58-64-0

Basic information

• Product Name: ADP
• Synonyms: adenosine,5’-(trihydrogenpyrophosphate);adenosine5’-(trihydrogendiphosphate);adenosine5’-pyrophosphate;adenosine5’-pyrophosphoricacid;adenosinediphosphoricacid;adenosinepyrophosphate;adp(nucleotide);5'-ADP
• CAS NO: 58-64-0
• Molecular Formula: C10H15N5O10P2
• Molecular Weight: 427.2
• EINECS: 200-392-5
• Product Categories: Pharmaceutical Intermediates;Nucleic acids;Inhibitors
• Mol File: 58-64-0.mol
• Article Data: 114

Chemical Properties

• Boiling Point: 196°C
• Flash Point: 484.6°C
• Appearance: /
• Density: 2.49g/cm³
• Storage Temp.: −20°C
• Solubility: DMSO (Slightly, Heated), Methanol (Slightly), Water (Slightly)
• PKA: pK2: 4.2(-1);pK3: 7.20(-2) (25°C)
• Merck: 13,155
• BRN: 67722
• CAS DataBase Reference: ADP(CAS DataBase Reference)
• NIST Chemistry Reference: ADP(58-64-0)
• EPA Substance Registry System: ADP(58-64-0)

Safety Data

• Safety Statements: 24/25
• WGK Germany: 3
• RTECS: AU7467000
• F: 10-21
• Hazardous Substances Data: 58-64-0(Hazardous Substances Data)

Usage

Uses

Different sources of media describe the Uses of 58-64-0 differently. You can refer to the following data:
1. Adenosine-5'-diphosphate (ADP) is a central component of energy storage, metabolism, and signal transduction in vivo. It serves as a precursor for ATP and, in this capacity, is utilized in a wide number of cellular processes, including respiration, biosynthetic reactions, motility, and cell division.
2. Adenosine 5′-diphosphate (5′-ADP or ADP) was used as a test compound for studying the endothelium-dependent vascular response in salt sensitive (DS) and salt resistant Dahl rats (DR). The product was used to study the different P2-purinergic receptor subtypes on canine vascular smooth muscle and endothelium.

Definition

ChEBI: A purine ribonucleoside 5'-diphosphate having adenine as the nucleobase.

Agricultural Uses

Adenosine diphosphate (ADP) is a phosphorus compound formed during the breakdown of adenosine triphosphate (ATP) by dephosphorylation. It is made of adenine, ribose, five carbon sugars and two phosphate groups. ADP acts as a source of energy in biochemical reactions.

Biological Activity

adenosine-5'-diphosphate is an agonist of purinergic receptors.purinergic receptors, also known as purinoceptors, are a family of plasma membrane molecules that are found in almost all mammalian tissues. within the field of purinergic signalling, these receptors have been implicated in learning and memory, locomotor and feeding behavior, and sleep. more specifically, purinergic receptors are involved in several cellular functions, such as proliferation and migration of neural stem cells, vascular reactivity, apoptosis and cytokine secretion.

Biochem/physiol Actions

Adenosine 5′-diphosphate induces human platelet aggregation and non-competitively blocks the stimulated human platelet adenylate cyclase.

in vitro

adenosine 5'-diphosphate (adp) is an adenine nucleotide having two phosphate groups esterified to the sugar moiety at the 5’ position. adp is formed through dephosphorylation of adenosine 5’-triphosphate (atp) by atpases and can be converted back to atp by atp synthases. adp can also be metabolized to adenosine 5’-monophosphate (amp) and 2’-deoxyadenosine 5’-diphosphate (dadp). adp can modulate several receptors, such as activating certain purinergic receptors and inhibiting others, inhibiting rat ecto-5’nucleotidase (ki = 0.91 nm), as well as regulating the phosphorylation status of amp-activated protein kinase [1, 2].

