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Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii
by
Del Prete, Sonia
, Capasso, Clemente
, Supuran, Claudiu T.
, Nocentini, Alessio
in
Acetazolamide
/ Acetazolamide - chemistry
/ Acetazolamide - pharmacology
/ Amino Acid Sequence
/ Antibiotic resistance
/ Bacteria
/ bacterial CA
/ Bicarbonates
/ Burkholderia
/ Burkholderia - enzymology
/ Burkholderia territorii
/ Carbon dioxide
/ Carbonic anhydrase
/ Carbonic Anhydrase Inhibitors - chemistry
/ Carbonic Anhydrase Inhibitors - pharmacology
/ Carbonic anhydrases
/ Carbonic Anhydrases - genetics
/ Carbonic Anhydrases - isolation & purification
/ Carbonic Anhydrases - metabolism
/ Catalysts
/ catalytic ion cofactor
/ Dose-Response Relationship, Drug
/ Drug resistance
/ Enzymes
/ Genomes
/ Homology
/ hydratase activity
/ Hydration
/ iota-CA
/ Models, Molecular
/ Molecular Structure
/ Monomers
/ Phylogeny
/ Protons
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Research Paper
/ Structure-Activity Relationship
/ Sulfonamides
/ Sulfonamides - chemistry
/ Sulfonamides - pharmacology
2020
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Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii
by
Del Prete, Sonia
, Capasso, Clemente
, Supuran, Claudiu T.
, Nocentini, Alessio
in
Acetazolamide
/ Acetazolamide - chemistry
/ Acetazolamide - pharmacology
/ Amino Acid Sequence
/ Antibiotic resistance
/ Bacteria
/ bacterial CA
/ Bicarbonates
/ Burkholderia
/ Burkholderia - enzymology
/ Burkholderia territorii
/ Carbon dioxide
/ Carbonic anhydrase
/ Carbonic Anhydrase Inhibitors - chemistry
/ Carbonic Anhydrase Inhibitors - pharmacology
/ Carbonic anhydrases
/ Carbonic Anhydrases - genetics
/ Carbonic Anhydrases - isolation & purification
/ Carbonic Anhydrases - metabolism
/ Catalysts
/ catalytic ion cofactor
/ Dose-Response Relationship, Drug
/ Drug resistance
/ Enzymes
/ Genomes
/ Homology
/ hydratase activity
/ Hydration
/ iota-CA
/ Models, Molecular
/ Molecular Structure
/ Monomers
/ Phylogeny
/ Protons
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Research Paper
/ Structure-Activity Relationship
/ Sulfonamides
/ Sulfonamides - chemistry
/ Sulfonamides - pharmacology
2020
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Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii
by
Del Prete, Sonia
, Capasso, Clemente
, Supuran, Claudiu T.
, Nocentini, Alessio
in
Acetazolamide
/ Acetazolamide - chemistry
/ Acetazolamide - pharmacology
/ Amino Acid Sequence
/ Antibiotic resistance
/ Bacteria
/ bacterial CA
/ Bicarbonates
/ Burkholderia
/ Burkholderia - enzymology
/ Burkholderia territorii
/ Carbon dioxide
/ Carbonic anhydrase
/ Carbonic Anhydrase Inhibitors - chemistry
/ Carbonic Anhydrase Inhibitors - pharmacology
/ Carbonic anhydrases
/ Carbonic Anhydrases - genetics
/ Carbonic Anhydrases - isolation & purification
/ Carbonic Anhydrases - metabolism
/ Catalysts
/ catalytic ion cofactor
/ Dose-Response Relationship, Drug
/ Drug resistance
/ Enzymes
/ Genomes
/ Homology
/ hydratase activity
/ Hydration
/ iota-CA
/ Models, Molecular
/ Molecular Structure
/ Monomers
/ Phylogeny
/ Protons
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Research Paper
/ Structure-Activity Relationship
/ Sulfonamides
/ Sulfonamides - chemistry
/ Sulfonamides - pharmacology
2020
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Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii
Journal Article
Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii
2020
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Overview
The carbonic anhydrases (CAs, EC 4.2.1.1) catalyse a simple but physiologically crucial reversible reaction, the carbon dioxide hydration with the production of bicarbonate and protons. In the last years, and especially, to the rapid emergence of the bacterial antibiotic resistance that is occurring worldwide, the understanding of the function of bacterial CAs has increased significantly. Recently, a new CA-class (ι-CA) was discovered in the marine diatom T. pseudonana. It has been reported that bacterial genomes may contain genes with relevant homology to the diatom ι-class CA. Still, the catalytic activity of the enzyme encoded by the gene was not investigated. Thus, herein, for the first time, we cloned, expressed, and purified the recombinant bacterial ι-CA (acronym BteCAι) identified in the genome of Burkholderia territorii. The recombinant BteCAι resulted in a good catalyst for the hydration of CO
2
to bicarbonate and protons, with a k
cat
of 3.0 × 10
5
s
−1
and k
cat
/K
M
of 3.9 × 10
7
M
−1
s
−1
, and is also sensitive to inhibition by the sulphonamide acetazolamide. Furthermore, with the aid of the protonography, it has been demonstrated that BteCAι can be present as a dimer. This result is corroborated by the construction of a molecular model of BteCAι, which showed that the enzyme is formed by two equivalent monomers having a structure similar to a butterfly.
Publisher
Taylor & Francis,Taylor & Francis Ltd,Taylor & Francis Group
Subject
/ Acetazolamide - pharmacology
/ Bacteria
/ Carbonic Anhydrase Inhibitors - chemistry
/ Carbonic Anhydrase Inhibitors - pharmacology
/ Carbonic Anhydrases - genetics
/ Carbonic Anhydrases - isolation & purification
/ Carbonic Anhydrases - metabolism
/ Dose-Response Relationship, Drug
/ Enzymes
/ Genomes
/ Homology
/ iota-CA
/ Monomers
/ Protons
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
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