sodium pyrophosphate (V)

ID: ALA450079

Chembl Id: CHEMBL450079

Max Phase: Unknown

Molecular Formula: Na4O7P2

Molecular Weight: 177.97

Molecule Type: Small molecule

Associated Items:

Names and Identifiers

Synonyms: Sodium pyrophosphate | Tetrasodium pyrophosphate | NSC-56751

Canonical SMILES:  O=P([O-])([O-])OP(=O)([O-])[O-].[Na+].[Na+].[Na+].[Na+]

Standard InChI:  InChI=1S/4Na.H4O7P2/c;;;;1-8(2,3)7-9(4,5)6/h;;;;(H2,1,2,3)(H2,4,5,6)/q4*+1;/p-4

Standard InChI Key:  FQENQNTWSFEDLI-UHFFFAOYSA-J

Associated Targets(Human)

CA1 Tclin Carbonic anhydrase I (13240 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA2 Tclin Carbonic anhydrase II (17698 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA4 Tclin Carbonic anhydrase IV (2163 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA7 Tclin Carbonic anhydrase VII (2318 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA12 Tclin Carbonic anhydrase XII (6231 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA9 Tclin Carbonic anhydrase IX (8255 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA14 Tclin Carbonic anhydrase XIV (1305 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
TDP1 Tchem Tyrosyl-DNA phosphodiesterase 1 (345557 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
BTN3A1 Tchem Butyrophilin subfamily 3 member A1 (291 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID

Associated Targets(non-human)

Ca13 Carbonic anhydrase XIII (322 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
Astrosclerin-3 (80 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
Carbonic anhydrase (197 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
Trypanosoma cruzi (99888 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
Carbonic anhydrase (37 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID

Molecule Features

Natural Product: NoOral: NoChemical Probe: NoParenteral: No
Molecule Type: Small moleculeTopical: NoFirst In Class: NoBlack Box: No
Chirality: YesAvailability: NoProdrug: No

Drug Indications

MESH IDMESH Heading EFO IDsEFO TermsMax Phase for IndicationReferences

Mechanisms of Action

Mechanism of ActionAction Typetarget IDTarget NameTarget TypeTarget OrganismBinding Site NameReferences

Calculated Properties

Molecular Weight: 177.97Molecular Weight (Monoisotopic): 177.9432AlogP: -0.81#Rotatable Bonds: 2
Polar Surface Area: 124.29Molecular Species: ACIDHBA: 3HBD: 4
#RO5 Violations: 0HBA (Lipinski): 7HBD (Lipinski): 4#RO5 Violations (Lipinski): 0
CX Acidic pKa: 1.70CX Basic pKa: CX LogP: -1.44CX LogD: -6.88
Aromatic Rings: 0Heavy Atoms: 9QED Weighted: 0.41Np Likeness Score: 0.89