Enzyme inhibitor

This adenine nucleotide (FWfree-acid = 504.16 g/mol; CAS 58-64-0; Molar Absorptivity = 15,400 M–1cm–1, l = 259 nm) is a product in ATPdependent transphosphorylases, phosphohydrolases, and molecular motors; as such, ADP often inhibits these enzymes. Enzymatic Phosphorylation: ADP is a substrate for adenylate kinase (Reaction: ADP2– + MeADP " MeATP2– + AMP) and other enzymes that stabilize ATP concentrations in prokaryotes [e.g., acetate kinase (Reaction: MgADP + Acetyl-phosphate ! MeATP2– + Acetate)] and eukaryotes [e.g., pyruvate kinase (Reaction: MgADP + Phosphoenolpyruvate ! MgATP2– + Pyruvate), creatine kinase (Reaction: MgADP + Creatine-phosphate ! MgATP2– + Creatine), arginine kinase (Reaction: MgADP + Arginine-phosphate ! MgATP2– + Arginine), and nuclecleotide diphosphate kinase (Reaction: ADP2– + MgGTP2– " MgATP2– + GDP2–)]. ATP Synthase: ADP is a primary substrate for the FOF1 ATP synthase (Reaction: MgADP + Pi + High Chemiosmotic Gradient Energization State ! MgATP2– + Low Chemiosmotic Gradient Energization State). ADP can also become entrapped within a catalytic site of the rotary motor, when proton motive is low, absent, or uncoupled, and its inhibitory action under such conditions is believed to prevent wasteful hydrolysis of ATP (Reaction: MgATP2– + H2O ? MgADP + Pi). Metal Ion Binding Properties: As a polyanion, ADP not only binds physiologic divalent cations Mg2+ and Ca2+, but also forms reversible complexes with Mn2+ and Co2+. For reversible complexation of ADP2– with a metal ion Me2+, (Reaction: ADP2– + Me2+ ! MeADP), Kformation = [MeADP]/[ADP2–]free[Me2+]free, indicating that [MeADP]/[ADP2– ]free = Kformation ′ [Me2+]free. In many cases, metal-free ADP is not a substrate and instead acts as a revesible inhibitor. Good experimental design therefore demands rigorous control of free metal ion concentration to control the ratio of metal-bound and metal-free forms. When exposed to Cr(III) at elevated temperature, ADP also forms ligand exchange-inert complexes with Cr3+. Platelet Aggregation: ADP is also a well-known activator of platelet aggregation, as mediated by the ADP receptors P2Y1, P2Y12 and P2X1. Upon conversion to adenosine by ecto-ADPases, platelet activation is inhibited by means of adenosine receptors. Target(s): Hydrogenomonas facilis ribulosediphosphate (RuDP) carboxylase and NADH-, ATP-dependent CO2 fixation; platelet (Na+/K+)-ATPase; hydrogen-ion transport in chloroplasts; pyruvate dehydrogenase kinase; 5-oxo-L-prolinase, or L-pyroglutamate hydrolase; a-NADHdependent reductase, rat liver microsomes; nitrogenase; Trypanosoma cruzi hexokinase; maize leaf acetyl-coenzyme A carboxylase; rat brain mitochondrial calcium-efflux; sarcoplasmic reticulum Ca2+ ATPase; Na+-Na+ exchange mediated by (Na+/K+)ATPase reconstituted into liposomes; nitrate and nitrite assimilation in Zea mays under dark conditions; PGE1-activated platelet adenylate cyclase in rats and rabbits; mitochondrial F1-ATPase, inactive complex formed upon binding ADP at a catalytic site; ATP-sensitive K+ channels, frog skeletal muscle; human 5-phosphoribosyl-1pyrophosphate synthetase; Crithidia fasciculata glutathionylspermidine synthetase; myosin V ATPase; cystic fibrosis transmembrane conductance regulator (ABC transporter) via its adenylate kinase activity; V type ATPase/synthase.

