (chloric type) (polystyrene trimethylbenzyl ammonium type resin sold under the name of Dowex-1 from Dow Chemical Company, Mich. USA). Then, the column is washed with 750 parts by volume of an acid aqueous saline solution containing 0.01 normal hydrochloric acid and 0.02 normal sodium chloride and then eluted with 600 parts by volume of an acid aqueous saline solution composed of 0.01 normal hydrochloric acid and 0.2 normal sodium chloride. After neutralizing with a diluted sodium hydroxide solution, the eluate is treated with activated charcoal to adsorb ATP as its sodium salt. The separated activated charcoal is washed with water and eluted with 60% (volume) ethanol containing 2% (volume) of concentrated aqueous ammonia. The eluate is concentrated to 0.5 part by volume, then 5 parts by volume of ethanol is added. The precipitate thus deposited is centrifuged and dried at low temperature to obtain 0.155 part by weight of tetra-sodium salt of ATP containing 4 mols of water of crystallization as a colorless crystalline powder. The yield is 47% relative to the theoretical.

Therapeutic Function

Coenzyme, Vasodilator

Agricultural Uses

Adenosine triphosphate (ATP) is a nucleotide of fundamental importance as a carrier of chemical energy in all living organisms. The most important function of phosphorus in a plant system is to store and transfer energy. During biochemical processes, ATP gets synthesized to store releasable energy with the breakdown of ATP to adenosine triphosphate (ADP) and to phosphate ion by dephosphorylation. Here, ADP and ATP act as energy currency within the plant.

Safety Profile

Poison by intraperitoneal route.Human mutation data reported. When heated todecomposition it emits toxic fumes of POx and NOx.

Purification Methods

ATP is purified by precipitating it as the barium salt on adding excess barium acetate solution to a 5% solution of ATP in water. The precipitate is filtered off, washed with distilled water, dissolved in 0.2M HNO3 and again precipitated with barium acetate. The precipitate, after several washings with distilled water, is redissolved in 0.2M HNO3, and slightly more than an equivalent of 0.2M H2SO4 is added to precipitate all the barium as BaSO4 which is filtered off. The ATP is then precipitated by addition of a large excess of 95% ethanol. It is filtered off, washed several times with 100% EtOH and finally with dry diethyl ether. It is dried in vacuo. [Kashiwagi & Rabinovitch J Phys Chem 59 498 1955, Beilstein 26 III/IV 3654.]

Synthetic route

adenosine 5'-diphosphate (58-64-0) → adenosine-5'-O-(3-thiotriphosphate) (35094-46-3) + ATP (56-65-5) + phosphate

Conditions	Yield
With dihydroxyacetone phosphate; ethylenediaminetetraacetic acid; DL-dithiothreitol; NAD; trisodium thiophosphate; 2-oxo-propionic acid; magnesium chloride; phosphoglycerate kinase; immobil. triosephosphate isomerase; glyceraldehyde-3-phosphate dehydrogenase; lactate dehydrogenase In water for 72h; Ambient temperature; 1) pH 7.5;	A 80% B n/a C n/a

5'-tosyladenosine (5135-30-8) → ATP (56-65-5)

Conditions	Yield
With tetrakis(tetra-n-butylammonium) hydrogen triphosphate In acetonitrile for 48h; Ambient temperature;	72%

5'-adenosine monophosphate (61-19-8) → adenosine 5'-diphosphate (58-64-0) + ATP (56-65-5) + adenosine 5'-tetraphosphate (1062-98-2)

Conditions	Yield
With manganese(ll) chloride; tri-1-benzimidazolylphosphine oxide at 50℃; for 72h; N-ethylmorpholine buffer (pH 7.0);	A 65% B 17% C 3%
With magnesium chloride; tri-1-benzimidazolylphosphine oxide at 50℃; for 72h; N-ethylmorpholine buffer (pH 7.0);	A 26% B 36% C 18%

adenosine 5'-<α-thio>triphosphate (29220-54-0) → ATP (56-65-5)

Conditions	Yield
With dihydrogen peroxide	65%

tetrakis(tetra-n-butylammonium) hydrogen triphosphate (93978-77-9) + 5'-tosyladenosine (5135-30-8) → ATP (56-65-5)

Conditions	Yield
In acetonitrile for 23h;	55%

5'-adenosine monophosphate (61-19-8) → adenosine 5'-diphosphate (58-64-0) + ATP (56-65-5)

