5'-Adenylic acid, monoanhydride with sulfuric acid. The initial compound formed by the action of ATP sulfurylase on sulfate ions after sulfate uptake. Synonyms: adenosine sulfatophosphate; APS.
An enzyme that catalyzes the activation of sulfate ions by ATP to form adenosine-5'-phosphosulfate and pyrophosphate. This reaction constitutes the first enzymatic step in sulfate utilization following the uptake of sulfate. EC 2.7.7.4.
A nucleoside that is composed of ADENINE and D-RIBOSE. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter.
3'-Phosphoadenosine-5'-phosphosulfate. Key intermediate in the formation by living cells of sulfate esters of phenols, alcohols, steroids, sulfated polysaccharides, and simple esters, such as choline sulfate. It is formed from sulfate ion and ATP in a two-step process. This compound also is an important step in the process of sulfur fixation in plants and microorganisms.
A subclass of adenosine A2 receptors found in LEUKOCYTES, the SPLEEN, the THYMUS and a variety of other tissues. It is generally considered to be a receptor for ADENOSINE that couples to the GS, STIMULATORY G-PROTEIN.
A subtype of ADENOSINE RECEPTOR that is found expressed in a variety of tissues including the BRAIN and DORSAL HORN NEURONS. The receptor is generally considered to be coupled to the GI, INHIBITORY G-PROTEIN which causes down regulation of CYCLIC AMP.
An enzyme that catalyzes the hydrolysis of ADENOSINE to INOSINE with the elimination of AMMONIA.
A subtype of ADENOSINE RECEPTOR that is found expressed in a variety of locations including the BRAIN and endocrine tissues. The receptor is generally considered to be coupled to the GI, INHIBITORY G-PROTEIN which causes down regulation of CYCLIC AMP.
A subclass of adenosine A2 receptors found in the CECUM, the COLON, the BLADDER, and a variety of other tissues. It is generally considered to be a low affinity receptor for ADENOSINE that couples to the GS, STIMULATORY G-PROTEIN.
An enzyme that catalyzes the formation of ADP plus AMP from adenosine plus ATP. It can serve as a salvage mechanism for returning adenosine to nucleic acids. EC 2.7.1.20.
A subclass of ADENOSINE RECEPTORS that are generally considered to be coupled to the GS, STIMULATORY G-PROTEIN which causes up regulation of CYCLIC AMP.
Compounds that selectively bind to and activate ADENOSINE A2 RECEPTORS.

Reduction of adenosine-5'-phosphosulfate instead of 3'-phosphoadenosine-5'-phosphosulfate in cysteine biosynthesis by Rhizobium meliloti and other members of the family Rhizobiaceae. (1/37)

We have cloned and sequenced three genes from Rhizobium meliloti (Sinorhizobium meliloti) that are involved in sulfate activation for cysteine biosynthesis. Two of the genes display homology to the Escherichia coli cysDN genes, which code for an ATP sulfurylase (EC 2.7.7.4). The third gene has homology to the E. coli cysH gene, a 3'-phosphoadenosine-5'-phosphosulfate (PAPS) reductase (EC 1.8.99.4), but has greater homology to a set of genes found in Arabidopsis thaliana that encode an adenosine-5'-phosphosulfate (APS) reductase. In order to determine the specificity of the R. meliloti reductase, the R. meliloti cysH homolog was histidine tagged and purified, and its specificity was assayed in vitro. Like the A. thaliana reductases, the histidine-tagged R. meliloti cysH gene product appears to favor APS over PAPS as a substrate, with a Km for APS of 3 to 4 microM but a Km for PAPS of >100 microM. In order to determine whether this preference for APS is unique to R. meliloti among members of the family Rhizobiaceae or is more widespread, cell extracts from R. leguminosarum, Rhizobium sp. strain NGR234, Rhizobium fredii (Sinorhizobium fredii), and Agrobacterium tumefaciens were assayed for APS or PAPS reductase activity. Cell extracts from all four species also preferentially reduce APS over PAPS.  (+info)

Identification of a new class of 5'-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria. (2/37)

A gene was cloned from Burkholderia cepacia DBO1 that is homologous with Escherichia coli cysH encoding 3'-phosphoadenylylsulfate (PAPS) reductase. The B. cepacia gene is the most recent addition to a growing list of cysH homologs from a diverse group of sulfate-assimilating bacteria whose products show greater homology to plant 5'-adenylylsulfate (APS) reductase than they do to E. coli CysH. The evidence reported here shows that the cysH from one of the species, Pseudomonas aeruginosa, encodes APS reductase. It is able to complement an E. coli cysH mutant and a cysC mutant, indicating that the enzyme is able to bypass PAPS, synthesized by the cysC product. Insertional knockout mutation of P. aeruginosa cysH produced cysteine auxotrophy, indicating its role in sulfate assimilation. Purified P. aeruginosa CysH expressed as a His-tagged recombinant protein is able to reduce APS, but not PAPS. The enzyme has a specific activity of 5.8 micromol. min(-1). mg of protein(-1) at pH 8.5 and 30 degrees C with thioredoxin supplied as an electron donor. APS reductase activity was detected in several bacterial species from which the novel type of cysH has been cloned, indicating that this enzyme may be widespread. Although an APS reductase from dissimilatory sulfate-reducing bacteria is known, it shows no structural or sequence homology with the assimilatory-type APS reductase reported here. The results suggest that the dissimilatory and assimilatory APS reductases evolved convergently.  (+info)

Effects of AMP derivatives on cyclic AMP levels in NG108-15 cells. (3/37)