IC 50

67 nm for p2x2/3

Purification Methods

It is characterised by conversion to the acridine salt by addition of alcoholic acridine (1.1g in 50mL), filtering off the yellow salt and recrystallising from H2O. The salt has m 215o(dec), max 259nm ( 15,400) in 2O. [Baddiley & Todd J Chem Soc 648 1947, 582 1949, cf LePage Biochemical Preparations 1 1 1949, Martell & Schwarzenbach Helv Chim Acta 39 653 1956]. [Beilstein 26 III/IV 2369.]

references

1. azran, s.,frster, d.,danino, o., et al. highly efficient biocompatible neuroprotectants with dual activity as antioxidants and p2y receptor agonists. j. med. chem. 56(12), 4938-4952 (2013).2. jarvis, m.f.,bianchi, b.,uchic, j.t., et al. [3h]a-317491, a novel high-affinity non-nucleotide antagonist that specifically labels human p2x2/3 and p2x3 receptors. journal of pharmacology and experimental therapeutics 310(1), 407-416 (2004).

Upstream product

• 606-67-7 disodium adenosine-5' triphosphate 
• 7732-18-5 water 
• 1062-98-2 adenosine 5'-tetraphosphate 
• 58-85-5 biotin 
• 85-32-5 Guanosine 5'-monophosphate 
• 56-65-5 ATP 
• 506-68-3 bromocyane 
• 59286-20-3 Adenosine 5'<(S)α-thio>diphosphate 
• 5959-90-0 Diadenosine triphosphate 
• 5542-28-9 Diadenosine tetraphosphate 
• 20816-58-4 adenosine 5'-phosphorimidazolide 
• 61-19-8 5'-adenosine monophosphate 
• 6154-31-0 AMP-Amidate 
• 19375-33-8 adenosine 5'-phosphorofluoride 

Downstream Products

• 86119-84-8 phosphoric acid 
• 86-04-4 diphosphoric acid mono-inosin-5'-yl ester 
• 1927-31-7 dATP 
• 56-65-5 ATP 
• 35094-46-3 adenosine-5'-O-(3-thiotriphosphate) 
• 61-19-8 5'-adenosine monophosphate 
• 820-11-1 3-phosphoglyceric acid 
• 127-17-3 2-oxo-propionic acid 
• 58-61-7 adenosine 
• 58430-79-8 C₁₆H₂₀N₆O₉P₂ 
• 2140-58-1 adenosine-5'-(α-D-glucopyranosyl)diphosphate 
• 50-99-7 D-glucose 
• 86-01-1 Guanosine 5'-triphosphate 
• 14265-44-2 Phosphate 

Relevant articles and documents

Thermodynamic analysis of F1-ATPase rotary catalysis using high-speed imaging

F1-ATPase (F1) is a rotary motor protein fueled by ATP hydrolysis. Although the mechanism for coupling rotation and catalysis has been well studied, the molecular details of individual reaction steps remain elusive. In this study, we performed high-speed imaging of F1 rotation at various temperatures using the total internal reflection dark-field (TIRDF) illumination system, which allows resolution of the F1 catalytic reaction into elementary reaction steps with a high temporal resolution of 72 μs. At a high concentration of ATP, F1 rotation comprised distinct 80° and 40° substeps. The 80° substep, which exhibited significant temperature dependence, is triggered by the temperature-sensitive reaction, whereas the 40° substep is triggered by ATP hydrolysis and the release of inorganic phosphate (Pi). Then, we conducted Arrhenius analysis of the reaction rates to obtain the thermodynamic parameters for individual reaction steps, that is, ATP binding, ATP hydrolysis, Pi release, and TS reaction. Although all reaction steps exhibited similar activation free energy values, ΔG? = 53-56 kJ mol-1, the contributions of the enthalpy (ΔH?), and entropy (ΔS?) terms were significantly different; the reaction steps that induce tight subunit packing, for example, ATP binding and TS reaction, showed high positive values of both ΔH? and ΔS?. The results may reflect modulation of the excluded volume as a function of subunit packing tightness at individual reaction steps, leading to a gain or loss in water entropy.