Conditions	Yield
With phosphorotriimidazolide; magnesium chloride at 22℃; for 168h; N-ethylmorpholine buffer (pH 7.0);	A 25% B 43%
With 2,3,6-trimethyl-beta-cyclodextrin In water at 37℃; Product distribution; equilibrium constant phosphate buffer, pH 7.00;
With magnesium; β‐cyclodextrin In water at 37℃; Product distribution; equilibrium constant phosphate buffer, pH 7.00;

Morpholin-4-yl-phosphonic acid mono-{(3aR,4R,6R,6aR)-2-methoxy-6-[6-(4-methoxy-phenylamino)-purin-9-yl]-tetrahydro-furo[3,4-d][1,3]dioxol-4-ylmethyl} ester → ATP (56-65-5)

Conditions	Yield
With bis(tri-n-butylammonium) pyrophosphate In N,N-dimethyl-formamide	42%

fructose-1,6-bisphosphate (488-69-7) + 5'-adenosine monophosphate (61-19-8) → ATP (56-65-5)

Conditions	Yield
With yeast-maceration juice

Phosphocreatine (67-07-2) + 5'-adenosine monophosphate (61-19-8) → ATP (56-65-5)

Conditions	Yield
With creatine-kinase beim Behandeln mit einem Enzym-Praeparat aus Escherichia coli;

5'-adenosine monophosphate (61-19-8) → ATP (56-65-5)

Conditions	Yield
With Tri-n-octylamine; phosphoric acid; cyclopentanone-[O-(4-nitro-benzenesulfonyl)-oxime ]; N,N-dimethyl-formamide
With pyridine; phosphoric acid; water; dicyclohexyl-carbodiimide Reagens 4: Tributylamin;
With 5-phosphoribosyl 1-pyrophosphate synthetase; 5-phosphoribosyl 1-pyrophosphate Enzyme kinetics;

adenosine (58-61-7) → 5'-adenosine monophosphate (61-19-8) + ATP (56-65-5)

Conditions	Yield
With phosphoric acid; brewer's yeast-substance; water
With D-glucose; phosphoric acid; brewer's yeast-substance; water
With fructose-1,6-bisphosphate; phosphoric acid; brewer's yeast-substance; water

adenosine 5'-triphosphate γ(1-[2-nitrophenyl]ethyl) ester (67030-27-7) → ortho-nitroso acetophenone (25798-61-2) + ATP (56-65-5)

Conditions	Yield
With N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid; potassium chloride; magnesium chloride at 21℃; Mechanism; Quantum yield; Rate constant; Irradiation; pH 7.1;
With brucine buffer In water at 10℃; Product distribution; Irradiation; other reagent;

phosphocreatine (4087-38-1) → ATP (56-65-5)

Conditions	Yield
With creatine kinease Rate constant;

Adenosine 5'<(S)α-thio>triphosphate (58976-48-0) → ATP (56-65-5)

Conditions	Yield
With bromine In water for 0.0666667h; Ambient temperature;

5'-adenosine monophosphate (61-19-8) → 5'-inosine monophosphate (131-99-7) + adenosine 5'-diphosphate (58-64-0) + ATP (56-65-5)

Conditions	Yield
With zinc(II) chloride In methanol at 25℃; Product distribution; biosynthesis; various typ-, and conc. of reagent;
In methanol at 25℃; biosynthesis by Candida boidnii No. 2201; pH = 6.5;	A 14.8 mmol B 36.8 mmol C 24.0 mmol
With zinc(II) chloride In methanol at 25℃; biosynthesis by Candida boidnii No. 2201; pH = 6.5;	A 2.0 mmol B n/a C 36.8 mmol
In methanol at 25℃; biosynthesis by Candida boidnii No. 2201; pH = 6.5;	A 14.8 mmol B 1.1 mmol C 24.0 mmol

ethyl ester of adenosine 5'-triiphospho-(Pγ-> N)-alanine (113693-26-8) → L-Alanine ethyl ester (3082-75-5) + ATP (56-65-5)

Conditions	Yield
With hydrogenchloride at 37℃; for 1h; Product distribution;

adenosine 5'-diphosphate (58-64-0) → 5'-adenosine monophosphate (61-19-8) + ATP (56-65-5)

Conditions	Yield
With heptakis(2,6-di-O-methyl)cyclomaltoheptaose; magnesium chloride In water at 37℃; Product distribution; equilibrium constant phosphate buffer, pH 7.00, ATP formation in presence and absence of DM-β-CD;
With magnesium; β‐cyclodextrin In water at 37℃; Product distribution; equilibrium constant phosphate buffer, pH 7.00;
With 2,3,6-trimethyl-beta-cyclodextrin In water at 37℃; Product distribution; equilibrium constant phosphate buffer, pH 7.00;
With adenylate kinase; magnesium sulfate In water at 36.9℃; Rate constant;
With tobacco chloroplast adenylate kinase; magnesium sulfate Enzyme kinetics; transphosphorylation;

adenosine 5'-diphosphate (58-64-0) → ATP (56-65-5)