1. In NG108-15 neuroblastomaxglioma hybrid cells, ATP stimulates intracellular cyclic AMP formation, which is inhibited by both adenosine (P(1)) and P2 receptor antagonists. In the present study, we examined the effects of several AMP derivatives in NG108-15 cells and mouse neuroblastoma N18TG-2 cells. 2. Adenosine 2'-monophosphate (A2P), adenosine 3'-monophosphate (A3P) and adenosine 5'-phosphosulphate (A5PS) increased cyclic AMP levels with similar concentration-dependencies in NG108-15 cells. 3. Increases in cyclic AMP by AMP derivatives were inhibited by the P2 receptor antagonist PPADS, but not by suramin. Effects of AMP derivatives were also inhibited by P(1) receptor antagonists ZM241385, XAC, DPCPX and partially by alloxazine. The ecto-nucleotidase inhibitor alpha, beta-methyleneADP was without effect. 4. In contrast, AMP derivatives did not change cyclic AMP levels in N18TG-2 cells. Accumulation of cyclic AMP in N18TG-2 cells was stimulated by adenosine A(2) receptor agonists CGS21680 and NECA, but not by ATP or beta, gamma-methyleneATP, agonists for cyclic AMP production in NG108-15 cells. 5. Reverse transcription-coupled polymerase chain reaction (RT - PCR) analyses revealed that N18TG-2 cells express both A(2A) and A(2B) receptors, while NG108-15 cells express mainly A(2A) receptors. 6. AMP derivatives did not affect the P2X and P2Y receptors expressed in NG108-15 cells. 7. These results suggest that A2P, A3P and A5PS act as agonists for cyclic AMP production and that these compounds are valuable tools for determinating the mechanism of ATP-stimulated cyclic AMP response in NG108-15 cells.  (+info)

Sulfate assimilation in higher plants characterization of a stable intermediate in the adenosine 5'-phosphosulfate reductase reaction. (4/37)

The enzyme catalysing the reduction of adenosine 5'-phosphosulfate (AdoPS) to sulfite in higher plants, AdoPS reductase, is considered to be the key enzyme of assimilatory sulfate reduction. In order to address its reaction mechanism, the APR2 isoform of this enzyme from Arabidopsis thaliana was overexpressed in Escherichia coli and purified to homogeneity. Incubation of the enzyme with [35S]AdoPS at 4 degrees C resulted in radioactive labelling of the protein. Analysis of APR2 tryptic peptides revealed 35SO2-3 bound to Cys248, the only Cys conserved between AdoPS and prokaryotic phosphoadenosine 5'-phosphosulfate reductases. Consistent with this result, radioactivity could be released from the protein by incubation with thiols, inorganic sulfide and sulfite. The intermediate remained stable, however, after incubation with sulfate, oxidized glutathione or AdoPS. Because truncated APR2, missing the thioredoxin-like C-terminal part, could be labelled even at 37 degrees C, and because this intermediate was more stable than the complete protein, we conclude that the thioredoxin-like domain was required to release the bound SO2-3 from the intermediate. Taken together, these results demonstrate for the first time the binding of 35SO2-3 from [35S]AdoPS to AdoPS reductase and its subsequent release, and thus contribute to our understanding of the molecular mechanism of AdoPS reduction in plants.  (+info)

Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation. (5/37)

ATP sulfurylases (ATPSs) are ubiquitous enzymes that catalyse the primary step of intracellular sulfate activation: the reaction of inorganic sulfate with ATP to form adenosine-5'-phosphosulfate (APS) and pyrophosphate (PPi). With the crystal structure of ATPS from the yeast Saccharomyces cerevisiae, we have solved the first structure of a member of the ATP sulfurylase family. We have analysed the crystal structure of the native enzyme at 1.95 Angstroms resolution using multiple isomorphous replacement (MIR) and, subsequently, the ternary enzyme product complex with APS and PPi bound to the active site. The enzyme consists of six identical subunits arranged in two stacked rings in a D:3 symmetric assembly. Nucleotide binding causes significant conformational changes, which lead to a rigid body structural displacement of domains III and IV of the ATPS monomer. Despite having similar folds and active site design, examination of the active site of ATPS and comparison with known structures of related nucleotidylyl transferases reveal a novel ATP binding mode that is peculiar to ATP sulfurylases.  (+info)

Identification of yacE (coaE) as the structural gene for dephosphocoenzyme A kinase in Escherichia coli K-12. (6/37)

Dephosphocoenzyme A (dephospho-CoA) kinase catalyzes the final step in coenzyme A biosynthesis, the phosphorylation of the 3'-hydroxy group of the ribose sugar moiety. Wild-type dephospho-CoA kinase from Corynebacterium ammoniagenes was purified to homogeneity and subjected to N-terminal sequence analysis. A BLAST search identified a gene from Escherichia coli previously designated yacE encoding a highly homologous protein. Amplification of the gene and overexpression yielded recombinant dephospho-CoA kinase as a 22.6-kDa monomer. Enzyme assay and nuclear magnetic resonance analyses of the product demonstrated that the recombinant enzyme is indeed dephospho-CoA kinase. The activities with adenosine, AMP, and adenosine phosphosulfate were 4 to 8% of the activity with dephospho-CoA. Homologues of the E. coli dephospho-CoA kinase were identified in a diverse range of organisms.  (+info)

Assay of adenosine 3'-phosphate 5'-sulphatophosphate in hepatic tissues. (7/37)

A fluorimetric assay, based on the ability of boiled hepatic extracts to support the sulphO-conjugation of harmol, was used to demonstrate and quantify PAdoPS (adenosine 3'-phosphate 5'-sulphatophosphate) present in liver. A stoicheiometric relationship was established between the sulphate conjugate formed and the 'active sulphate' utilized. Guinea-pig, rat, mouse and rabbit livers contain 3.3, 2.9, 0.8 and 0.5 mumol of PAdoPS/100 G wet wt. respectively.  (+info)

The presence of an iron-sulfur cluster in adenosine 5'-phosphosulfate reductase separates organisms utilizing adenosine 5'-phosphosulfate and phosphoadenosine 5'-phosphosulfate for sulfate assimilation. (8/37)