Kinetic mechanism and rate-limiting steps of focal adhesion kinase-1

Steady-state kinetic analysis of focal adhesion kinase-1 (FAK1) was performed using radiometric measurement of phosphorylation of a synthetic peptide substrate (Ac-RRRRRRSETDDYAEIID-NH2, FAK-tide) which corresponds to the sequence of an autophosphorylation site in FAK1. Initial velocity studies were consistent with a sequential kinetic mechanism, for which apparent kinetic values kcat (0.052 ± 0.001 s-1), KMgATP (1.2 ± 0.1 μM), KiMgATP (1.3 ± 0.2 μM), KFAK-tide (5.6 ± 0.4 μM), and K iFAK-tide (6.1 ± 1.1 μM) were obtained. Product and dead-end inhibition data indicated that enzymatic phosphorylation of FAK-tide by FAK1 was best described by a random bi bi kinetic mechanism, for which both E-MgADP-FAK-tide and E-MgATP-P-FAK-tide dead-end complexes form. FAK1 catalyzed the βγ-bridge:β-nonbridge positional oxygen exchange of [γ-18O4]ATP in the presence of 1 mM [γ- 18O4]ATP and 1.5 mM FAK-tide with a progressive time course which was commensurate with catalysis, resulting in a rate of exchange to catalysis of kx/kcat = 0.14 ± 0.01. These results indicate that phosphoryl transfer is reversible and that a slow kinetic step follows formation of the E-MgADP-P-FAK-tide complex. Further kinetic studies performed in the presence of the microscopic viscosogen sucrose revealed that solvent viscosity had no effect on kcat/KFAK-tide, while kcat and kcat/KMgATP were both decreased linearly at increasing solvent viscosity. Crystallographic characterization of inactive versus AMP-PNP-liganded structures of FAK1 showed that a large conformational motion of the activation loop upon ATP binding may be an essential step during catalysis and would explain the viscosity effect observed on kcat/Km for MgATP but not on kcat/K m for FAK-tide. From the positional isotope exchange, viscosity, and structural data it may be concluded that enzyme turnover (kcat) is rate-limited by both reversible phosphoryl group transfer (kforward ≈ 0.2 s-1 and kreverse ≈ 0.04 s-1) and a slow step (kconf ≈ 0.1 s-1) which is probably the opening of the activation loop after phosphoryl group transfer but preceding product release.

The ATPase activities of sulfonylurea receptor 2A and sulfonylurea receptor 2B are influenced by the C-terminal 42 amino acids

Unusually among ATP-binding cassette proteins, the sulfonylurea receptor (SUR) acts as a channel regulator. ATP-sensitive potassium channels are octameric complexes composed of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Two different genes encode SUR1 (ABCC8) and SUR2 (ABCC9), with the latter being differentially spliced to give SUR2A and SUR2B, which differ only in their C-terminal 42 amino acids. ATP-sensitive potassium channels containing these different SUR2 isoforms are differentially modulated by MgATP, with Kir6.2/SUR2B being activated more than Kir6.2/SUR2A. We show here that purified SUR2B has a lower ATPase activity and a 10-fold lower K m for MgATP than SUR2A. Similarly, the isolated nucleotide-binding domain (NBD) 2 of SUR2B was less active than that of SUR2A. We further found that the NBDs of SUR2B interact, and that the activity of full-length SUR cannot be predicted from that of either the isolated NBDs or NBD mixtures. Notably, deletion of the last 42 amino acids from NBD2 of SUR2 resulted in ATPase activity resembling that of NBD2 of SUR2A rather than that of NBD2 of SUR2B: this might indicate that these amino acids are responsible for the lower ATPase activity of SUR2B and the isolated NBD2 of SUR2B. We suggest that the lower ATPase activity of SUR2B may result in enhanced duration of the MgADP-bound state, leading to channel activation.

A zinc(II)-based receptor for ATP binding and hydrolysis

A protonated Zn(II) complex with a terpyridine-containing pentaamine macrocycle catalyses ATP hydrolysis in the presence of a second metal ion, which acts as cofactor assisting the phosphoryl transfer from ATP to an amine group of the receptor. The Royal Society of Chemistry 2005.

Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase: Product inhibition, cooperativity, and magnesium activation

In many photosynthetic organisms, tight-binding Rubisco inhibitors are released by the motor protein Rubisco activase (Rca). In higher plants, Rca plays a pivotal role in regulating CO2 fixation. Here, the ATPase activity of 0.005 mM tobacco Rca was monitored under steady-state conditions, and global curve fitting was utilized to extract kinetic constants. The kcat was best fit by 22.3 ± 4.9 min-1, the Km for ATP by 0.104 ± 0.024 mM, and the Ki for ADP by 0.037 ± 0.007 mM. Without ADP, the Hill coefficient for ATP hydrolysis was extracted to be 1.0 ± 0.1, indicating noncooperative behavior of homo-oligomeric Rca assemblies. However, the addition of ADP was shown to introduce positive cooperativity between two or more subunits (Hill coefficient 1.9 ± 0.2), allowing for regulation via the prevailing ATP/ADP ratio. ADP-mediated activation was not observed, although larger amounts led to competitive product inhibition of hydrolytic activity. The catalytic efficiency increased 8.4-fold upon cooperative binding of a second magnesium ion (Hill coefficient 2.5 ± 0.5), suggesting at least three conformational states (ATP-bound, ADP-bound, and empty) within assemblies containing an average of about six subunits. The addition of excess Rubisco (24:1, L8S8/Rca6) and crowding agents did not modify catalytic rates. However, high magnesium provided for thermal Rca stabilization. We propose that magnesium mediates the formation of closed hexameric toroids capable of high turnover rates and amenable to allosteric regulation. We suggest that in vivo, the Rca hydrolytic activity is tuned by fluctuating [Mg2+] in response to changes in available light.

Lipopolysaccharide biosynthesis without the lipids: Recognition promiscuity of Escherichia coli heptosyltransferase i

Heptosyltransferase I (HepI) is responsible for the transfer of l-glycero-d-manno-heptose to a 3-deoxy-α-d-oct-2-ulopyranosonic acid (Kdo) of the growing core region of lipopolysaccharide (LPS). The catalytic efficiency of HepI with the fully deacylated analogue of Escherichia coli HepI LipidA is 12-fold greater than with the fully acylated substrate, with a k cat/Km of 2.7 × 106 M-1 s -1, compared to a value of 2.2 × 105 M-1 s-1 for the Kdo2-LipidA substrate. Not only is this is the first demonstration that an LPS biosynthetic enzyme is catalytically enhanced by the absence of lipids, this result has significant implications for downstream enzymes that are now thought to utilize deacylated substrates.

Purification and characterization of mouse mevalonate pyrophosphate decarboxylase

Mevalonate pyrophosphate decarboxylase (MPD) in mouse liver was purified by affinity chromatography. The purified enzyme was a homodimer of 46-kDa subunits and had an isoelectric point of 5.0. Kinetic analysis revealed an apparent Km value of 10 μM for mevalonate pyrophosphate. The enzyme required ATP as a phosphate acceptor and Mg as a divalent cation, which could be substituted with Mn or Co. Its optimum pH was 4.0-7.0. A comparison with MPD from various other sources revealed the mouse MPD to have essentially the same properties as rat MPD, expect for the optimum pH range. An excess of rabbit anti-rat MPD antibody deleted approximately 80% of the MPD activity in the crude extract of mouse liver. These results suggested that the homodimer of 46-kDa subunits represents the major active form of MPD in mice.

Structural and enzymatic characterization of the choline kinase LicA from Streptococcus pneumoniae

LicA plays a key role in the cell-wall phosphorylcholine biosynthesis of Streptococcus pneumonia. Here we determined the crystal structures of apo-form LicA at 1.94 ? and two complex forms LicA-choline and LicA-AMP-MES, at 2.01 and 1.45 ? resolution, respectively. The overall structure adopts a canonical protein kinase-like fold, with the active site located in the crevice of the N- and C- terminal domains. The three structures present distinct poses of the active site, which undergoes an open-closed-open conformational change upon substrate binding and product release. The structure analyses combined with mutageneses and enzymatic assays enabled us to figure out the key residues for the choline kinase activity of LicA. In addition, structural comparison revealed the loop between helices α7 and α8 might modulate the substrate specificity and catalytic activity. These findings shed light on the structure and mechanism of the prokaryotic choline kinase LicA, and might direct the rational design of novel anti-pneumococcal drugs.