Conditions	Yield
With acetylphosphoric acid; magnesium(II); 1,13-Dioxa-4,7,10,16,19,22-hexaazacyclotetracosane In water at 40℃; Product distribution; Mechanism; also in the absence of metal cation; other solvents;
With acetic acid phosphoric acid-anhydride; iron(III) sulfate at 30℃; var. metal salts;
With aminacrine; phosphoric acid; N-tris(hydroxymethyl) methylglycine; chloroplasts from spinach; potassium chloride; 1,1'-dibenzyl-4,4'-bipyridinium; phenazine methosulfate; magnesium chloride; ascorbic acid at 20℃; for 0.0166667h; Kinetics; Mechanism; Irradiation; var. of H+ conc.;

C19H19ClN6O10P2 (170638-51-4) → ATP (56-65-5)

Conditions	Yield
With phosphoric acid; copper dichloride for 24h; Ambient temperature; Yield given;

C18H23N6O15P3 → ortho-nitroso acetophenone (25798-61-2) + ATP (56-65-5)

Conditions	Yield
With potassium hydroxide; N-(2-acetamido)-3-iminodiacetic acid at 22℃; Rate constant; Irradiation;

adenosine (58-61-7) → ATP (56-65-5)

Conditions	Yield
With human deoxycytidine kinase; ATP; magnesium chloride In water at 37℃; pH=7.5; Enzyme kinetics; phosphorylation;
Multistep reaction;

C20H26N6*C10H16N5O13P3 → ATP (56-65-5) + 2,5,8,11-tetraaza<12>-<12>(2,9)<1,10>-phenanthrolinophane (221350-58-9)

Conditions	Yield
With tetramethlyammonium chloride In water at 24.95℃; pH=2.5 - 11; Equilibrium constant; decomplexation;

C23H32N6*C10H16N5O13P3 → ATP (56-65-5) + 2,6,10,14-tetraaza[15](2,9)cyclo(1,10)phenanthrolinophane (246247-12-1)

Conditions	Yield
With tetramethlyammonium chloride In water at 24.95℃; pH=2.5 - 11; Equilibrium constant; decomplexation;

C48H72N4O4(4+)*C10H16N5O13P3*4Cl(1-) → 5,11,17,23-tetramethoxy-25,26,27,28-tetrakis(trimethylammoniomethyl)calix<4>arene tetrachloride (139934-97-7) + ATP (56-65-5)

Conditions	Yield
In water-d2 at 24.85℃; Equilibrium constant; Thermodynamic data; decomplexation;

C56H88N4O4(4+)*C10H16N5O13P3*4Cl(1-) → 5,11,17,23-tetrakis(trimethylammoniomethyl)-25,26,27,28-tetrapropoxycalix<4>arene tetrachloride + ATP (56-65-5)

Conditions	Yield
In water-d2 at 24.85℃; Equilibrium constant; Thermodynamic data; decomplexation;

C72H108N6O6(6+)*C10H16N5O13P3*6Cl(1-) → 5,11,17,23,29,35-hexakis-37,38,39,40,41,42-hexamethoxycalix<6>arene + ATP (56-65-5)

Conditions	Yield
In water-d2 at 24.85℃; Equilibrium constant; Thermodynamic data; decomplexation;

C96H144N8O8(8+)*C10H16N5O13P3*8Cl(1-) → ATP (56-65-5) + 49,50,51,52,53,54,55,56-octamethoxy-5,11,17,23,29,35,41,47-octakis(trimethylammoniomethyl)calix[8]arene octachloride

Conditions	Yield
In water-d2 at 24.85℃; Equilibrium constant; Thermodynamic data; decomplexation;

dibenzyl phosphochloridate (538-37-4) + disilver-salt of/the/ <5'>adenylic acid → ATP (56-65-5)

Conditions	Yield
With acetonitrile; phenol beim anschliessenden Hydrieren an Palladium in wss. Dioxan;

adenosine 5'-diphosphate (58-64-0) + polymer metaphosphate + poly phosphate-kinase → ATP (56-65-5)

Conditions	Yield
reversible Phosphorylierung;

L-methionine (63-68-3) + ATP (56-65-5) → (S)-(S)-adenosyl-L-methionine

Conditions	Yield
With Tris-HCl buffer; ethylenediaminetetraacetic acid; Escherichia coli S-adenosyl-L-methionine synthetase; potassium chloride; 2-hydroxyethanethiol; magnesium chloride In water for 5h; Ambient temperature;	100%