It was generally accepted that plants, algae, and phototrophic bacteria use adenosine 5'-phosphosulfate (APS) for assimilatory sulfate reduction, whereas bacteria and fungi use phosphoadenosine 5'-phosphosulfate (PAPS). The corresponding enzymes, APS and PAPS reductase, share 25-30% identical amino acids. Phylogenetic analysis of APS and PAPS reductase amino acid sequences from different organisms, which were retrieved from the GenBank(TM), revealed two clusters. The first cluster comprised known PAPS reductases from enteric bacteria, cyanobacteria, and yeast. On the other hand, plant APS reductase sequences were clustered together with many bacterial ones, including those from Pseudomonas and Rhizobium. The gene for APS reductase cloned from the APS-reducing cyanobacterium Plectonema also clustered together with the plant sequences, confirming that the two classes of sequences represent PAPS and APS reductases, respectively. Compared with the PAPS reductase, all sequences of the APS reductase cluster contained two additional cysteine pairs homologous to the cysteine residues involved in binding an iron-sulfur cluster in plants. Mossbauer analysis revealed that the recombinant APS reductase from Pseudomonas aeruginosa contains a [4Fe-4S] cluster with the same characteristics as the plant enzyme. We conclude, therefore, that the presence of an iron-sulfur cluster determines the APS specificity of the sulfate-reducing enzymes and thus separates the APS- and PAPS-dependent assimilatory sulfate reduction pathways.  (+info)

Adenosine phosphosulfate (APS) is a biological compound that plays a crucial role in the sulfur metabolism of many organisms. It is an activated form of sulfate, which means it is ready to be used in various biochemical reactions. APS consists of adenosine monophosphate (AMP), a molecule related to adenosine triphosphate (ATP), linked to a sulfate group through a phosphate bridge.

In the human body, APS is primarily produced in the liver and is involved in the synthesis of the amino acids cysteine and methionine, which contain sulfur atoms. These amino acids are essential for various biological processes, including protein synthesis, antioxidant defense, and detoxification.

APS is also a key intermediate in the bacterial process of dissimilatory sulfate reduction, where sulfate is reduced to hydrogen sulfide (H2S) as a terminal electron acceptor during anaerobic respiration. This process is important for the global sulfur cycle and the ecology of anaerobic environments.

Sulfate adenylyltransferase is an enzyme involved in the metabolism of sulfur-containing compounds. It catalyzes the first step in the assimilatory sulfate reduction pathway, which is the conversion of sulfate (SO4^2-) to adenosine 5'-phosphosulfate (APS) by transferring an adenylyl group from ATP to sulfate.

The reaction catalyzed by sulfate adenylyltransferase is as follows:

ATP + SO4^2- -> APS + PPi (pyrophosphate)

APS is then further reduced in subsequent steps of the sulfate reduction pathway to form cysteine, which is a building block for proteins and other important biological molecules. Sulfate adenylyltransferase plays a crucial role in the assimilation of sulfur into organic compounds and is widely distributed in nature, being found in bacteria, archaea, and eukaryotes.

Adenosine is a purine nucleoside that is composed of a sugar (ribose) and the base adenine. It plays several important roles in the body, including serving as a precursor for the synthesis of other molecules such as ATP, NAD+, and RNA.

In the medical context, adenosine is perhaps best known for its use as a pharmaceutical agent to treat certain cardiac arrhythmias. When administered intravenously, it can help restore normal sinus rhythm in patients with paroxysmal supraventricular tachycardia (PSVT) by slowing conduction through the atrioventricular node and interrupting the reentry circuit responsible for the arrhythmia.

Adenosine can also be used as a diagnostic tool to help differentiate between narrow-complex tachycardias of supraventricular origin and those that originate from below the ventricles (such as ventricular tachycardia). This is because adenosine will typically terminate PSVT but not affect the rhythm of VT.

It's worth noting that adenosine has a very short half-life, lasting only a few seconds in the bloodstream. This means that its effects are rapidly reversible and generally well-tolerated, although some patients may experience transient symptoms such as flushing, chest pain, or shortness of breath.

Phosphoadenosine phosphosulfate (PAPS) is not exactly a medical term, but a biochemical term. However, it is often referred to in the context of medical and biological research.

PAPS is a crucial molecule in the metabolism of living organisms and serves as the primary donor of sulfate groups in the process of sulfonation, which is a type of enzymatic modification that adds a sulfate group to various substrates such as proteoglycans, hormones, neurotransmitters, and xenobiotics. This process plays an essential role in several biological processes, including detoxification, signal transduction, and cell-cell recognition.

Therefore, PAPS is a critical molecule for maintaining proper physiological functions in the body, and its dysregulation has been implicated in various diseases, such as cancer, inflammation, and neurodevelopmental disorders.

Adenosine A2A receptor is a type of G protein-coupled receptor that binds to the endogenous purine nucleoside, adenosine. It is a subtype of the A2 receptor along with the A2B receptor and is widely distributed throughout the body, particularly in the brain, heart, and immune system.

The A2A receptor plays an essential role in various physiological processes, including modulation of neurotransmission, cardiovascular function, and immune response. In the brain, activation of A2A receptors can have both excitatory and inhibitory effects on neuronal activity, depending on the location and context.

In the heart, A2A receptor activation has a negative chronotropic effect, reducing heart rate, and a negative inotropic effect, decreasing contractility. In the immune system, A2A receptors are involved in regulating inflammation and immune cell function.

Pharmacologically, A2A receptor agonists have been investigated for their potential therapeutic benefits in various conditions, including Parkinson's disease, chronic pain, ischemia-reperfusion injury, and cancer. Conversely, A2A receptor antagonists have also been studied as a potential treatment for neurodegenerative disorders, such as Alzheimer's disease, and addiction.

Adenosine A1 receptor is a type of G protein-coupled receptor that binds to the endogenous purine nucleoside adenosine. When activated, it inhibits the production of cyclic AMP (cAMP) in the cell by inhibiting adenylyl cyclase activity. This results in various physiological effects, such as decreased heart rate and reduced force of heart contractions, increased potassium conductance, and decreased calcium currents. The Adenosine A1 receptor is widely distributed throughout the body, including the brain, heart, kidneys, and other organs. It plays a crucial role in various biological processes, including cardiovascular function, neuroprotection, and inflammation.