References

1. Innocenti A, Scozzafava A, Supuran CT..  (2009)  Carbonic anhydrase inhibitors. Inhibition of cytosolic isoforms I, II, III, VII and XIII with less investigated inorganic anions.,  19  (7): [PMID:19269822] [10.1016/j.bmcl.2009.02.088]
2. Innocenti A, Scozzafava A, Supuran CT..  (2010)  Carbonic anhydrase inhibitors. Inhibition of transmembrane isoforms IX, XII, and XIV with less investigated anions including trithiocarbonate and dithiocarbamate.,  20  (5): [PMID:20137947] [10.1016/j.bmcl.2010.01.081]
3. Burghout P, Vullo D, Scozzafava A, Hermans PW, Supuran CT..  (2011)  Inhibition of the β-carbonic anhydrase from Streptococcus pneumoniae by inorganic anions and small molecules: Toward innovative drug design of antiinfectives?,  19  (1): [PMID:21163660] [10.1016/j.bmc.2010.11.031]
4. Vullo D, Nishimori I, Minakuchi T, Scozzafava A, Supuran CT..  (2011)  Inhibition studies with anions and small molecules of two novel β-carbonic anhydrases from the bacterial pathogen Salmonella enterica serovar Typhimurium.,  21  (12): [PMID:21570835] [10.1016/j.bmcl.2011.04.105]
5. Ohradanova A, Vullo D, Pastorekova S, Pastorek J, Jackson DJ, Wörheide G, Supuran CT..  (2012)  Anion inhibition studies of an α-carbonic anhydrase from the living fossil Astrosclera willeyana.,  22  (3): [PMID:22227210] [10.1016/j.bmcl.2011.12.085]
6. De Luca V, Vullo D, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C..  (2012)  Anion inhibition studies of an α-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1.,  22  (17): [PMID:22835873] [10.1016/j.bmcl.2012.06.106]
7. USP Dictionary of USAN and International Names (2010 edition) and USAN registrations 2007-date, 
8. Vullo D, De Luca V, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C..  (2012)  Anion inhibition studies of the fastest carbonic anhydrase (CA) known, the extremo-CA from the bacterium Sulfurihydrogenibium azorense.,  22  (23): [PMID:23072866] [10.1016/j.bmcl.2012.09.065]
9. PubChem BioAssay data set, 
10. Vullo D, Isik S, Del Prete S, De Luca V, Carginale V, Scozzafava A, Supuran CT, Capasso C..  (2013)  Anion inhibition studies of the α-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae.,  23  (6): [PMID:23414807] [10.1016/j.bmcl.2013.01.084]
11. Monti SM, De Simone G, Dathan NA, Ludwig M, Vullo D, Scozzafava A, Capasso C, Supuran CT..  (2013)  Kinetic and anion inhibition studies of a β-carbonic anhydrase (FbiCA 1) from the C4 plant Flaveria bidentis.,  23  (6): [PMID:23414801] [10.1016/j.bmcl.2013.01.087]
12. Del Prete S, Vullo D, De Luca V, Carginale V, Scozzafava A, Supuran CT, Capasso C..  (2013)  A highly catalytically active γ-carbonic anhydrase from the pathogenic anaerobe Porphyromonas gingivalis and its inhibition profile with anions and small molecules.,  23  (14): [PMID:23769640] [10.1016/j.bmcl.2013.05.063]
13. Pan P, Vermelho AB, Scozzafava A, Parkkila S, Capasso C, Supuran CT..  (2013)  Anion inhibition studies of the α-carbonic anhydrase from the protozoan pathogen Trypanosoma cruzi, the causative agent of Chagas disease.,  21  (15): [PMID:23790722] [10.1016/j.bmc.2013.05.058]
14. Vullo D, Sai Kumar RS, Scozzafava A, Capasso C, Ferry JG, Supuran CT..  (2013)  Anion inhibition studies of a β-carbonic anhydrase from Clostridium perfringens.,  23  (24): [PMID:24210500] [10.1016/j.bmcl.2013.10.037]
15. Nishimori I, Vullo D, Minakuchi T, Scozzafava A, Osman SM, AlOthman Z, Capasso C, Supuran CT..  (2014)  Anion inhibition studies of two new β-carbonic anhydrases from the bacterial pathogen Legionella pneumophila.,  24  (4): [PMID:24461298] [10.1016/j.bmcl.2013.12.124]
16. Del Prete S, Vullo D, Fisher GM, Andrews KT, Poulsen SA, Capasso C, Supuran CT..  (2014)  Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum--the η-carbonic anhydrases.,  24  (18): [PMID:25168745] [10.1016/j.bmcl.2014.08.015]
17. Vullo D, Del Prete S, Osman SM, Scozzafava A, Alothman Z, Supuran CT, Capasso C..  (2014)  Anion inhibition study of the β-class carbonic anhydrase (PgiCAb) from the oral pathogen Porphyromonas gingivalis.,  24  (18): [PMID:25168748] [10.1016/j.bmcl.2014.08.014]
18. De Luca V, Vullo D, Del Prete S, Carginale V, Scozzafava A, Osman SM, AlOthman Z, Supuran CT, Capasso C..  (2015)  Cloning, characterization and anion inhibition studies of a new γ-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis.,  23  (15): [PMID:26145820] [10.1016/j.bmc.2015.06.021]
19. Pinard MA, Lotlikar SR, Boone CD, Vullo D, Supuran CT, Patrauchan MA, McKenna R..  (2015)  Structure and inhibition studies of a type II beta-carbonic anhydrase psCA3 from Pseudomonas aeruginosa.,  23  (15): [PMID:26068018] [10.1016/j.bmc.2015.05.029]
20. De Luca V, Vullo D, Del Prete S, Carginale V, Osman SM, AlOthman Z, Supuran CT, Capasso C..  (2016)  Cloning, characterization and anion inhibition studies of a γ-carbonic anhydrase from the Antarctic bacterium Colwellia psychrerythraea.,  24  (4): [PMID:26778292] [10.1016/j.bmc.2016.01.005]
21. Del Prete S, Vullo D, De Luca V, Carginale V, di Fonzo P, Osman SM, AlOthman Z, Supuran CT, Capasso C..  (2016)  Anion inhibition profiles of the complete domain of the η-carbonic anhydrase from Plasmodium falciparum.,  24  (18): [PMID:27480028] [10.1016/j.bmc.2016.07.034]
22. Del Prete S, Vullo D, Di Fonzo P, Osman SM, AlOthman Z, Supuran CT, Capasso C..  (2017)  Anion inhibition profiles of the γ-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei responsible of melioidosis and highly drug resistant to common antibiotics.,  25  (2): [PMID:27914949] [10.1016/j.bmc.2016.11.021]
23. Del Prete S, Vullo D, di Fonzo P, Carginale V, Supuran CT, Capasso C..  (2017)  Comparison of the anion inhibition profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei.,  25  (6): [PMID:28238511] [10.1016/j.bmc.2017.02.032]
24. Del Prete S, Vullo D, Osman SM, AlOthman Z, Donald WA, Winum JY, Supuran CT, Capasso C..  (2017)  Anion inhibitors of the β-carbonic anhydrase from the pathogenic bacterium responsible of tularemia, Francisella tularensis.,  25  (17): [PMID:28754318] [10.1016/j.bmc.2017.07.033]
25. Poe MM, Agabiti SS, Liu C, Li V, Teske KA, Hsiao CC, Wiemer AJ..  (2019)  Probing the Ligand-Binding Pocket of BTN3A1.,  62  (14): [PMID:31268699] [10.1021/acs.jmedchem.9b00825]