ATP (56-65-5) → adenosine 5'-diphosphate (58-64-0)

Conditions	Yield
With Dehydracetic acid; immobilized Glycerokinase for 2h; Ambient temperature;	98%
With hydrogenchloride
With manganese(II) sulfate; phosphoric acid

ATP (56-65-5) → Diadenosine tetraphosphate (5542-28-9)

Conditions	Yield
With LEUCINE In various solvent(s) at 40℃; at pH 7.5; ATP-regenerating system of acetate kinase, adenylate kinase, PPase with acetyl phosphate;	98%
With LEUCINE In various solvent(s) at 40℃; Product distribution; effect of different di- and tri-charged cations on Ap4A synthesis;
With L-lysine; lysyl tRNA synthetase (LysU); TRIS buffer pH 8; potassium chloride; magnesium chloride; zinc(II) chloride at 37℃; Rate constant; various temp, pH, various metal chloride;
Multi-step reaction with 2 steps 1: ZnCl2, MgCl2, KCl, TRIS buffer pH 8 / 2.5 h / 37 °C / lysyl tRNA synthetase (LysU), inorganic pyrophosphatase 2: ZnCl2, MgCl2, KCl, TRIS buffer pH 8, L-lysine / 37 °C / lysyl tRNA synthetase (LisU), inorganic pyrophosphatase View Scheme

1-(2'-deoxy-2'-fluoro-β-D-arabinofuranosyl)nicotinamide-5'-phosphate (133473-75-3) + ATP (56-65-5) → 2'-deoxy-2'-fluoroarabino-NAD+ (133575-27-6)

Conditions	Yield
With pyrophosphatase; magnesium chloride In water at 37℃; for 1h; pH=Ca. 7.4; aq. phosphate buffer; Enzymatic reaction;	95%

[10a-13C1]riboflavin + ATP (56-65-5) → C26(13)CH33N9O15P2

Conditions	Yield
With rabbit muscle pyruvate kinase; baker's yeast inorganic pyrophosphatase; Corynebacterium ammoniagenes recombinant flavokinase/FAD synthetase In aq. buffer at 37℃; for 12h; pH=8; Enzymatic reaction;	95%

β-2'-deoxy-2'-fluororibonicotinamide mononucleotide (1173700-41-8) + ATP (56-65-5) → 2'-deoxy-2'-fluororibo-NAD+ (159993-17-6)

Conditions	Yield
With pyrophosphatase; magnesium chloride In water at 37℃; for 1h; pH=Ca. 7.4; aq. phosphate buffer; Enzymatic reaction;	94%

β-2'-deoxy-2',2'-difluororibonicotinamide mononucleotide (1173700-38-3) + ATP (56-65-5) → 2'-deoxy-2',2'-difluoro-NAD+ (1260238-56-9)

Conditions	Yield
With pyrophosphatase; magnesium chloride In water at 37℃; for 1h; pH=Ca. 7.4; aq. phosphate buffer; Enzymatic reaction;	90%
With magnesium chloride; pyrophosphatase; yeast nicotinamide mononucleotide adenylyltransferase 1 at 37℃; for 1h; pH=~ 7.4; Aqueous phosphate buffer; Enzymatic reaction;

[8a-13C1]-6,7-dimethyl-8-ribityllumazine + 3,4-dihydroxy-2-butanone 4-phosphate (114155-98-5) + ATP (56-65-5) → C26(13)CH33N9O15P2

Conditions	Yield
With rabbit muscle pyruvate kinase; Bacillus subtilis recombinant lumazine synthase; Corynebacterium ammoniagenes recombinant flavokinase/FAD synthetase; Escherichia coli recombinant riboflavin synthase In aq. buffer at 37℃; for 12h; pH=7.6;	90%

ATP (56-65-5) → dATP (1927-31-7)

Conditions	Yield
With DL-dithiothreitol; L. leichmannii ribonucleosidetriphosphate reductase In various solvent(s) at 25℃; for 120h; Reduction; Enzymatic reaction;	89%
With ribonucleoside triphosphate reductase; 5'-deoxyadenosylcobalamine; NADPH at 37℃; Kinetics; Reduction;

L-2H3>methionine (13010-53-2) + ATP (56-65-5) → S-adenosyl-L-[methyl-2H3]methionine (68684-40-2)

