Compounds > 2,4-dichloro-5-sulfamoylbenzoic acid
Page last updated: 2024-11-05

2,4-dichloro-5-sulfamoylbenzoic acid

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Description

2,4-dichloro-5-sulfamoylbenzoic acid, also known as diclofenac, is a nonsteroidal anti-inflammatory drug (NSAID) commonly used to treat pain and inflammation. Its synthesis involves a series of steps, starting with the reaction of 2,4-dichlorobenzoic acid with sulfamic acid. Diclofenac exerts its effects by inhibiting the production of prostaglandins, which are chemicals that promote pain and inflammation. It is widely studied for its potential therapeutic benefits in conditions such as rheumatoid arthritis, osteoarthritis, and acute pain. The compound's effectiveness, safety profile, and potential interactions with other medications continue to be a focus of research.'

2,4-dichloro-5-sulfamoylbenzoic acid: used in the manufacture of furosemide; occupational asthma and rhinitis was observed in workers from a lasamide production line [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID17655
CHEMBL ID120886
SCHEMBL ID574023
MeSH IDM0509332

Synonyms (50)

Synonym
EN300-16167
OPREA1_168593
benzoic acid, 2,4-dichloro-5-sulfamoyl-
m 12325
2,4-dichloro-5-sulphamoylbenzoic acid
einecs 220-358-3
5-aminosulfonyl-2,4-dichlorobenzoic acid
3-sulfamoyl-4,6-dichlorobenzoic acid
5-carboxy-2,4-dichlorobenzenesulfonamide
brn 2219046
OPREA1_483230
5-(aminosulfonyl)-2,4-dichlorobenzoic acid
benzoic acid, 5-(aminosulfonyl)-2,4-dichloro-
inchi=1/c7h5cl2no4s/c8-4-2-5(9)6(15(10,13)14)1-3(4)7(11)12/h1-2h,(h,11,12)(h2,10,13,14
STK298896
2736-23-4
leadquest compound 9
bdbm13075
2,4-dichloro-5-sulfamoylbenzoic acid
AC-11765
AKOS000143948
CHEMBL120886
F1901-0102
D2541
ec 220-358-3
unii-leg53tf0sn
leg53tf0sn ,
lasamide
2,4-dichloro-5-sulfamoyl-benzoic acid
BBL010665
BP-12719
FT-0610019
AM84865
furosemide impurity b [ep impurity]
SCHEMBL574023
2,4-dichloro-5-sulfonamidobenzoic acid
ZSHHRBYVHTVRFK-UHFFFAOYSA-N
W-107116
DTXSID90181791
SR-01000537051-1
sr-01000537051
mfcd00007931
furosemide imp. b (ep); 2,4-dichloro-5-sulphamoylbenzoic acid; furosemide impurity b
AS-10817
D70121
Q27282949
SY049410
CS-W014032
Z53021521
PD129784
[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)
Carbonic anhydrase 1Homo sapiens (human)IC50 (µMol)7.12000.00582.14107.9000AID1802976; AID1802977; AID1802978; AID461088; AID461322; AID461324
Carbonic anhydrase 2Homo sapiens (human)IC50 (µMol)981,406,668,125.10840.00021.10608.3000AID1796991; AID1802976; AID1802977; AID1802978; AID461089; AID461323; AID461325; AID48105
[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)
Carbonic anhydrase 12Homo sapiens (human)Kd0.31410.00070.29432.0000AID1361375; AID1361390; AID1520076; AID1520088
Carbonic anhydrase 1Homo sapiens (human)Kd25.07500.00071.368910.0000AID1361366; AID1361381; AID1520067; AID1520079
Carbonic anhydrase 2Homo sapiens (human)Kd0.16600.00000.41575.5500AID1361367; AID1361382; AID1520068; AID1520080
Carbonic anhydrase 3Homo sapiens (human)Kd5.52920.00841.18044.6000AID1361368; AID1361383; AID1520069; AID1520081
Carbonic anhydrase 4Homo sapiens (human)Kd0.75070.00030.30841.5000AID1361369; AID1361384; AID1520070; AID1520082
Carbonic anhydrase 6Homo sapiens (human)Kd2.00050.00100.71724.0000AID1361372; AID1361387; AID1520073; AID1520085
Carbonic anhydrase 5A, mitochondrialHomo sapiens (human)Kd10.02100.00700.38641.0000AID1361370; AID1361385; AID1520071; AID1520083
Carbonic anhydrase 7Homo sapiens (human)Kd0.05530.00010.37616.6700AID1361373; AID1361388; AID1520074; AID1520086
