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BioAssay: AID 577543

Ratio of kcat to Km for human carbonic anhydrase VA

A beta-carbonic anhydrase (CA, EC 4.2.1.1) from the bacterial pathogen Brucella suis, bsCA II, has been cloned, purified, and characterized kinetically. bsCA II showed high catalytic activity for the hydration of CO(2) to bicarbonate, with a k(cat) of 1.1#10(6), and k(cat)/K(m) of 8.9#10(7)M(-1)s(-1). A panel of sulfonamides and sulfamates have been investigated for inhibition of this enzyme. All more ..
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 Tested Compounds
 Tested Compounds
All(1)
 
 
Unspecified(1)
 
 
 Tested Substances
 Tested Substances
All(1)
 
 
Unspecified(1)
 
 
 Related BioAssays
 Related BioAssays
AID: 577543
Data Source: ChEMBL (726083)
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2011-09-18
Modify Date: 2014-05-27

Data Table ( Complete ):           View All Data
Target
Sequence: RecName: Full=Carbonic anhydrase 5A, mitochondrial; AltName: Full=Carbonate dehydratase VA; AltName: Full=Carbonic anhydrase VA; Short=CA-VA; Flags: Precursor
Description ..   
Protein Family: alpha_CA_V
Comment ..   

Gene:CA5A     Related Protein 3D Structures     More BioActivity Data..
Tested Compound:
Description:
Title: A new beta-carbonic anhydrase from Brucella suis, its cloning, characterization, and inhibition with sulfonamides and sulfamates, leading to impaired pathogen growth.

Abstract: A beta-carbonic anhydrase (CA, EC 4.2.1.1) from the bacterial pathogen Brucella suis, bsCA II, has been cloned, purified, and characterized kinetically. bsCA II showed high catalytic activity for the hydration of CO(2) to bicarbonate, with a k(cat) of 1.1#10(6), and k(cat)/K(m) of 8.9#10(7)M(-1)s(-1). A panel of sulfonamides and sulfamates have been investigated for inhibition of this enzyme. All types of activities, from the low nanomolar to the micromolar, have been detected for these derivatives, which showed inhibition constants in the range of 7.3nM-8.56muM. The best bsCA II inhibitors were some glycosylated sulfanilamides, aliphatic sulfamates, and halogenated sulfanilamides, with inhibition constants of 7.3-87nM. Some of these dual inhibitors of bsCA I and II, also inhibited bacterial growth in vitro, in liquid cultures. These promising data on live bacteria allow us to propose bacterial beta-CA inhibition as an approach for obtaining anti-infective agents with a new mechanism of action compared to classical antibiotics.
(PMID: 21251841)
Categorized Comment
Assay Type: Binding

Assay Data Source: Scientific Literature

BAO: Assay Format: biochemical format

Target Type: Target is a single protein chain

Protein Target Class: enzyme lyase

Result Definitions
TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Kcat/Km activity commentKcat/Km activity commentString
2Kcat/Km standard flagKcat/Km standard flagInteger
3Kcat/Km qualifierKcat/Km qualifierString
4Kcat/Km published valueKcat/Km published valueFloat10'7/M/s
5Kcat/Km standard valueKcat/Km standard valueFloat10'7/M/s

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