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Molecular cloning of groESL locus, and purification and characterization of chaperonins, GroEL and GroES, from Bacillus brevis.

The groESL locus of a protein-hypersecreting bacterium, Bacillus brevis, was cloned by PCR using primers designed based on the DNA sequence of a B. subtilis homolog. GroEL protein was purified to apparent homogeneity and its ATPase activity was characterized: it hydrolyzed ATP, CTP, and TTP in this order of reaction rate, and its specific activity for ATP was 0.1 micromole/min/mg protein. Purified GroEL forms a tetradecamer. GroEL was estimated to contain 22% alpha-helix, 24% beta-sheet, and 19% turn structures, by CD measurement. GroES protein was also highly purified to examine its chaperonin activity. GroEL protected from thermal inactivation of and showed refolding-promoting activity for malate dehydrogenase, strictly depending on the presence of ATP and GroES.

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ATP cleavage by cone tetraguanidinocalix[4]arene

The upper rim cone tetraguanidinocalix[4]arene 1 is a highly effective catalyst of ATP hydrolysis. The catalytically most active species is the triprotonated form of the catalyst. The three protonated guanidinium groups provide the electrostatic driving force for substrate binding and activation, while the neutral guanidine most likely acts as a nucleophilic catalyst.

Bacillus subtilis DEAD protein YdbR possesses ATPase, RNA binding, and RNA unwinding activities

The product of an open reading frame (ORF) (called YdbR) identified while analyzing the Bacillus subtilis genome has been classified as an Asp-Glu-Ala-Asp (DEAD) protein, but the biological function and enzymology of YdbR have not been characterized in detail. Here we show that recombinant YdbR-His6 purified from Escherichia coli is an ATP-independent RNA binding protein. It also possesses RNA-dependent ATPase activity stimulated not only by total RNA from B. subtilis but also by an RNA that is irrelevant to that of B. subtilis. Functional analysis indicated that the growth rate of a ΔydbR mutant strain of B. subtilis was reduced as compared with that of the wild type not only at 37°C, but more severely at 22°C.

Compound and preparation method thereof, and preparation method of nucleoside oligophosphate

The invention relates to the technical field of nucleotide synthesis, in particular to a compound and a preparation method thereof, and a preparation method of nucleoside oligophosphate. The preparation method of the compound comprises the following steps: putting a nucleoside phosphate raw material, imidazole and an activating agent into a first solvent for a first reaction. According to the invention, the water-soluble raw material and the activating agent are subjected to a reaction to prepare the compound, and the compound can be used as a raw material for synthesizing nucleoside oligophosphate, so that rapid and stable synthesis of nucleoside oligophosphate is facilitated. The phosphate raw material and the compound prepared in the invention are subjected to a second reaction in a second solvent, and then desalination is performed to prepare nucleoside oligophosphate; compared with the prior art, triethylamine conversion does not need to be carried out on the nucleoside phosphate raw material, the utilization rate of the nucleoside phosphate raw material is increased, and the reaction period is shortened.

Class III Polyphosphate Kinase 2 Enzymes Catalyze the Pyrophosphorylation of Adenosine-5′-Monophosphate

Polyphosphate kinase 2 (PPK2) transfer phosphate from inorganic polyphosphate to nucleotides. According to their activity, PPK2 enzymes are classified into three groups. Among them, class III enzymes catalyze both the phosphorylation of nucleotide mono- to diphosphates and di- to triphosphates by using polyphosphate, which is a very inexpensive substrate. Therefore, class III enzymes are very attractive for use in biotechnological applications. Despite several studies on class III enzymes, a detailed mechanism of how phosphate is transferred from the polyphosphate to the nucleotide remains to be elucidated. Herein, it is reported that PPK2 class III enzymes from two different bacterial species catalyze the phosphorylation of adenosine mono- (AMP) into triphosphate (ATP) not only through step-by-step phosphorylation, but also by pyrophosphorylation. These are the first PPK2 enzymes that have been shown to possess polyphosphate-dependent pyrophosphorylation activity.