Carbonic anhydrase 9Homo sapiens (human)Kd0.33460.00060.13420.6700AID1361374; AID1361389; AID1520075; AID1520087
Carbonic anhydrase 13Homo sapiens (human)Kd0.16620.00070.384910.0000AID1361376; AID1361391; AID1520077; AID1520089
Carbonic anhydrase 14Homo sapiens (human)Kd0.22080.00040.09510.4420AID1361377; AID1361392; AID1520078; AID1520090
Carbonic anhydrase 5B, mitochondrialHomo sapiens (human)Kd1.25190.00050.53992.5000AID1361371; AID1361386; AID1520072; AID1520084
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (20)

Processvia Protein(s)Taxonomy
estrous cycleCarbonic anhydrase 12Homo sapiens (human)
chloride ion homeostasisCarbonic anhydrase 12Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 12Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 1Homo sapiens (human)
morphogenesis of an epitheliumCarbonic anhydrase 2Homo sapiens (human)
positive regulation of synaptic transmission, GABAergicCarbonic anhydrase 2Homo sapiens (human)
positive regulation of cellular pH reductionCarbonic anhydrase 2Homo sapiens (human)
angiotensin-activated signaling pathwayCarbonic anhydrase 2Homo sapiens (human)
regulation of monoatomic anion transportCarbonic anhydrase 2Homo sapiens (human)
secretionCarbonic anhydrase 2Homo sapiens (human)
regulation of intracellular pHCarbonic anhydrase 2Homo sapiens (human)
neuron cellular homeostasisCarbonic anhydrase 2Homo sapiens (human)
positive regulation of dipeptide transmembrane transportCarbonic anhydrase 2Homo sapiens (human)
regulation of chloride transportCarbonic anhydrase 2Homo sapiens (human)
carbon dioxide transportCarbonic anhydrase 2Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 2Homo sapiens (human)
response to bacteriumCarbonic anhydrase 3Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 3Homo sapiens (human)
bicarbonate transportCarbonic anhydrase 4Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 4Homo sapiens (human)
detection of chemical stimulus involved in sensory perception of bitter tasteCarbonic anhydrase 6Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 6Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 5A, mitochondrialHomo sapiens (human)
positive regulation of synaptic transmission, GABAergicCarbonic anhydrase 7Homo sapiens (human)
positive regulation of cellular pH reductionCarbonic anhydrase 7Homo sapiens (human)
neuron cellular homeostasisCarbonic anhydrase 7Homo sapiens (human)
regulation of chloride transportCarbonic anhydrase 7Homo sapiens (human)
regulation of intracellular pHCarbonic anhydrase 7Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 7Homo sapiens (human)
response to hypoxiaCarbonic anhydrase 9Homo sapiens (human)
morphogenesis of an epitheliumCarbonic anhydrase 9Homo sapiens (human)
response to xenobiotic stimulusCarbonic anhydrase 9Homo sapiens (human)
response to testosteroneCarbonic anhydrase 9Homo sapiens (human)
secretionCarbonic anhydrase 9Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 9Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 13Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 14Homo sapiens (human)
response to bacteriumCarbonic anhydrase 5B, mitochondrialHomo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 5B, mitochondrialHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (8)

Processvia Protein(s)Taxonomy
zinc ion bindingCarbonic anhydrase 12Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 12Homo sapiens (human)
arylesterase activityCarbonic anhydrase 1Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 1Homo sapiens (human)