Adenosine Deaminase (ADA) is an enzyme that plays a crucial role in the immune system by helping to regulate the levels of certain chemicals called purines within cells. Specifically, ADA helps to break down adenosine, a type of purine, into another compound called inosine. This enzyme is found in all tissues of the body, but it is especially active in the immune system's white blood cells, where it helps to support their growth, development, and function.

ADA deficiency is a rare genetic disorder that can lead to severe combined immunodeficiency (SCID), a condition in which babies are born with little or no functional immune system. This makes them extremely vulnerable to infections, which can be life-threatening. ADA deficiency can be treated with enzyme replacement therapy, bone marrow transplantation, or gene therapy.

Adenosine A3 receptor (A3R) is a type of G-protein coupled receptor that binds to adenosine, a purine nucleoside, and plays a role in various physiological processes. The activation of A3R leads to the inhibition of adenylate cyclase activity, which results in decreased levels of intracellular cAMP. This, in turn, modulates several downstream signaling pathways that are involved in anti-inflammatory and neuroprotective effects.

A3R is widely expressed in various tissues, including the brain, heart, lungs, liver, kidneys, and immune cells. In the central nervous system, A3R activation has been shown to have neuroprotective effects, such as reducing glutamate release, protecting against excitotoxicity, and modulating neuroinflammation. Additionally, A3R agonists have been investigated for their potential therapeutic benefits in various pathological conditions, including pain management, ischemia-reperfusion injury, and neurodegenerative diseases.

Overall, the Adenosine A3 receptor is an important target for drug development due to its role in modulating inflammation and cellular responses in various tissues and diseases.

Adenosine A2B receptor (A2BAR) is a type of G protein-coupled receptor that binds the endogenous purine nucleoside adenosine. It is a subtype of the A2 class of adenosine receptors, which also includes A2A receptor.

The A2BAR is widely expressed in various tissues and cells, including vascular smooth muscle cells, endothelial cells, fibroblasts, immune cells, and epithelial cells. Activation of the A2BAR by adenosine leads to a variety of cellular responses, such as relaxation of vascular smooth muscle, inhibition of platelet aggregation, modulation of inflammatory responses, and stimulation of fibroblast proliferation and collagen production.

The A2BAR has been implicated in several physiological and pathophysiological processes, such as cardiovascular function, pain perception, neuroprotection, tumor growth and metastasis, and pulmonary fibrosis. Therefore, the development of selective A2BAR agonists or antagonists has been an area of active research for therapeutic interventions in these conditions.

Adenosine kinase (ADK) is an enzyme that plays a crucial role in the regulation of adenosine levels in cells. The medical definition of adenosine kinase is:

"An enzyme (EC 2.7.1.20) that catalyzes the phosphorylation of adenosine to form adenosine monophosphate (AMP) using ATP as the phosphate donor. This reaction helps maintain the balance between adenosine and its corresponding nucleotides in cells, and it plays a significant role in purine metabolism, cell signaling, and energy homeostasis."

Adenosine kinase is widely distributed in various tissues, including the brain, heart, liver, and muscles. Dysregulation of adenosine kinase activity has been implicated in several pathological conditions, such as ischemia-reperfusion injury, neurodegenerative disorders, and cancer. Therefore, modulating adenosine kinase activity has emerged as a potential therapeutic strategy for treating these diseases.

Adenosine A2 receptors are a type of G-protein coupled receptor that binds the endogenous purine nucleoside adenosine. They are divided into two subtypes, A2a and A2b, which have different distributions in the body and couple to different G proteins.

A2a receptors are found in high levels in the brain, particularly in the striatum, and play a role in regulating the release of neurotransmitters such as dopamine and glutamate. They also have anti-inflammatory effects and are being studied as potential targets for the treatment of neurological disorders such as Parkinson's disease and multiple sclerosis.

A2b receptors, on the other hand, are found in a variety of tissues including the lung, blood vessels, and immune cells. They play a role in regulating inflammation and vasodilation, and have been implicated in the development of conditions such as asthma and pulmonary fibrosis.

Both A2a and A2b receptors are activated by adenosine, which is released in response to cellular stress or injury. Activation of these receptors can lead to a variety of downstream effects, depending on the tissue and context in which they are expressed.

Adenosine A2 receptor agonists are pharmaceutical agents that bind to and activate the A2 subtype of adenosine receptors, which are G-protein coupled receptors found in various tissues throughout the body. Activation of these receptors leads to a variety of physiological effects, including vasodilation, increased coronary blood flow, and inhibition of platelet aggregation.

A2 receptor agonists have been studied for their potential therapeutic benefits in several medical conditions, such as:

1. Heart failure: A2 receptor agonists can improve cardiac function and reduce symptoms in patients with heart failure by increasing coronary blood flow and reducing oxygen demand.
2. Atrial fibrillation: These agents have been shown to terminate or prevent atrial fibrillation, a common abnormal heart rhythm disorder, through their effects on the electrical properties of cardiac cells.
3. Asthma and COPD: A2 receptor agonists can help relax airway smooth muscle and reduce inflammation in patients with asthma and chronic obstructive pulmonary disease (COPD).
4. Pain management: Some A2 receptor agonists have been found to have analgesic properties, making them potential candidates for pain relief in various clinical settings.

Examples of A2 receptor agonists include regadenoson, which is used as a pharmacological stress agent during myocardial perfusion imaging, and dipyridamole, which is used to prevent blood clots in patients with certain heart conditions. However, it's important to note that these agents can have side effects, such as hypotension, bradycardia, and bronchoconstriction, so their use must be carefully monitored and managed by healthcare professionals.