Conditions	Yield
With pyrophosphatase; ethylenediaminetetraacetic acid; AdoMet synthetase lysate; tris hydrochloride; 2-hydroxyethanethiol at 25℃; pH=8.0;	87.9%
With SAM synthetase overexpressed by E. coli strain DM22-(pK8); magnesium chloride In acetonitrile at 20℃; for 5h; pH=8; Enzymatic reaction;

C12H17FO8 + ATP (56-65-5) → guanosine 5'-diphosphono-6-fluoro-β-L-fucopyranoside

Conditions	Yield
Stage #1: C12H17FO8 With sodium methylate In methanol at 20℃; for 2h; Stage #2: ATP With L-fucokinase/GDP-fucose pyrophosphorylase; magnesium chloride; manganese(ll) chloride at 37℃; pH=7.5; Enzymatic reaction;	87%

[methyl-13C]-L-methionine (49705-26-2) + ATP (56-65-5) → [S-13C-methyl]adenosyl-L-methionine

Conditions	Yield
With pyrophosphatase; ethylenediaminetetraacetic acid; AdoMet synthetase lysate; tris hydrochloride; 2-hydroxyethanethiol at 25℃; pH=8.0;	86%
With recombinant Methanococcus jannaschii AdoMet synthetase at 24.84℃; for 5h; Enzymatic reaction;
With methionine adenosyltransferase from Sulfolobus solfataricus In aq. phosphate buffer at 37℃; for 1h; pH=8; Enzymatic reaction;

ATP (56-65-5) → adenosine 5'-tetraphosphate (1062-98-2)

Conditions	Yield
With LEUCINE In various solvent(s) at 40℃; at pH 7.5; ATP-regenerating system of acetate kinase, adenylate kinase, PPase with acetyl phosphate;	84%
With pyrophosphatase; L-lysine; tripolyphosphate; potassium chloride; magnesium chloride In water at 37℃; for 2h; pH 8;	52%
Multi-step reaction with 2 steps 1: ZnCl2, MgCl2, KCl, TRIS buffer pH 8 / 2.5 h / 37 °C / lysyl tRNA synthetase (LysU), inorganic pyrophosphatase 2: 52 percent / sodium tripolyphosphate, ZnCl2 / 37 °C View Scheme

ATP (56-65-5) + adenosine 5'-tetraphosphate (1062-98-2) → p1,p5-di(adenosine 5'-)pentaphosphate (41708-91-2)

Conditions	Yield
With LEUCINE In various solvent(s) at 40℃; at pH 7.5; ATP-regenerating system of acetate kinase, adenylate kinase, PPase with acetyl phosphate;	80%

C27H45N10O15P3S + ATP (56-65-5) → C37H57N15O21P4S

Conditions	Yield
With L-lysine; tris hydrochloride; magnesium chloride; zinc(II) chloride at 37℃; for 0.666667h; pH=8; Enzymatic reaction;	80%

C26H43N10O16P3S + ATP (56-65-5) → C36H55N15O22P4S

Conditions	Yield
With L-lysine; tris hydrochloride; magnesium chloride; zinc(II) chloride at 37℃; for 0.666667h; pH=8; Enzymatic reaction;	80%

ATP (56-65-5) + (3S,4R,5R,6S)-3-fluoro-6-methyl-tetrahydro-2H-pyran-2,4,5-triyl triacetate (188783-78-0) → guanosine 5'-diphospho-2-deoxy-2-fluoro-β-L-fucopyranoside

Conditions	Yield
Stage #1: (3S,4R,5R,6S)-3-fluoro-6-methyl-tetrahydro-2H-pyran-2,4,5-triyl triacetate With sodium methylate In methanol at 20℃; for 2h; Stage #2: ATP With L-fucokinase/GDP-fucose pyrophosphorylase; magnesium chloride; manganese(ll) chloride at 37℃; pH=7.5; Enzymatic reaction;	80%

ATP (56-65-5) + α-D-glucopyranosyl-1-phosphate (59-56-3) → adenosine-5'-(α-D-glucopyranosyl)diphosphate (2140-58-1)

Conditions	Yield
With Glucose-1-phosphate thymidylyltransferase from Streptococcus pneumonia serotype 23F; magnesium chloride at 37℃; for 6h; Enzymatic reaction;	78%
With Tris-HCl buffer; A. thermoaerophilus DSM 10155 RmlA3 thymidylyltransferase; magnesium chloride; inorganic pyrophosphatase at 37℃; for 24h;