protein bindingCarbonic anhydrase 1Homo sapiens (human)
zinc ion bindingCarbonic anhydrase 1Homo sapiens (human)
hydro-lyase activityCarbonic anhydrase 1Homo sapiens (human)
cyanamide hydratase activityCarbonic anhydrase 1Homo sapiens (human)
arylesterase activityCarbonic anhydrase 2Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 2Homo sapiens (human)
protein bindingCarbonic anhydrase 2Homo sapiens (human)
zinc ion bindingCarbonic anhydrase 2Homo sapiens (human)
cyanamide hydratase activityCarbonic anhydrase 2Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 3Homo sapiens (human)
protein bindingCarbonic anhydrase 3Homo sapiens (human)
zinc ion bindingCarbonic anhydrase 3Homo sapiens (human)
nickel cation bindingCarbonic anhydrase 3Homo sapiens (human)
protein bindingCarbonic anhydrase 4Homo sapiens (human)
zinc ion bindingCarbonic anhydrase 4Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 4Homo sapiens (human)
zinc ion bindingCarbonic anhydrase 6Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 6Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 5A, mitochondrialHomo sapiens (human)
zinc ion bindingCarbonic anhydrase 5A, mitochondrialHomo sapiens (human)
zinc ion bindingCarbonic anhydrase 7Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 7Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 9Homo sapiens (human)
protein bindingCarbonic anhydrase 9Homo sapiens (human)
zinc ion bindingCarbonic anhydrase 9Homo sapiens (human)
molecular function activator activityCarbonic anhydrase 9Homo sapiens (human)
protein bindingCarbonic anhydrase 13Homo sapiens (human)
zinc ion bindingCarbonic anhydrase 13Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 13Homo sapiens (human)
zinc ion bindingCarbonic anhydrase 14Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 14Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 5B, mitochondrialHomo sapiens (human)
zinc ion bindingCarbonic anhydrase 5B, mitochondrialHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (26)

Processvia Protein(s)Taxonomy
plasma membraneCarbonic anhydrase 12Homo sapiens (human)
membraneCarbonic anhydrase 12Homo sapiens (human)
basolateral plasma membraneCarbonic anhydrase 12Homo sapiens (human)
apical plasma membraneCarbonic anhydrase 12Homo sapiens (human)
plasma membraneCarbonic anhydrase 12Homo sapiens (human)
cytosolCarbonic anhydrase 1Homo sapiens (human)
extracellular exosomeCarbonic anhydrase 1Homo sapiens (human)
cytoplasmCarbonic anhydrase 2Homo sapiens (human)
cytosolCarbonic anhydrase 2Homo sapiens (human)
plasma membraneCarbonic anhydrase 2Homo sapiens (human)
myelin sheathCarbonic anhydrase 2Homo sapiens (human)
apical part of cellCarbonic anhydrase 2Homo sapiens (human)
extracellular exosomeCarbonic anhydrase 2Homo sapiens (human)
cytoplasmCarbonic anhydrase 2Homo sapiens (human)
plasma membraneCarbonic anhydrase 2Homo sapiens (human)
apical part of cellCarbonic anhydrase 2Homo sapiens (human)
cytosolCarbonic anhydrase 3Homo sapiens (human)
cytosolCarbonic anhydrase 3Homo sapiens (human)
cytoplasmCarbonic anhydrase 3Homo sapiens (human)
basolateral plasma membraneCarbonic anhydrase 4Homo sapiens (human)
rough endoplasmic reticulumCarbonic anhydrase 4Homo sapiens (human)
endoplasmic reticulum-Golgi intermediate compartmentCarbonic anhydrase 4Homo sapiens (human)
Golgi apparatusCarbonic anhydrase 4Homo sapiens (human)
trans-Golgi networkCarbonic anhydrase 4Homo sapiens (human)
plasma membraneCarbonic anhydrase 4Homo sapiens (human)