... is a protein that in humans is encoded by the SLC35B2 gene. Solute carrier ... 2003). "Molecular cloning and identification of 3'-phosphoadenosine 5'-phosphosulfate transporter". J. Biol. Chem. 278 (28): ...
"Adenosine-5'-phosphosulfate". pubchem.ncbi.nlm.nih.gov. Retrieved 2022-07-14. (CS1 German-language sources (de), CS1: long ... In biochemistry, metabolism of sulfate may use such a group, for example with adenosine-5'-phosphosulfate. Frost, Ray L.; ... "Sodium intercalation in the phosphosulfate cathode NaFe2(PO4)(SO4)2". Journal of Power Sources. 382: 144-151. Bibcode:2018JPS ...
... phosphosulfate kinase, adenosine phosphosulfate kinase, adenosine phosphosulfokinase, adenosine-5'-phosphosulfate-3'- ... MacRae IJ, Rose AB, Segel IH (October 1998). "Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed ... Other names in common use include adenylylsulfate kinase (phosphorylating), 5'-phosphoadenosine sulfate kinase, adenosine 5'- ... phosphosulfate synthase and its functional domains". J. Biol. Chem. 273 (30): 19311-20. doi:10.1074/jbc.273.30.19311. PMID ...
PPi is pyrophosphate APS is adenosine 5-phosphosulfate; ATP is adenosine triphosphate; O2 is oxygen molecule; AMP is adenosine ... and with the substrates adenosinephosphosulfate (APS) and luciferin. The addition of one of the four deoxynucleotide ... This incorporation releases pyrophosphate (PPi). ATP sulfurylase converts PPi to ATP in the presence of adenosine 5´ ... phosphosulfate. This ATP acts as a substrate for the luciferase-mediated conversion of luciferin to oxyluciferin that generates ...
... phosphosulfate-forming). Other names in common use include adenosine phosphosulfate reductase, adenosine 5'-phosphosulfate ... Grant K, Carey NM, Mendoza M, Schulze J, Pilon M, Pilon-Smits EA, van Hoewyk D (September 2011). "Adenosine 5'-phosphosulfate ... 2018). "Central Role of Adenosine 5'-Phosphosulfate Reductase in the Control of Plant Hydrogen Sulfide Metabolism". Frontiers ... phosphosulfate reductase. Adenosine 5'-monophosphate inhibitor and key role of arginine 317 in switching the course of ...
Other names in common use include adenosine 5-phosphosulfate sulfohydrolase, and adenylylsulfate sulfohydrolase. This enzyme ...
... adenosine 5′phosphosulfate sulfohydrolase and adenosine-5′-phosphosulfate cyclase activities". Eur. J. Biochem. 65 (1): 113-21 ... The enzyme 3′(2′),5′-bisphosphate nucleotidase (EC 3.1.3.7) catalyzes the reaction adenosine 3′,5′-bisphosphate + H2O ⇌ {\ ... The systematic name is adenosine-3′(2′),5′-bisphosphate 3′(2′)-phosphohydrolase. Other names in common use include ... Farooqui AA, Balasubramanian AS (1970). "Enzymatic dephosphorylation 3′-phosphoadenosine 5′-phoaphosulfate to adenosine 5′- ...
... phosphosulfate. This product is then hydrolysed by 3'(2'),5'-bisphosphate nucleotidase to give adenosine monophosphate, which ... Adenosine 3',5'-bisphosphate is a form of an adenosine nucleotide with two phosphate groups attached to different carbons in ... Adenosine 3',5'-bisphosphate is produced as a product of sulfotransferase enzymes from the donation of a sulfate group from the ... This is distinct from adenosine diphosphate, where the two phosphate groups are attached in a chain to the 5' carbon atom in ...
... adenosinephosphosulfate into 5′-phosphosulfate. The 5'-phosphosulfate is then changed into 3′-phosphoadenosine 5′-phosphate and ... Abola AP, Willits MG, Wang RC, Long SR (September 1999). "Reduction of adenosine-5'-phosphosulfate instead of 3'- ... The systematic name of this enzyme class is AMP, sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5'-phosphosulfate- ... and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5'-phosphosulfate reductase". Journal of Molecular Biology. 364 (2 ...
Li, J. Y.; Schiff, J. A. (1991). "Purification and properties of adenosine 5'-phosphosulphate sulphotransferase from Euglena". ... Li, Jiayang (1991). Purification and properties of ATP sulfurylase and adenosine 5'-phosphosulfate sulfotransferase from ... ATP sulfurylase and adenosine 5'-phosphosulfate sulfotransferase) in the single-celled organism Euglena. Following his PhD, Li ...
The enzymes reduce adenosine-5'-phosphosulfate by nucleophilic attack to produce the sulfite product. This typically involves a ...
17 Reactions of the adenosine 5'-phosphosulfate (APS) sulfotransferase from Chlorella and studies of model reactions which ... Schmidt A (January 1976). "The adenosine-5'-phosphosulfate sulfotransferase from spinach (Spinacea oleracea L.). Stabilization ... Other names in common use include phosphoadenylylsulfate-thiol sulfotransferase, PAPS sulfotransferase, and adenosine 3'- ... adenosine 3',5'-bisphosphate + an S-alkyl thiosulfate Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate ...
Once inside the cell, sulfate is activated by ATP sulfurylase to form adenosine 5'-phosphosulfate (APS), which is then reduced ... Sulfate needs to be activated to adenosine 5'-phosphosulfate (APS) prior to its reduction to sulfite. The activation of sulfate ...
3′-Phosphoadenosine-5′-phosphosulfate (PAPS) is a derivative of adenosine monophosphate (AMP) that is phosphorylated at the 3′ ... It is endogenously synthesized by organisms via the phosphorylation of adenosine 5′-phosphosulfate (APS), an intermediary ... In humans such reaction is performed by bifunctional 3′-phosphoadenosine 5′-phosphosulfate synthases (PAPSS1 and PAPSS2) using ... Venkatachalam, K. V. (2003). "Human 3′-phosphoadenosine 5′-phosphosulfate (PAPS) synthase: Biochemistry, molecular biology and ...
