Page last updated: 2024-12-08

adenosine 2',5'-diphosphate

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Related Drugs Related Conditions Protein Interactions Research Growth Market Indicators

Cross-References

ID SourceID
PubMed CID168973
MeSH IDM0132816
PubMed CID440141
CHEMBL ID1161861
SCHEMBL ID1122523
MeSH IDM0132816

Synonyms (32)

Synonym
3805-37-6
adenosine 2',5'-diphosphate
2',5'-adp
[(2r,5r)-2-(6-aminopurin-9-yl)-4-hydroxy-5-(phosphonooxymethyl)oxolan-3-yl] dihydrogen phosphate
2'-adenylic acid, 5'-(dihydrogen phosphate)
ado(2',5')p2
2'-phospho-amp
gtpl1717
adenosine-2'-5'-diphosphate
a2p ,
C03850 ,
adenosine 2',5'-bisphosphate
a2p5p
DB02098
{[(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)oxolan-2-yl]methoxy}phosphonic acid
1HI3
bdbm11941
1H1H
adenosine-2 -5 -diphosphate
9ICD
1O0O
2,5-adp
[(2r,3r,4r,5r)-2-(6-aminopurin-9-yl)-4-hydroxy-5-(phosphonooxymethyl)oxolan-3-yl] dihydrogen phosphate
CHEMBL1161861
adenosine 2',5'-diphosphate sodium salt
SCHEMBL1122523
[(2r,3r,4r,5r)-2-(6-aminopurin-9-yl)-4-hydroxy-5-(phosphonooxymethyl)tetrahydrofuran-3-yl] dihydrogen phosphate
J-009072
adenosine 2',5'-bis(dihydrogen phosphate)
Q27074060
9-(2,5-di-o-phosphonopentofuranosyl)-9h-purin-6-amine
DTXSID70959011
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (12)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Chain A, EOSINOPHIL CATIONIC PROTEINHomo sapiens (human)Ki6.00006.00006.00006.0000AID977610
Chain A, EOSINOPHIL-DERIVED NEUROTOXINHomo sapiens (human)Ki64.000032.000062.666792.0000AID977610
Chain A, EOSINOPHIL-DERIVED NEUROTOXINHomo sapiens (human)Ki64.000032.000062.666792.0000AID977610
Chain A, EOSINOPHIL-DERIVED NEUROTOXINHomo sapiens (human)Ki64.000032.000062.666792.0000AID977610
Chain A, Ribonuclease pancreaticBos taurus (cattle)Ki8.00001.200024.050082.0000AID977610
Chain A, Ribonuclease pancreaticBos taurus (cattle)Ki8.00001.200024.050082.0000AID977610
Chain A, Ribonuclease pancreaticBos taurus (cattle)Ki8.00001.200024.050082.0000AID977610
Chain A, Ribonuclease pancreaticBos taurus (cattle)Ki8.00001.200024.050082.0000AID977610
Chain A, Ribonuclease pancreaticBos taurus (cattle)Ki8.00001.200024.050082.0000AID977610
P2Y purinoceptor 1Meleagris gallopavo (turkey)IC50 (µMol)8.46004.19006.04258.4600AID165239
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Activation Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Chain A, ISOCITRATE DEHYDROGENASEEscherichia coliKd125.0000125.0000125.0000125.0000AID977611
2-dehydropantoate 2-reductaseEscherichia coli K-12Kd100.00000.26000.26000.2600AID269136
P2Y purinoceptor 1Meleagris gallopavo (turkey)EC50 (µMol)1.37000.00251.70498.0000AID165236
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (1)

Processvia Protein(s)Taxonomy
pantothenate biosynthetic process2-dehydropantoate 2-reductaseEscherichia coli K-12
pantothenate biosynthetic process2-dehydropantoate 2-reductaseEscherichia coli K-12
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (4)

Processvia Protein(s)Taxonomy
2-dehydropantoate 2-reductase activity2-dehydropantoate 2-reductaseEscherichia coli K-12
oxidoreductase activity2-dehydropantoate 2-reductaseEscherichia coli K-12
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor2-dehydropantoate 2-reductaseEscherichia coli K-12
NADP binding2-dehydropantoate 2-reductaseEscherichia coli K-12
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (1)

Processvia Protein(s)Taxonomy
cytoplasm2-dehydropantoate 2-reductaseEscherichia coli K-12
cytoplasm2-dehydropantoate 2-reductaseEscherichia coli K-12
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (16)