external side of plasma membraneCarbonic anhydrase 4Homo sapiens (human)
cell surfaceCarbonic anhydrase 4Homo sapiens (human)
membraneCarbonic anhydrase 4Homo sapiens (human)
apical plasma membraneCarbonic anhydrase 4Homo sapiens (human)
transport vesicle membraneCarbonic anhydrase 4Homo sapiens (human)
secretory granule membraneCarbonic anhydrase 4Homo sapiens (human)
brush border membraneCarbonic anhydrase 4Homo sapiens (human)
perinuclear region of cytoplasmCarbonic anhydrase 4Homo sapiens (human)
extracellular exosomeCarbonic anhydrase 4Homo sapiens (human)
plasma membraneCarbonic anhydrase 4Homo sapiens (human)
extracellular regionCarbonic anhydrase 6Homo sapiens (human)
extracellular spaceCarbonic anhydrase 6Homo sapiens (human)
cytosolCarbonic anhydrase 6Homo sapiens (human)
extracellular exosomeCarbonic anhydrase 6Homo sapiens (human)
extracellular spaceCarbonic anhydrase 6Homo sapiens (human)
mitochondrial matrixCarbonic anhydrase 5A, mitochondrialHomo sapiens (human)
mitochondrionCarbonic anhydrase 5A, mitochondrialHomo sapiens (human)
cytoplasmCarbonic anhydrase 5A, mitochondrialHomo sapiens (human)
mitochondrionCarbonic anhydrase 5A, mitochondrialHomo sapiens (human)
cytosolCarbonic anhydrase 7Homo sapiens (human)
cytoplasmCarbonic anhydrase 7Homo sapiens (human)
nucleolusCarbonic anhydrase 9Homo sapiens (human)
plasma membraneCarbonic anhydrase 9Homo sapiens (human)
membraneCarbonic anhydrase 9Homo sapiens (human)
basolateral plasma membraneCarbonic anhydrase 9Homo sapiens (human)
microvillus membraneCarbonic anhydrase 9Homo sapiens (human)
plasma membraneCarbonic anhydrase 9Homo sapiens (human)
cytosolCarbonic anhydrase 13Homo sapiens (human)
myelin sheathCarbonic anhydrase 13Homo sapiens (human)
intracellular membrane-bounded organelleCarbonic anhydrase 13Homo sapiens (human)
cytoplasmCarbonic anhydrase 13Homo sapiens (human)
cytosolCarbonic anhydrase 13Homo sapiens (human)
plasma membraneCarbonic anhydrase 14Homo sapiens (human)
membraneCarbonic anhydrase 14Homo sapiens (human)
basolateral plasma membraneCarbonic anhydrase 14Homo sapiens (human)
apical plasma membraneCarbonic anhydrase 14Homo sapiens (human)
plasma membraneCarbonic anhydrase 14Homo sapiens (human)
mitochondrionCarbonic anhydrase 5B, mitochondrialHomo sapiens (human)
mitochondrial matrixCarbonic anhydrase 5B, mitochondrialHomo sapiens (human)
mitochondrionCarbonic anhydrase 5B, mitochondrialHomo sapiens (human)
cytoplasmCarbonic anhydrase 5B, mitochondrialHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (60)

Assay IDTitleYearJournalArticle
AID1520071Binding affinity to recombinant human carbonic anhydrase 5a expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1520068Binding affinity to recombinant human carbonic anhydrase 2 expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361377Binding affinity to recombinant N-terminal His6-tagged human carbonic anhydrase 14 (20 to 280 residues) expressed in Escherichia coli Rosetta2 (DE3) strain in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID48105Binding activity against human Carbonic anhydrase II (hCAII)2002Journal of medicinal chemistry, Aug-15, Volume: 45, Issue:17
Successful virtual screening for novel inhibitors of human carbonic anhydrase: strategy and experimental confirmation.
AID461322Inhibition of esterase-activity of CA1 from human erythrocytes by spectrophotometry2010Bioorganic & medicinal chemistry, Jan-15, Volume: 18, Issue:2
Synthesis, characterization and antiglaucoma activity of a novel proton transfer compound and a mixed-ligand Zn(II) complex.