The systematic name of this enzyme class is AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5'-phosphosulfate- ... adenosine-5'-phosphosulfate-forming), and plant-type 5'-adenylylsulfate reductase. In plants, APS is reduced by the plastidic ... 2 glutathione The 3 substrates of this enzyme are adenosine monophosphate, sulfite, and glutathione disulfide, whereas its two ...
... kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5'-phosphosulfate kinase domains". Biochemistry. 43 ... Sekulic N, Konrad M, Lavie A (2007). "Structural mechanism for substrate inhibition of the adenosine 5'-phosphosulfate kinase ... 1998). "cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate ... In humans, PAPS is synthesized from adenosine 5-prime triphosphate (ATP) and inorganic sulfate by 2 isoforms, PAPSS1 and PAPSS2 ...
"Genomic organization of the mouse and human genes encoding the ATP sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2 ... "Entrez Gene: PAPSS2 3'-phosphoadenosine 5'-phosphosulfate synthase 2". Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale ... Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 is an enzyme that in humans is encoded by the PAPSS2 gene. ... In mammals, the sulfate source is 3'-phosphoadenosine 5'-phosphosulfate (PAPS), created from ATP and inorganic sulfate. Two ...
This is done by the enzyme ATP-sulfurylase, which uses ATP and sulfate to create adenosine 5′-phosphosulfate (APS). APS is ...
... usually adenosine 5'-phosphosulfate (APS) or 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Sulfate esters may be hydrolyzed by ...
In this biochemical pathway, AMP reacts with sulfite in the presence of the enzyme APS reductase, giving APS (adenosine 5'- ... phosphosulfate). Then, APS reacts with the enzyme ATP sulfurylase in presence of pyrophosphate (PPi) giving ATP (substrate- ...
... adenosine 3',5'-bisphosphate,sulfite:oxidized-thioredoxin, and oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming). ... adenosine 3'-phosphate 5'-phosphosulfate reductase, 3'-phosphoadenylylsulfate reductase, thioredoxin:3'-phospho-adenylylsulfate ... The systematic name of this enzyme class is adenosine 3',5'-bisphosphate,sulfite:thioredoxin-disulfide oxidoreductase (3'- ... phosphoadenosine-5'-phosphosulfate-forming). Other names in common use include PAPS reductase, thioredoxin-dependent, PAPS ...
ATP sulfurylase first generates adenosine-5'-phosphosulfate (APS) and then APS kinase transfers a phosphate from ATP to APS to ... Kamio, K.; Honke, K.; Makita, A. (Dec 1995). "Pyridoxal 5'-phosphate binds to a lysine residue in the adenosine 3'-phosphate 5 ... In eukaryotic cells the activated sulfate donor is 3'-phosphoadenosine-5'-phosphosulfate (PAPS) (Figure 1). PAPS is synthesized ... May 1997). "Sulfation and sulfotransferases 5: the importance of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) in the regulation ...
It is predicted that the potential use of the sox genes would be in the adenosine 5'-phosphosulfate (APS)/ 3'-Phosphoadenosine- ... 5'-phosphosulfate (PAPS) pathway. Though KT71 and other AAnPs can make up over 10% of the bacterioplanktonic community in ...
Sulfate is an inert anion, so nature activates it by the formation of ester derivative of adenosine 5'-phosphosulfate (APS) and ... 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Many organisms utilize these reactions for metabolic purposes or for the ...
... adenosine 5'-phosphosulfate) thereby consuming ATP. The APS is then reduced by the enzyme APS reductase to form sulfite (SO2− 3 ...
... to Adenosine 5'-phosphosulfate (APS) via adenylation at the cost of an ATP. If the organisms participating in the DSR pathway ... Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulfate. Within the cell Sulfate ... Some sulfate adenylyltransferases are part of a bifunctional polypeptide chain associated with adenosyl phosphosulfate (APS) ... Other names in common use include adenosine-5'-triphosphate sulfurylase, adenosinetriphosphate sulfurylase, adenylylsulfate ...
Heparan sulfate 6-sulfotransferases catalyses the transfer of sulfate from adenosine 3'-phosphate, 5'-phosphosulfate to the 6th ...
... occurs in four steps: Conversion (activation) of sulfate to adenosine 5'-phosphosulfate (APS) ...
... phosphosulfate + chondroitin ⇌ {\displaystyle \rightleftharpoons } adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate Thus, ... I Transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate to mucopolysaccharides". J. Biol. Chem. 235: 257-266. PMID ... the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and chondroitin, whereas its two products are adenosine 3',5'- ...
... phosphosulfate and 5beta-scymnol, whereas its two products are adenosine 3',5'-bisphosphate and 5beta-scymnol sulfate. This ... phosphosulfate + 5beta-scymnol ⇌ {\displaystyle \rightleftharpoons } adenosine 3',5'-bisphosphate + 5beta-scymnol sulfate Thus ... The systematic name of this enzyme class is 3'-Phosphoadenosine-5'-phosphosulfate:5beta-scymnol sulfotransferase. Macrides TA, ...
Adenosine 3-phospho 5-phosphosulfate transporter 1 is a protein that in humans is encoded by the SLC35B2 gene. Solute carrier ... 2003). "Molecular cloning and identification of 3-phosphoadenosine 5-phosphosulfate transporter". J. Biol. Chem. 278 (28): ...