C19H28N2O6 + ATP (56-65-5) → C29H42N7O18P3

Conditions	Yield
With pantothenate kinase; dephosphocoenzyme A kinase; phosphopantetheine adenyltransferase; potassium chloride; magnesium chloride In aq. buffer pH=8; Enzymatic reaction;	77%

adenosine 5'-phosphorimidazolide (20816-58-4, 116273-87-1) + ATP (56-65-5) → Diadenosine tetraphosphate (5542-28-9)

Conditions	Yield
With H96F-Fhit; magnesium chloride In various solvent(s) at 20℃; for 1h; pH=5.5;	75%

23,24-Bisnorchola-1,4-dien-3-one-22-carboxylic acid (3614-61-7, 5327-60-6, 66512-12-7, 96686-97-4, 14508-05-5) + ATP (56-65-5) + coenzyme A (85-61-0) → 3-oxo-23,24-bisnorchol-4-en-22-oyl-coenzyme A (1380518-01-3) + 5'-adenosine monophosphate (61-19-8)

Conditions	Yield
With recombinant Rhodococcus jostii RHA1 CasI; magnesium chloride In ethanol at 22℃; for 7h; pH=7.5; aq. buffer; Enzymatic reaction;	A 75% B n/a

C12H15F3O8 + ATP (56-65-5) → GDP-6,6,6-trifluorofucose

Conditions	Yield
Stage #1: C12H15F3O8 With sodium methylate In methanol at 20℃; for 2h; Stage #2: ATP With L-fucokinase/GDP-fucose pyrophosphorylase; magnesium chloride; manganese(ll) chloride at 37℃; pH=7.5; Enzymatic reaction;	75%

ATP (56-65-5) + 5'-XTP (6253-56-1) → adenosine(xanthosine) 5',5'''-P1,P4-tetraphosphate

Conditions	Yield
With pyrophosphatase; L-lysine; potassium chloride; magnesium chloride In water at 37℃; for 2h; pH 8;	74%
With L-lysine; TRIS buffer pH 8; potassium chloride; magnesium chloride; zinc(II) chloride at 37℃; for 24h; lysyl tRNA synthetase (LisU), inorganic pyrophosphatase;	66%

ATP (56-65-5) → adenosine 5'-diphosphate (58-64-0) + PAPS (482-67-7)

Conditions	Yield
With phospho(enol)pyruvate; potassium chloride; sodium sulfate; magnesium chloride for 8h; Ambient temperature; tris-HCl buffer pH 8.0, ATP sulfurylase, APS kinase, pyruvate kinase, inorganic pyrophosphatase;	A n/a B 73%

dTTP (365-08-2, 92627-33-3, 106119-81-7) + ATP (56-65-5) → adenosine(2'-deoxythymidyne) 5',5'''-P1,P4-tetraphosphate

Conditions	Yield
With L-lysine; TRIS buffer pH 8; potassium chloride; magnesium chloride; zinc(II) chloride at 37℃; for 24h; lysyl tRNA synthetase (LisU), inorganic pyrophosphatase;	73%

C11H23N3O4 (943528-71-0) + ATP (56-65-5) → amino-coenzyme A (943528-72-1)

Conditions	Yield
With DPCK; PanK; PPAT; potassium chloride; magnesium chloride for 1.5h; pH=9; aq. Tris/HCl; Enzymatic reaction;	72%

C12H16F2O8 + ATP (56-65-5) → C16H23F2N5O15P2

Conditions	Yield
Stage #1: C12H16F2O8 With sodium methylate In methanol at 20℃; for 2h; Stage #2: ATP With L-fucokinase/GDP-fucose pyrophosphorylase; magnesium chloride; manganese(ll) chloride at 37℃; pH=7.5; Enzymatic reaction;	72%

Inosine 5'-triphosphate (132-06-9) + ATP (56-65-5) → adenosine(inosine) 5',5'''-P1,P4-tetraphosphate

Conditions	Yield
With pyrophosphatase; L-lysine; potassium chloride; magnesium chloride In water at 37℃; for 2h; pH 8;	70%

Upstream product

• 488-69-7 fructose-1,6-bisphosphate 
• 61-19-8 5'-adenosine monophosphate 
• 67-07-2 Phosphocreatine 
• 4087-38-1 phosphocreatine 
• 58-64-0 adenosine 5'-diphosphate 
• 138-08-9 phosphoenolpyruvic acid 
• 29886-19-9 2',3'-di-O-acetyladenosine 
• 58-61-7 L-adenosine 
• 58-64-0 adenosine 5'-diphosphate 
• 235764-37-1 β-L-adenosine 
• 146-91-8 guanosine-5'-diphosphate 
• 1069055-17-9 C₂₄H₃₁N₆O₁₅P₃ 
• 41708-91-2 p¹,p⁵-di(adenosine 5'-)pentaphosphate 
• 5542-28-9 Diadenosine tetraphosphate 