AID1361370Binding affinity to recombinant C-terminal His6-tagged full-length human carbonic anhydrase 5A expressed in Escherichia coli BL21 (DE3) strain in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1361389Binding affinity to recombinant human carbonic anhydrase 9 (38 to 414 residues) expressed in 293-F cells assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520087Binding affinity to recombinant human carbonic anhydrase 9 expressed in mammalian cell expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1520086Binding affinity to recombinant human carbonic anhydrase 7 expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361368Binding affinity to recombinant human carbonic anhydrase 3 (4 to 260 residues) expressed in Escherichia coli BL21 (DE3) strain in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520075Binding affinity to recombinant human carbonic anhydrase 9 expressed in mammalian cell expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1520076Binding affinity to recombinant human carbonic anhydrase 12 expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361384Binding affinity to recombinant human carbonic anhydrase 4 (19 to 284 residues) expressed in mammalian expression system assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520080Binding affinity to recombinant human carbonic anhydrase 2 expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361392Binding affinity to recombinant N-terminal His6-tagged human carbonic anhydrase 14 (20 to 280 residues) expressed in Escherichia coli Rosetta2 (DE3) strain assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520084Binding affinity to recombinant human carbonic anhydrase 5b expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361374Binding affinity to recombinant human carbonic anhydrase 9 (38 to 414 residues) expressed in 293-F cells in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520069Binding affinity to recombinant human carbonic anhydrase 3 expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1520067Binding affinity to recombinant human carbonic anhydrase 1 expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361375Binding affinity to recombinant human carbonic anhydrase 12 (30 to 291 residues) expressed in Escherichia coli Rosetta 2 (DE3) strain in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID461323Inhibition of esterase-activity of human erythrocytes CA2 by spectrophotometry2010Bioorganic & medicinal chemistry, Jan-15, Volume: 18, Issue:2
Synthesis, characterization and antiglaucoma activity of a novel proton transfer compound and a mixed-ligand Zn(II) complex.
AID1361385Binding affinity to recombinant C-terminal His6-tagged full-length human carbonic anhydrase 5A expressed in Escherichia coli BL21 (DE3) strain assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID461089Inhibition of hydratase-activity of human erythrocytes CA2 by CO2-hydration method2010Bioorganic & medicinal chemistry, Jan-15, Volume: 18, Issue:2
Synthesis, characterization and antiglaucoma activity of a novel proton transfer compound and a mixed-ligand Zn(II) complex.
AID1520105Dissociation constant, pKa of compound by UV-vis spectroscopy2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1520073Binding affinity to recombinant human carbonic anhydrase 6 expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361387Binding affinity to recombinant N-terminal His6-tagged human carbonic anhydrase 6 (21 to 290 residues) expressed in Escherichia coli Rosetta 2 (DE3) strain assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID461325Inhibition of human erythrocytes CA2 by Lineweaver-Burke analysis2010Bioorganic & medicinal chemistry, Jan-15, Volume: 18, Issue:2
Synthesis, characterization and antiglaucoma activity of a novel proton transfer compound and a mixed-ligand Zn(II) complex.
