Phenylarsonic acid

ID: ALA364571

Chembl Id: CHEMBL364571

Cas Number: 98-05-5

PubChem CID: 7365

Product Number: P101336

Max Phase: Preclinical

Molecular Formula: C6H7AsO3

Molecular Weight: 202.04

Molecule Type: Small molecule

Associated Items:

Names and Identifiers

Synonyms: Phenylarsonic Acid | Phenylarsonic acid|BENZENEARSONIC ACID|98-05-5|Monophenylarsonic acid|Arsonic acid, phenyl-|Arsonic acid, As-phenyl-|CHEMBL364571|CHEBI:29851|57F9KU116M|NSC-15566|Kyselina benzenarsonova [Czech]|Kyselina benzenarsonova|HSDB 6381|EINECS 202-631-9|NSC 15566|BRN 2935741|UNII-57F9KU116M|AI3-16050|benzenarsonic acid|Benzenearsonie acid|PhAsO3H2|PhAsO(OH)2|4-16-00-01183 (Beilstein Handbook Reference)|SCHEMBL707127|WLN: Q-AS-QO & R|BENZENEARSONIC ACID [MI]|DTXSID6059158|BDBM26997|LShow More

Synonyms from Alternative Forms(2): Sodium Phenylarsonate | Phenylarsonic Acid Sodium Salt

Canonical SMILES:  O=[As](O)(O)c1ccccc1

Standard InChI:  InChI=1S/C6H7AsO3/c8-7(9,10)6-4-2-1-3-5-6/h1-5H,(H2,8,9,10)

Standard InChI Key:  LVKZSFMYNWRPJX-UHFFFAOYSA-N

Alternative Forms

  1. Parent:

  2. Alternative Forms:

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
CA5B Tclin Carbonic anhydrase V (54 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA9 Tclin Carbonic anhydrase IX (8255 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA7 Tclin Carbonic anhydrase VII (2318 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA5B Tclin Carbonic anhydrase VB (957 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA5A Tclin Carbonic anhydrase VA (1168 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA6 Tclin Carbonic anhydrase VI (993 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA12 Tclin Carbonic anhydrase XII (6231 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA14 Tclin Carbonic anhydrase XIV (1305 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID

Associated Targets(non-human)

NCE103 Carbonic anhydrase (253 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
NCE103 Carbonic anhydrase (85 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
NCE103 Carbonic anhydrase (137 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA Alpha carbonic anhydrase (93 Activities)
Activity TypeRelationActivity valueUnitsAction TypeJournalPubMed IddoiAssay Aladdin ID
CA2 Carbonic anhydrase (56 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: YesOral: NoChemical Probe: NoParenteral: No
Molecule Type: Small moleculeTopical: NoFirst In Class: NoBlack Box: No
Chirality: NoAvailability: 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: 202.04Molecular Weight (Monoisotopic): 201.9611AlogP: #Rotatable Bonds:
Polar Surface Area: Molecular Species: HBA: HBD:
#RO5 Violations: HBA (Lipinski): HBD (Lipinski): #RO5 Violations (Lipinski):
CX Acidic pKa: CX Basic pKa: CX LogP: CX LogD:
Aromatic Rings: Heavy Atoms: QED Weighted: Np Likeness Score:

References

1. Innocenti A, Firnges MA, Antel J, Wurl M, Scozzafava A, Supuran CT..  (2004)  Carbonic anhydrase inhibitors: inhibition of the membrane-bound human isozyme IV with anions.,  14  (23): [PMID:15501038] [10.1016/j.bmcl.2004.09.063]
2. Vullo D, Ruusuvuori E, Kaila K, Scozzafava A, Supuran CT..  (2006)  Carbonic anhydrase inhibitors: inhibition of the cytosolic human isozyme VII with anions.,  16  (12): [PMID:16621537] [10.1016/j.bmcl.2006.03.078]
3. Nishimori I, Innocenti A, Vullo D, Scozzafava A, Supuran CT..  (2007)  Carbonic anhydrase inhibitors: the inhibition profiles of the human mitochondrial isoforms VA and VB with anions are very different.,  15  (21): [PMID:17761422] [10.1016/j.bmc.2007.08.008]
4. Nishimori I, Innocenti A, Vullo D, Scozzafava A, Supuran CT..  (2007)  Carbonic anhydrase inhibitors. Inhibition studies of the human secretory isoform VI with anions.,  17  (4): [PMID:17127063] [10.1016/j.bmcl.2006.11.028]
5. Innocenti A, Vullo D, Pastorek J, Scozzafava A, Pastorekova S, Nishimori I, Supuran CT..  (2007)  Carbonic anhydrase inhibitors. Inhibition of transmembrane isozymes XII (cancer-associated) and XIV with anions.,  17  (6): [PMID:17257840] [10.1016/j.bmcl.2006.12.113]
6. Isik S, Kockar F, Arslan O, Guler OO, Innocenti A, Supuran CT..  (2008)  Carbonic anhydrase inhibitors. Inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with anions.,  18  (24): [PMID:18993072] [10.1016/j.bmcl.2008.10.100]
7. Bertucci A, Innocenti A, Zoccola D, Scozzafava A, Allemand D, Tambutté S, Supuran CT..  (2009)  Carbonic anhydrase inhibitors: inhibition studies of a coral secretory isoform with inorganic anions.,  19  (3): [PMID:19121582] [10.1016/j.bmcl.2008.12.056]
8. Innocenti A, Leewattanapasuk W, Mühlschlegel FA, Mastrolorenzo A, Supuran CT..  (2009)  Carbonic anhydrase inhibitors. Inhibition of the beta-class enzyme from the pathogenic yeast Candida glabrata with anions.,  19  (16): [PMID:19574046] [10.1016/j.bmcl.2009.06.048]
9. Bertucci A, Innocenti A, Scozzafava A, Tambutté S, Zoccola D, Supuran CT..  (2011)  Carbonic anhydrase inhibitors. Inhibition studies with anions and sulfonamides of a new cytosolic enzyme from the scleractinian coral Stylophora pistillata.,  21  (2): [PMID:21208801] [10.1016/j.bmcl.2010.11.124]
10. 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]
11. 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]
12. 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]
13. 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]
14. Nishimori I, Vullo D, Minakuchi T, Scozzafava A, Capasso C, Supuran CT..  (2013)  Restoring catalytic activity to the human carbonic anhydrase (CA) related proteins VIII, X and XI affords isoforms with high catalytic efficiency and susceptibility to anion inhibition.,  23  (1): [PMID:23200251] [10.1016/j.bmcl.2012.10.103]
15. 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]
16. 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]
17. 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]
18. 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]
19. 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]
20. 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]
21. 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]
22. 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]
23. 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]
24. 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]
25. 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]
26. Vullo D, Del Prete S, De Luca V, Carginale V, Ferraroni M, Dedeoglu N, Osman SM, AlOthman Z, Capasso C, Supuran CT..  (2016)  Anion inhibition studies of the β-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae.,  26  (5): [PMID:26853167] [10.1016/j.bmcl.2016.01.072]
27. 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 α-, β- and γ-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae.,  24  (16): [PMID:27283786] [10.1016/j.bmc.2016.05.029]
28. 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]
29. 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]
30. 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]
31. 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]

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