SRB measured using the adenosine-5-phosphosulfate reductase gene (aps) and the dissimilatory sulfite reductase gene (dsr) both ... SRB: Sulfate-reducing bacteria, aps: Adenosine-5-phosphosulfate reductase gene, dsr: Dissimilatory sulfite reductase gene. ... SRB: Sulfate-reducing bacteria, aps: Adenosine-5-phosphosulfate reductase gene, dsr: Dissimilatory sulfite reductase gene. ... SRB: Sulfate-reducing bacteria, aps: Adenosine-5-phosphosulfate reductase gene, dsr: Dissimilatory sulfite reductase gene. ...
Q-PCR of the functional gene (adenosine-5′-phosphosulfate reductase alpha subunit gene, aprA) of SRB. We further determined the ... Meyer B, Kuever J. Molecular analysis of the distribution and phylogeny of dissimilatory adenosine-5′-phosphosulfate reductase- ...
Phosphoadenosine phosphosulfate + Dehydroepiandrosterone → Adenosine 3,5-diphosphate + Dehydroepiandrosterone sulfate. ...
AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5-phosphosulfate-forming). Brite. KEGG Orthology (KO) [BR:ko00001] ...
Biochem., 177, 67 - 71 (1989), "Synthesis and Properties of a Nonhydrolyzable Adenosine Phosphosulfate Analog" ... Commun., 595, 0 - 0 (1982), "Synthesis of Adenosine 5 [(R)alpha-17O]Triphosphate" ...
3′-Phosphoadenosine 5′-phosphosulfate allosterically regulates sulfotransferase turnover. Wang, T., Cook, I. & Leyh, T. S., Nov ... Potent inhibition of human sulfotransferase 1A1 by 17α- ethinylestradiol: Role of 3′-phosphoadenosine 5′-phosphosulfate binding ...
Phosphoadenosine Phosphosulfate. *Vidarabine Phosphate. Below are MeSH descriptors whose meaning is more specific than " ... "Adenosine Monophosphate" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... CD73-generated adenosine restricts lymphocyte migration into draining lymph nodes. J Immunol. 2008 May 01; 180(9):6288-96. ... This graph shows the total number of publications written about "Adenosine Monophosphate" by people in this website by year, ...
Adenosine-5-phosphosulfate reductase beta subunit. HJ. PF13187 Fer4_9. 4Fe-4S dicluster domain. ...
... adenosine 5-phosphosulphate (APS) as a signalling molecule for sulphate excess. Mol Microbiol. 2002, 43 (5): 1347-1358. ...
Match: YPR011C_mRNA (Mitochondrial transporter; major substrates are adenosine 5-phosphosulfate (APS) and 3-phospho-adenosine ... 5-phosphosulfate (PAPS); member of the mitochondrial carrier family; the authentic, non-tagged protein is detected in highly ...
Slalom encodes an adenosine 3′-phosphate 5′-phosphosulfate transporter essential for development in Drosophila. EMBO J. ... Slalom encodes an adenosine 3′-phosphate 5′-phosphosulfate transporter essential for development in Drosophila. EMBO J. ...
phosphosulfate. Adenosine 3,5-diphosphate. Dehydroepiandrosterone sulfate. Testosterone. O. 2. H. 2. O. NAD. NADH. H. +. 5b- ... phosphosulfate. Estrone sulfate. Adenosine 3,5-diphosphate. 19-Oxoandrost-4-ene-3,17-dione. Estradiol. NADP. NADPH. 19- ...
This enzymatic reaction requires PAPS (3 -phospho-adenosine-5 -phosphosulfate) biosynthesis mediated by PAPS synthase 2 ( ...
In the absence of adenosine 5-phosphosulfate reductase, we hypothesized that MBGE perform sulfite reduction rather than ...
In humans, PAPS is synthesized from adenosine 5-prime triphosphate (ATP) and inorganic sulfate by 2 isoforms, PAPSS1 and PAPSS2 ... phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3- ... Three-prime-phosphoadenosine 5-prime-phosphosulfate (PAPS) is the sulfate donor cosubstrate for all sulfotransferase (SULT) ... The first step is the transfer of a sulfate group to ATP to yield adenosine 5- ...
In this report, PAPS was regenerated following sulfuryl group transfer between adenosine 3,5-diphosphate and 4- ... Tyrosylprotein sulfotransferase (TPST) catalyzes protein sulfation using 3-phosphate 5-phosphosulfate (PAPS) as sulfuryl ... improves the CoCl-induced autophagy of cardiomyocytes via upregulation of adenosine 5-monophosphate-activated protein kinase ( ...
... phosphosulfate reductase (APR) activity. However, the mutants had lower levels of these metabolites, while the sulfate content ... which are downstream to adenosine 5′ phosphosulfate reductase (APR) activity. However, the mutants had lower levels of these ... Glutathion reductase Sulfur assimilation pathway 5 phosphosulfate reductase Glutathione Cysteine Arabidopsis mutants ...
","adenosine kinase","protein_coding" "LOC_Os04g45280.1","No alias","Oryza sativa","Bifunctional adenosine 5-phosphosulfate ... ","adenosine kinase","protein_coding" "AT2G37585","No alias","Arabidopsis thaliana","Core-2/I-branching beta-1,6-N- ... ","adenosine kinase 1","protein_coding" "AT3G10180","No alias","Arabidopsis thaliana","P-loop containing nucleoside ... ","component TAD3 of TAD2-TAD3 tRNA adenosine deaminase complex","protein_coding" "LOC_Os09g09630.1","No alias","Oryza sativa ...
1 2 The reduction of sulfate requires its activation by an ATP-dependent activation to form adenosine-5′-phosphosulfate (APS). ... postition of the adenosine 5′-phosphate (AMP) moiety reminiscent of APS and PAPS. In glutathione reductase the switch in ... phosphosulfate (PAPS) the substrate for PAPS reductase (PAPR; Plan 1 Table 1 and Number 1). These essential enzymes ...