Assay IDTitleYearJournalArticle
AID165243Antagonist activity at P2Y1 receptor measured as capacity to inhibit phospholipase C stimulation elicited by 10 nM 2-MeSATP1998Journal of medicinal chemistry, Jan-15, Volume: 41, Issue:2
Deoxyadenosine bisphosphate derivatives as potent antagonists at P2Y1 receptors.
AID269131Inhibition of Escherichia coli KPR at 1 mM2006Journal of medicinal chemistry, Aug-10, Volume: 49, Issue:16
Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods.
AID165236Agonist activity at P2Y1 receptor measured as capacity to stimulate 50% phospholipase C in turkey erythrocyte membranes1998Journal of medicinal chemistry, Jan-15, Volume: 41, Issue:2
Deoxyadenosine bisphosphate derivatives as potent antagonists at P2Y1 receptors.
AID269135Inhibition of Escherichia coli KPR2006Journal of medicinal chemistry, Aug-10, Volume: 49, Issue:16
Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods.
AID165240Agonist activity at P2Y1 receptor measured as capacity to stimulate phospholipase C in turkey erythrocyte membranes1998Journal of medicinal chemistry, Jan-15, Volume: 41, Issue:2
Deoxyadenosine bisphosphate derivatives as potent antagonists at P2Y1 receptors.
AID165239Antagonist activity at P2Y1 receptor measured as capacity to inhibit 50% of phospholipase C stimulation elicited by 10 nM 2-MeSATP1998Journal of medicinal chemistry, Jan-15, Volume: 41, Issue:2
Deoxyadenosine bisphosphate derivatives as potent antagonists at P2Y1 receptors.
AID269136Binding affinity to Escherichia coli KPR2006Journal of medicinal chemistry, Aug-10, Volume: 49, Issue:16
Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods.
AID1811Experimentally measured binding affinity data derived from PDB1991Biochemistry, Sep-03, Volume: 30, Issue:35
Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes.
AID977611Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB1991Biochemistry, Sep-03, Volume: 30, Issue:35
Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes.
AID1346309Human P2Y1 receptor (P2Y receptors)1996Molecular pharmacology, Nov, Volume: 50, Issue:5
Identification of competitive antagonists of the P2Y1 receptor.
AID977610Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB2002Biochemistry, Oct-08, Volume: 41, Issue:40
The crystal structure of eosinophil cationic protein in complex with 2',5'-ADP at 2.0 A resolution reveals the details of the ribonucleolytic active site.
AID1811Experimentally measured binding affinity data derived from PDB2002Biochemistry, Oct-08, Volume: 41, Issue:40
The crystal structure of eosinophil cationic protein in complex with 2',5'-ADP at 2.0 A resolution reveals the details of the ribonucleolytic active site.
AID977610Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB2003Protein science : a publication of the Protein Society, Nov, Volume: 12, Issue:11
High-resolution crystal structures of ribonuclease A complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors.
AID1811Experimentally measured binding affinity data derived from PDB2003Protein science : a publication of the Protein Society, Nov, Volume: 12, Issue:11
High-resolution crystal structures of ribonuclease A complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors.
AID1811Experimentally measured binding affinity data derived from PDB2001The Journal of biological chemistry, May-04, Volume: 276, Issue:18
Mapping the ribonucleolytic active site of eosinophil-derived neurotoxin (EDN). High resolution crystal structures of EDN complexes with adenylic nucleotide inhibitors.
AID977610Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB2001The Journal of biological chemistry, May-04, Volume: 276, Issue:18
Mapping the ribonucleolytic active site of eosinophil-derived neurotoxin (EDN). High resolution crystal structures of EDN complexes with adenylic nucleotide inhibitors.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (35)

TimeframeStudies, This Drug (%)All Drugs %
pre-19905 (14.29)18.7374
1990's12 (34.29)18.2507
2000's16 (45.71)29.6817
2010's2 (5.71)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 11.11

According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be weak demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index11.11 (24.57)
Research Supply Index3.40 (2.92)
Research Growth Index4.51 (4.65)
Search Engine Demand Index0.00 (26.88)
Search Engine Supply Index0.00 (0.95)

This Compound (11.11)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Trials0 (0.00%)5.53%
Reviews1 (3.45%)6.00%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Observational0 (0.00%)0.25%
Other28 (96.55%)84.16%
Other7 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]