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BioAssay: AID 598728

Inhibition of recombinant human carbonic anhydrase 2 after 15 mins by stopped flow CO2 hydration assay at pH 8.3

Two new beta-carbonic anhydrases (CAs, EC 4.2.1.1) from the bacterial pathogen Salmonella enterica serovar Typhimurium, stCA 1 and stCA 2, were characterized kinetically. The two enzymes possess appreciable activity as catalysts for the hydration of CO(2) to bicarbonate, with k(cat) of 0.79#10(6) s(-1) and 1.0#10(6) s(-1), and k(cat)/K(m) of 5.2#10(7) M(-1) s(-1) and of 8.3#10(7) M(-1) s(-1), more ..
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 Tested Compounds
 Tested Compounds
All(34)
 
 
Active(5)
 
 
Unspecified(29)
 
 
 Tested Substances
 Tested Substances
All(38)
 
 
Active(5)
 
 
Unspecified(33)
 
 
AID: 598728
Data Source: ChEMBL (748879)
BioAssay Type: Confirmatory, Concentration-Response Relationship Observed
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2012-02-15
Modify Date: 2014-08-23

Data Table ( Complete ):           View Active Data    View All Data
Target
Sequence: RecName: Full=Carbonic anhydrase 2; AltName: Full=Carbonate dehydratase II; AltName: Full=Carbonic anhydrase C; Short=CAC; AltName: Full=Carbonic anhydrase II; Short=CA-II
Description ..   
Protein Family: alpha_CA_I_II_III_XIII
Comment ..   

Gene:CA2     Related Protein 3D Structures     More BioActivity Data..
BioActive Compounds: 5
Description:
Title: Inhibition studies with anions and small molecules of two novel beta-carbonic anhydrases from the bacterial pathogen Salmonella enterica serovar Typhimurium.

Abstract: Two new beta-carbonic anhydrases (CAs, EC 4.2.1.1) from the bacterial pathogen Salmonella enterica serovar Typhimurium, stCA 1 and stCA 2, were characterized kinetically. The two enzymes possess appreciable activity as catalysts for the hydration of CO(2) to bicarbonate, with k(cat) of 0.79#10(6) s(-1) and 1.0#10(6) s(-1), and k(cat)/K(m) of 5.2#10(7) M(-1) s(-1) and of 8.3#10(7) M(-1) s(-1), respectively. A large number of simple/complex inorganic anions as well as other small molecules (sulfamide, sulfamic acid, phenylboronic acid, phenylarsonic acid, dialkyldithiocarbamates) showed interesting inhibitory properties towards the two new enzymes, with several low micromolar inhibitors discovered. As many strains of S. enterica show extensive resistance to classical antibiotics, inhibition of the beta-CAs investigated here may be useful for developing lead compounds for novel types of antibacterials.
(PMID: 21570835)
Comment
Compounds with activity <= 50uM or explicitly reported as active by ChEMBL are flagged as active in this PubChem assay presentation.

Categorized Comment - additional comments and annotations
From BioAssay Depositor:
Assay Type: Binding
Target Type: Target is a single protein chain
Assay Data Source: Scientific Literature
Protein Target Class: enzyme lyase
Result Definitions
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TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Ki*Ki PubChem standard valueFloatμM
3BEIBinding Efficiency Index(nM)Float
2SEISurface 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
13Ki activity commentKi activity commentString
14Ki standard flagKi standard flagInteger
15Ki qualifierKi qualifierString
16Ki published valueKi published valueFloatnM
17Ki standard valueKi standard valueFloatnM
18Ki data validityKi data validityString
19Ki binding domainsKi binding domainsString

* Activity Concentration.

Data Table (Concise)
Data Table ( Complete ):     View Active Data    View All Data
Classification
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