Downstream Products

• 58-98-0 UDP 
• 63-39-8 UTP 
• 58-64-0 adenosine 5'-diphosphate 
• 1927-31-7 dATP 
• 5959-90-0 Diadenosine triphosphate 
• 129785-74-6 (S)-2-[(S)-2-(2-{2-[(S)-2-Amino-3-(4-{[(2R,3S,4R,5R)-5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethoxy]-hydroxy-phosphoryloxy}-phenyl)-propionylamino]-acetylamino}-acetylamino)-3-phenyl-propionylamino]-4-methyl-pentanoic acid 
• 61-19-8 5'-adenosine monophosphate 
• 117137-55-0 Ap4(arabino-A) 
• 67030-27-7 adenosine 5'-triphosphate γ(1-[2-nitrophenyl]ethyl) ester 
• 5542-28-9 P¹,P⁴-di(adenosine-5′)tetraphosphate 
• 41708-91-2 p¹,p⁵-di(adenosine 5'-)pentaphosphate 
• 129785-78-0 C₅₉H₈₁N₁₈O₁₈P 
• 129785-77-9 C₆₀H₈₃N₁₈O₁₈P 

Relevant articles and documents

Analytical Techniques for the Determination of Chemical Exchange Rate Constants with Application to the Creatine Kinase Reaction

A method for determining biochemical exchange rates for analysis of inversion recovery experiments is described.As used in the current application, the technique involves fitting multiexponential equations to the magnetization recovery curves for PCr and ATP.From the parameters of the exponential fits expressions for the forward and reverse rate constants are derived.Results obtained with this technique were compared with inversion transfer and with previously published results using saturation transfer.The addition of a third exchanging species was also investigated and found to have no significant effect on the calculated values for the forward and reverse rate constants.In addition, the feasibility of using an abbreviated 6-point sampling strategy was evaluated; values for the rate constants were similar to those obtained using all 21 data points.The results of this study indicate that chemical exchange rate constants can be determined using inversion recovery techniques which avoid many of the difficulties associated with selective excitation methods.

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Formation of ATP by photochemical excitation of benzoquinones in dimethylacetamide solution

A new method of adenosine triphosphate production is described which involves photo-excitation of p-benzoquinones under the presence of adenosine diphosphate and inorganic phosphate in N,N-dimethylacetamide solution. A possible mechanism for the reaction is presented.

Physiological and biochemical characterization of three nucleoside diphosphate kinase isozymes from rice (Oryza sativa L.)

Nucleoside diphosphate kinase (NDPK) is a ubiquitous enzyme that catalyzes the transfer of the γ-phosphoryl group from a nucleoside triphosphate to a nucleoside diphosphate. In this study, we examined the subcellular localization, tissue-specific gene expression, and enzymatic characteristics of three rice NDPK isozymes (OsNDPK1-OsNDPK3). Sequence comparison of the three OsNDPKs suggested differential subcellular localization. Transient expression of green fluorescence protein-fused proteins in onion cells indicated that OsNDPK2 and OsNDPK3 are localized to plastid and mitochondria respectively, while OsNDPK1 is localized to the cytosol. Expression analysis indicated that all the OsNDPKs are expressed in the leaf, leaf sheath, and immature seeds, except for OsNDPK1, in the leaf sheath. Recombinant OsNDPK2 and OsNDPK3 showed lower optimum pH and higher stability under acidic pH than OsNDPK1. In ATP formation, all the OsNDPKs displayed lower Km values for the second substrate, ADP, than for the first substrate, NTP, and showed lowest and highest K m values for GTP and CTP respectively.

N-acetyl-homocysteinthiolacton as a means of an oxidative synthesis of adenosine diphosphate and adenosine triphosphate from adenosine monophosphate and orthophosphate

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Supramolecular catalysis of adenosine triphosphate synthesis in aqueous solution mediated by a macrocyclic polyamine and divalent metal cations

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Supramolecularly Assembled Nanocomposites as Biomimetic Chloroplasts for Enhancement of Photophosphorylation

Prototypes of natural biosystems provide opportunities for artificial biomimetic systems to break the limits of natural reactions and achieve output control. However, mimicking unique natural structures and ingenious functions remains a challenge. Now, multiple biochemical reactions were integrated into artificially designed compartments via molecular assembly. First, multicompartmental silica nanoparticles with hierarchical structures that mimic the chloroplasts were obtained by a templated synthesis. Then, photoacid generators and ATPase-liposomes were assembled inside and outside of silica compartments, respectively. Upon light illumination, protons produced by a photoacid generator in the confined space can drive the liposome-embedded enzyme ATPase towards ATP synthesis, which mimics the photophosphorylation process in vitro. The method enables fabrication of bioinspired nanoreactors for photobiocatalysis and provides insight for understanding sophisticated biochemical reactions.