AID1361383Binding affinity to recombinant human carbonic anhydrase 3 (4 to 260 residues) expressed in Escherichia coli BL21 (DE3) strain assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520090Binding affinity to recombinant human carbonic anhydrase 14 expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361372Binding affinity to recombinant N-terminal His6-tagged human carbonic anhydrase 6 (21 to 290 residues) expressed in Escherichia coli Rosetta 2 (DE3) strain in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1361371Binding affinity to recombinant N-terminal His6-tagged human carbonic anhydrase 5B (40 to 317 residues) expressed in Escherichia coli Rosetta 2 (DE3) strain in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1361367Binding affinity to recombinant full-length human carbonic anhydrase 2 expressed in Escherichia coli in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520085Binding affinity to recombinant human carbonic anhydrase 6 expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1520082Binding affinity to recombinant human carbonic anhydrase 4 expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1520078Binding affinity to recombinant human carbonic anhydrase 14 expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361382Binding affinity to recombinant full-length human carbonic anhydrase 2 expressed in Escherichia coli assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520077Binding affinity to recombinant human carbonic anhydrase 13 expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1520088Binding affinity to recombinant human carbonic anhydrase 12 expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361391Binding affinity to recombinant human carbonic anhydrase 13 (1 to 262 residues) expressed in Escherichia coli Rosetta 2 (DE3) strain assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520070Binding affinity to recombinant human carbonic anhydrase 4 expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361381Binding affinity to recombinant human carbonic anhydrase 1 expressed in Escherichia coli assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1361390Binding affinity to recombinant human carbonic anhydrase 12 (30 to 291 residues) expressed in Escherichia coli Rosetta 2 (DE3) strain assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1361366Binding affinity to recombinant human carbonic anhydrase 1 expressed in Escherichia coli in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520081Binding affinity to recombinant human carbonic anhydrase 3 expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1520089Binding affinity to recombinant human carbonic anhydrase 13 expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361388Binding affinity to recombinant N-terminal His-tagged human carbonic anhydrase 7 (3 to 264 residues) expressed in Escherichia coli BL21 (DE3) strain assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1361369Binding affinity to recombinant human carbonic anhydrase 4 (19 to 284 residues) expressed in mammalian expression system in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1361386Binding affinity to recombinant N-terminal His6-tagged human carbonic anhydrase 5B (40 to 317 residues) expressed in Escherichia coli Rosetta 2 (DE3) strain assessed as intrinsic Kd in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520079Binding affinity to recombinant human carbonic anhydrase 1 expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID461088Inhibition of hydratase-activity of CA1 from human erythrocytes by CO2-hydration method2010Bioorganic & medicinal chemistry, Jan-15, Volume: 18, Issue:2
Synthesis, characterization and antiglaucoma activity of a novel proton transfer compound and a mixed-ligand Zn(II) complex.
AID1520072Binding affinity to recombinant human carbonic anhydrase 5b expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1520083Binding affinity to recombinant human carbonic anhydrase 5a expressed in Escherichia coli expression system assessed as kinetic dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID1361373Binding affinity to recombinant N-terminal His-tagged human carbonic anhydrase 7 (3 to 264 residues) expressed in Escherichia coli BL21 (DE3) strain in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1520074Binding affinity to recombinant human carbonic anhydrase 7 expressed in Escherichia coli expression system assessed as observed dissociation constant fluorescent thermal shift assay2020European journal of medicinal chemistry, Jan-01, Volume: 185Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.
AID461324Inhibition of CA1 from human erythrocytes by Lineweaver-Burke analysis2010Bioorganic & medicinal chemistry, Jan-15, Volume: 18, Issue:2
Synthesis, characterization and antiglaucoma activity of a novel proton transfer compound and a mixed-ligand Zn(II) complex.
AID1361376Binding affinity to recombinant human carbonic anhydrase 13 (1 to 262 residues) expressed in Escherichia coli Rosetta 2 (DE3) strain in presence of ANS by fluorescent thermal shift assay2018European journal of medicinal chemistry, Aug-05, Volume: 156Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.
AID1802976Hydratase Activity Assay from Article 10.3109/14756361003733639: \\Synthesis and characterisation of two novel proton transfer compounds and their inhibition studies on carbonic anhydrase isoenzymes.\\2011Journal of enzyme inhibition and medicinal chemistry, Feb, Volume: 26, Issue:1
Synthesis and characterisation of two novel proton transfer compounds and their inhibition studies on carbonic anhydrase isoenzymes.
AID1802977Esterase Activity Assay from Article 10.3109/14756361003733639: \\Synthesis and characterisation of two novel proton transfer compounds and their inhibition studies on carbonic anhydrase isoenzymes.\\2011Journal of enzyme inhibition and medicinal chemistry, Feb, Volume: 26, Issue:1
Synthesis and characterisation of two novel proton transfer compounds and their inhibition studies on carbonic anhydrase isoenzymes.
AID1802978Enzyme Activity Assay from Article 10.3109/14756361003733639: \\Synthesis and characterisation of two novel proton transfer compounds and their inhibition studies on carbonic anhydrase isoenzymes.\\2011Journal of enzyme inhibition and medicinal chemistry, Feb, Volume: 26, Issue:1
Synthesis and characterisation of two novel proton transfer compounds and their inhibition studies on carbonic anhydrase isoenzymes.
