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BioAssay: AID 730754

Inhibition of human carbonic anhydrase 1 preincubated for 15 mins by stopped flow CO2 hydration assay

An alpha-carbonic anhydrase (CA, EC 4.2.1.1) has been recently cloned and characterized in the human pathogenic bacterium Vibrio cholerae, denominated VchCA (Del Prete et al. J. Med. Chem.2012, 55, 10742). This enzyme shows a good catalytic activity for the CO2 hydration reaction, comparable to that of the human (h) isoform hCA I. Many inorganic anions and several small molecules were more ..
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 Tested Compounds
 Tested Compounds
All(32)
 
 
Active(6)
 
 
Unspecified(26)
 
 
 Tested Substances
 Tested Substances
All(35)
 
 
Active(6)
 
 
Unspecified(29)
 
 
 Related BioAssays
 Related BioAssays
AID: 730754
Data Source: ChEMBL (943322)
Depositor Category: Literature, Extracted
Deposit Date: 2013-11-07

Data Table ( Complete ):           Active    All
Target
Sequence: RecName: Full=Carbonic anhydrase 1; AltName: Full=Carbonate dehydratase I; AltName: Full=Carbonic anhydrase B; Short=CAB; AltName: Full=Carbonic anhydrase I; Short=CA-I
Description ..   
Protein Family: alpha_CA_I_II_III_XIII
Comment ..   

Gene:CA1     Related Protein 3D Structures     More BioActivity Data..
BioActive Compounds: 6
Description:
Title: Anion inhibition studies of the alpha-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae.

Abstract: An alpha-carbonic anhydrase (CA, EC 4.2.1.1) has been recently cloned and characterized in the human pathogenic bacterium Vibrio cholerae, denominated VchCA (Del Prete et al. J. Med. Chem.2012, 55, 10742). This enzyme shows a good catalytic activity for the CO2 hydration reaction, comparable to that of the human (h) isoform hCA I. Many inorganic anions and several small molecules were investigated as VchCA inhibitors. Inorganic anions such as cyanate, cyanide, hydrogen sulfide, hydrogen sulfite, and trithiocarbonate were effective VchCA inhibitors with inhibition constants in the range of 33-88muM. Other effective inhibitors were diethyldithiocarbamate, sulfamide, sulfamate, phenylboronic acid and phenylarsonic acid, with KIs of 7-43muM. Halides (bromide, iodide), bicarbonate and carbonate were much less effective VchCA inhibitors, with KIs in the range of 4.64-28.0mM. The resistance of VchCA to bicarbonate inhibition may represent an evolutionary adaptation of this enzyme to living in an environment rich in this ion, such as the gastrointestinal tract, as bicarbonate is a virulence enhancer of this bacterium.
(PMID: 23414807)
Comment
Compounds with activity <= 50uM or explicitly reported as active by ChEMBL are flagged as active in this PubChem assay presentation.

Categorized Comment
ChEMBL Assay Type: Binding

ChEMBL Assay Data Source: Scientific Literature

ChEMBL Target ID: 10193

ChEMBL Target Type: Target is a single protein chain

Result Definitions
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TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Ki*Ki PubChem standard valueFloatμM
2BEIBinding Efficiency Index(nM)Float
3SEISurface Efficiency Index(nM)Float
4LELigand EfficiencyFloat
5LLELipophilic Ligand EfficiencyFloat
6Ki activity commentKi activity commentString
7Ki standard flagKi standard flagInteger
8Ki qualifierKi qualifierString
9Ki published valueKi published valueFloatmM
10Ki standard valueKi standard valueFloatnM
11Ki data validityKi data validityString
12Ki binding domainsKi binding domainsString

* Activity Concentration.

Data Table (Concise)
Classification
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