16-weeks-old). S-supply negatively influenced adenosine-5′-phosphosulphate (APS) reductase (APR) enzyme activity in both ... 16-weeks-old). S-supply negatively influenced adenosine-5′-phosphosulphate (APS) reductase (APR) enzyme activity in both ... 16-weeks-old). S-supply negatively influenced adenosine-5′-phosphosulphate (APS) reductase (APR) enzyme activity in both ... 16-weeks-old). S-supply negatively influenced adenosine-5′-phosphosulphate (APS) reductase (APR) enzyme activity in both ...
Adenosine Monophosphate D3.438.759.646.138.180 D3.633.100.759.646.138.180 Adenosine Phosphosulfate D3.438.759.646.138.180.80 ... Adenosine A1 D12.776.543.750.100.700.700.100 D12.776.543.750.695.700.700.100 Receptor, Adenosine A2A D12.776.543.750.100.700. ... Adenosine D3.438.759.590.138 D3.633.100.759.590.138 Adenosine Diphosphate D3.438.759.646.138.124 D3.633.100.759.646.138.124 ... Adenosine Diphosphate Ribose D3.438.759.646.138.124.70.125 D3.633.100.759.646.138.124.70.125 Adenosine Diphosphate Sugars ...
Adenosine Monophosphate D3.438.759.646.138.180 D3.633.100.759.646.138.180 Adenosine Phosphosulfate D3.438.759.646.138.180.80 ... Adenosine A1 D12.776.543.750.100.700.700.100 D12.776.543.750.695.700.700.100 Receptor, Adenosine A2A D12.776.543.750.100.700. ... Adenosine D3.438.759.590.138 D3.633.100.759.590.138 Adenosine Diphosphate D3.438.759.646.138.124 D3.633.100.759.646.138.124 ... Adenosine Diphosphate Ribose D3.438.759.646.138.124.70.125 D3.633.100.759.646.138.124.70.125 Adenosine Diphosphate Sugars ...
... phosphosulfate kinase, adenosine phosphosulfate kinase, adenosine phosphosulfokinase, adenosine-5-phosphosulfate-3- ... c] : apsName: Adenosine 5-phosphosulfate. Formula: C10H12N5O10PS. Charge: -2. click to see details on this item + atpName: ATP ... Other names: adenylylsulfate kinase (phosphorylating), 5-phosphoadenosine sulfate kinase, adenosine 5- ...
The activity of the key sulphur assimilatory enzyme, adenosine 5′-phosphosulphate reductase was not coordinated with increasing ...
3,5 cAMP binding ; adenosine 3,5-cyclophosphate binding ; cyclic AMP binding. ... 3-phosphoadenosine 5-phosphosulfate binding 5-O-phosphono-alpha-D-ribofuranosyl diphosphate binding ...
1. Synthesis of S-adenosylmethionine: Methionine condenses with adenosine triphosphate (ATP), forming SAM, a high-energy ... Note: The sulfate released can be used to synthesize 3-phosphoadenosine-5I-phosphosulfate (PAPS), an activated sulfur donor to ... and adenosine. Hcy has two fates. If there is a deficiency of methionine, Hcy may be remethylated to methionine (see Figure ...
First, ATP sulfurylase attaches sulfate to the adenosine nucleotide, then APS kinase adds an additional phosphoryl group to ... These enzymes take a sulfuryl group from the convenient carrier molecule PAPS (3-phosphoadenosine-5-phosphosulfate), and ...
  • In the absence of adenosine 5'-phosphosulfate reductase, we hypothesized that MBGE perform sulfite reduction rather than sulfate reduction to conserve energy. (edu.sa)
  • The results showed that the transgenic plants have higher levels of sulfite, cysteine, glutathione and methionine, which are downstream to adenosine 5′ phosphosulfate reductase (APR) activity. (hal.science)
  • S-supply negatively influenced adenosine-5′-phosphosulphate (APS) reductase (APR) enzyme activity in both cultivars at bulbing only, and a higher abundance of APR was observed in both cultivars at bulbing in response to low S-supply. (edu.sa)
  • This enzymatic reaction requires PAPS (3 '-phospho-adenosine-5 '-phosphosulfate) biosynthesis mediated by PAPS synthase 2 (PAPSS2). (ktu.edu.tr)
  • The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). (nih.gov)
  • Three-prime-phosphoadenosine 5-prime-phosphosulfate (PAPS) is the sulfate donor cosubstrate for all sulfotransferase (SULT) enzymes (Xu et al. (nih.gov)
  • Structurally NADP and NAD differ by a phosphate group at the 3′-postition of the adenosine 5′-phosphate (AMP) moiety reminiscent of APS and PAPS. (researchhunt.com)
  • Note: The sulfate released can be used to synthesize 3-phosphoadenosine-5 I -phosphosulfate (PAPS), an activated sulfur donor to a variety of acceptors. (pharmacy180.com)
  • Intro Assimilatory sulfate reduction supplies prototrophic organisms with reduced sulfur that is required for the biosynthesis of all sulfur-containing metabolites including the amino acids cysteine and methionine (1 2 The reduction of sulfate requires its activation by an ATP-dependent activation to form adenosine-5′-phosphosulfate (APS). (researchhunt.com)
  • Analysis of sulfate metabolism in fibroblast cultures showed, in the patient's cells, normal intracellular levels of free sulfate but markedly reduced levels of the two intermediate compounds in the sulfate activation pathway, adenosine-phosphosulfate and phosphoadenosine-phosphosulfate. (nih.gov)
  • Adenosine 5′ phosphosulfate (APS) is used as a substrate of adenosine triphosphate (ATP) sulfurylase to complete a PP(i)-recycling loop for exponential ATP amplification in firefly luciferase ATP luminescence assay and other pyrophosphate regeneration-dependent detection assays. (sigmaaldrich.com)
  • Adenosine 5′-phosphosulfate sodium salt has been used in enzyme-linked bioluminescence assay for adenosine triphosphate (ATP) and pyrophosphate quantification. (sigmaaldrich.com)
  • Molecular cloning and characterization of a novel 3'-phosphoadenosine 5'-phosphosulfate transporter, PAPST2. (nih.gov)
  • Expression and the role of 3'-phosphoadenosine 5'-phosphosulfate transporters in human colorectal carcinoma. (nih.gov)