AID1796991Carbonic Anhydrase Enzyme Inhibition Assay from Article 10.1021/jm011112j: \\Successful virtual screening for novel inhibitors of human carbonic anhydrase: strategy and experimental confirmation.\\2002Journal of medicinal chemistry, Aug-15, Volume: 45, Issue:17
Successful virtual screening for novel inhibitors of human carbonic anhydrase: strategy and experimental confirmation.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (8)

TimeframeStudies, This Drug (%)All Drugs %
pre-19901 (12.50)18.7374
1990's0 (0.00)18.2507
2000's2 (25.00)29.6817
2010's4 (50.00)24.3611
2020's1 (12.50)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 21.52

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 moderate demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index21.52 (24.57)
Research Supply Index2.20 (2.92)
Research Growth Index4.42 (4.65)
Search Engine Demand Index18.60 (26.88)
Search Engine Supply Index2.00 (0.95)

This Compound (21.52)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies1 (12.50%)4.05%
Observational0 (0.00%)0.25%
Other7 (87.50%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]
SubstanceRelationship StrengthStudiesTrialsClassesRoles
acetazolamide
Acetazolamide: One of the CARBONIC ANHYDRASE INHIBITORS that is sometimes effective against absence seizures. It is sometimes useful also as an adjunct in the treatment of tonic-clonic, myoclonic, and atonic seizures, particularly in women whose seizures occur or are exacerbated at specific times in the menstrual cycle. However, its usefulness is transient often because of rapid development of tolerance. Its antiepileptic effect may be due to its inhibitory effect on brain carbonic anhydrase, which leads to an increased transneuronal chloride gradient, increased chloride current, and increased inhibition. (From Smith and Reynard, Textbook of Pharmacology, 1991, p337)		2.9840monocarboxylic acid amide;
sulfonamide;
thiadiazoles		anticonvulsant;
diuretic;
EC 4.2.1.1 (carbonic anhydrase) inhibitor
acetohydroxamic acid
acetohydroxamic acid: urease inhibitor. oxime : Compounds of structure R2C=NOH derived from condensation of aldehydes or ketones with hydroxylamine. Oximes from aldehydes may be called aldoximes; those from ketones may be called ketoximes.. N-hydroxyacetimidic acid : A carbohydroximic acid consisting of acetimidic acid having a hydroxy group attached to the imide nitrogen.. acetohydroxamic acid : A member of the class of acetohydroxamic acids that is acetamide in which one of the amino hydrogens has been replaced by a hydroxy group.		2.0110acetohydroxamic acids;
carbohydroximic acid		algal metabolite;
EC 3.5.1.5 (urease) inhibitor
amantadine
amant: an antiviral compound consisting of an adamantane derivative chemically linked to a water-solube polyanioic matrix; structure in first source		1.9610adamantanes;
primary aliphatic amine		analgesic;
antiparkinson drug;
antiviral drug;
dopaminergic agent;
NMDA receptor antagonist;
non-narcotic analgesic
dichlorphenamide
Dichlorphenamide: A carbonic anhydrase inhibitor that is used in the treatment of glaucoma.. diclofenamide : A sulfonamide that is benzene-1,3-disulfonamide in which the hydrogens at positions 4 and 5 are substituted by chlorine. An oral carbonic anhydrase inhibitor, it partially suppresses the secretion (inflow) of aqueous humor in the eye and so reduces intraocular pressure. It is used for the treatment of glaucoma.		2.0110dichlorobenzene;
sulfonamide		antiglaucoma drug;
EC 4.2.1.1 (carbonic anhydrase) inhibitor;
ophthalmology drug
ethylenediamine
ethylenediamine: RN given refers to parent cpd; edamine is the recommended contraction for the ethylenediamine radical. ethylenediamine : An alkane-alpha,omega-diamine in which the alkane is ethane.		2.0610alkane-alpha,omega-diamineGABA agonist
hydrochlorothiazide