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Fe(III)-ion-Catalysed Non-enzymatic Transformation of ADP into ATP

Non-enzymatic phosphorylation of ADP to ATP has been found to occur readily when Fe(III) ion is present in aqueous solutions of ADP and acetyl phosphate.As long as the reaction temperature is low enough (25 deg C or less), the phosphorylation of ADP to ATP proceeds to about 20percent conversion with 100percent selectivity.At higher temperatures, the yield decreases owing to the hydrolysis of acetyl phosphate.Among several phosphoryl donors studied, acetyl phosphate was found to be the best phosphorylating reagent.Creatine phosphate also produced ATP but the efficiency was very low.The phosphorylation of AMP was unsuccessful, even with acetyl phosphate.

Boric Acid-Fueled ATP Synthesis by FoF1 ATP Synthase Reconstituted in a Supramolecular Architecture

Significant strides toward producing biochemical fuels have been achieved by mimicking natural oxidative and photosynthetic phosphorylation. Here, different from these strategies, we explore boric acid as a fuel for tuneable synthesis of energy-storing molecules in a cell-like supramolecular architecture. Specifically, a proton locked in boric acid is released in a modulated fashion by the choice of polyols. As a consequence, controlled proton gradients across the lipid membrane are established to drive ATP synthase embedded in the biomimetic architecture, which facilitates tuneable ATP production. This strategy paves a unique route to achieve highly efficient bioenergy conversion, holding broad applications in synthesis and devices that require biochemical fuels.

The mechanism of ion translocation in mitochondria. 3. Coupling of K+ efflux with ATP synthesis.

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Stereospecificity, substrate, and inhibitory properties of nucleoside diphosphate analogs for creatine and pyruvate kinases

Antiviral α-P-borano substituted NTPs are promising chain terminators targeting HIV reverse transcriptase (RT). Activation of antiviral nucleoside diphosphates (NDPs) to NTPs may be carried out by pyruvate kinase (PK) and creatine kinase (CK). Herein, are presented the effects of nucleobase, ribose, and α-phosphate substitutions on substrate specificities of CK and PK. Both enzymes showed two binding modes and negative cooperativity with respect to substrate binding. The stereospecificity and inhibition of ADP phosphorylation by α-P-borano substituted NDP (NDPαB) stereoisomers were also investigated. The Sp-ADPαB isomer was a 70-fold better substrate for CK than the Rp isomer, whereas PK preferred the Rp isomer of NDPαBs. For CK, the Sp-ADPαB isomer was a competitive inhibitor; for PK, the Rp-ADPαB isomer was a poor competitive inhibitor and the Sp-ADPαB isomer was a poor non-competitive inhibitor. Taken together, these data suggest that, although the Rp-NDPαB isomer would be minimally phosphorylated by CK or PK, it should not inhibit either enzyme.

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ATP regeneration by a single polyphosphate kinase powers multigram-scale aldehyde synthesisin vitro

ATP recycling systems are required to avoid the addition of stoichiometric quantities of cofactor and facilitate industrial implementation of ATP-dependent enzymes. One factor that limits the biocatalytic application of these enzymes is the lack of a scalable AMP to ATP regeneration system. Whole-cells or a combination of purified enzymes are often exploited for ATP regeneration from AMP, whereas cell free systems comprising a single crude enzyme preparation would be preferred. To establish such a system, we focussed on polyphosphate kinases (PPKs) to find a single enzyme that could be used to power ATP-consuming reactions. Screening of some previously reported PPKs revealed limitations of these biocatalysts for scale-up purposes. As such, a panel of novel putative PPK2-III enzymes was constructed and compared to characterised enzymes belonging to the same class. Multidimensional small-scale screening revealed that PPK12 (from an unclassifiedErysipelotrichaceaebacterium) displays enhanced expression levels, ATP formation rates, polyphosphate tolerance and stability under a variety of harsh conditions. The carboxylic acid reductase (CAR) catalysed reduction of carboxylates to aldehydes was chosen as a model reaction to test the applicability of PPK12 as a bifunctional biocatalyst for ATP regeneration from AMP. The implementation of the identified ATP-recycling enzyme provided the first example of cell free multigram-scale aldehyde synthesis employing enzymes and a single PPK2-III, paving the way for affordable scalable ATP regeneration technologies.