Hydrochlorothiazide: A thiazide diuretic often considered the prototypical member of this class. It reduces the reabsorption of electrolytes from the renal tubules. This results in increased excretion of water and electrolytes, including sodium, potassium, chloride, and magnesium. It is used in the treatment of several disorders including edema, hypertension, diabetes insipidus, and hypoparathyroidism.. hydrochlorothiazide : A benzothiadiazine that is 3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide substituted by a chloro group at position 6 and a sulfonamide at 7. It is diuretic used for the treatment of hypertension and congestive heart failure.		2.0110benzothiadiazine;
organochlorine compound;
sulfonamide		antihypertensive agent;
diuretic;
environmental contaminant;
xenobiotic
methazolamide
Methazolamide: A carbonic anhydrase inhibitor that is used as a diuretic and in the treatment of glaucoma.		2.0110sulfonamide;
thiadiazoles
alpha-aminopyridine
alpha-aminopyridine: RN given refers to parent cpd; structure in Merck Index, 9th ed, #485. aminopyridine : Compounds containing a pyridine skeleton substituted by one or more amine groups.		2.0610
2-amino-3-methylpyridine
2-amino-3-methylpyridine: structure in first source		2.0610
2-(aminomethyl)pyridine
[no description available]		2.0510pyridines
chlorine
Chlorine: An element with atomic symbol Cl, atomic number 17, and atomic weight 35, and member of the halogen family.		2.0710diatomic chlorine;
gas molecular entity		bleaching agent
sezolamide
sezolamide: decreases intraocular pressure, topically in vivo; inhibits carbonic anhydrase; RN given refers to parent cpd without isomeric designation		2.0110
5-dimethylaminonaphthalene-1-sulfonamide
[no description available]		2.0110
trifluoromethylsulfonamide
trifluoromethylsulfonamide: RN given refers to parent		2.0110
dorzolamide
dorzolamide: topically effective ocular hypotensive carbonic anhydrase inhibitor; RN refers to mono-HCl (4S-trans)-isomer. dorzolamide : 5,6-Dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide in which hydrogens at the 4 and 6 positions are substituted by ethylamino and methyl groups, respectively (4S, trans-configuration). A carbonic anhydrase inhibitor, it is used as the hydrochloride in ophthalmic solutions to lower increased intraocular pressure in the treatment of open-angle glaucoma and ocular hypertension.		2.0110sulfonamide;
thiophenes		antiglaucoma drug;
antihypertensive agent;
EC 4.2.1.1 (carbonic anhydrase) inhibitor
ConditionIndicatedRelationship StrengthStudiesTrials
Glaucoma
An ocular disease, occurring in many forms, having as its primary characteristics an unstable or a sustained increase in the intraocular pressure which the eye cannot withstand without damage to its structure or impairment of its function. The consequences of the increased pressure may be manifested in a variety of symptoms, depending upon type and severity, such as excavation of the optic disk, hardness of the eyeball, corneal anesthesia, reduced visual acuity, seeing of colored halos around lights, disturbed dark adaptation, visual field defects, and headaches. (Dictionary of Visual Science, 4th ed)		02.4620
Viral Diseases
[description not available]		01.9610
Virus Diseases
A general term for diseases caused by viruses.		01.9610
Asthma, Bronchial
[description not available]		02.0310
Diseases, Occupational
[description not available]		02.0310
Rhinitis, Allergic, Nonseasonal
[description not available]		02.0310
Asthma
A form of bronchial disorder with three distinct components: airway hyper-responsiveness (RESPIRATORY HYPERSENSITIVITY), airway INFLAMMATION, and intermittent AIRWAY OBSTRUCTION. It is characterized by spasmodic contraction of airway smooth muscle, WHEEZING, and dyspnea (DYSPNEA, PAROXYSMAL).		02.0310
Rhinitis, Allergic, Perennial
Inflammation of the mucous membrane of the nose similar to that found in hay fever except that symptoms persist throughout the year. The causes are usually air-borne allergens, particularly dusts, feathers, molds, animal fur, etc.		02.0310