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Bacterial ι-CAs.

Clemente Capasso1, Claudiu T Supuran2

  • 1Department of Biology, Agriculture and Food Sciences, Institute of Biosciences and Bioresources, CNR, Napoli, Italy.

The Enzymes
|September 2, 2024
PubMed
Summary
This summary is machine-generated.

A novel carbonic anhydrase (CA) class, ι-CA, found in diverse microbes, exhibits unique biochemical properties and catalytic mechanisms. These findings advance understanding of carbon metabolism and CA evolution.

Keywords:
Carbonic anhydrasesCatalytic mechanismEnzyme activityFree metal CAIota-CA, bacteria

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Area of Science:

  • Biochemistry and Molecular Biology
  • Microbial Genomics and Evolution
  • Enzyme Function and Catalysis

Background:

  • A novel carbonic anhydrase (CA) class, designated ι-CA, has been identified across various microbial genomes, including marine diatoms, algae, cyanobacteria, bacteria, and archaea.
  • This CA class presents unique biochemical properties and evolutionary significance, prompting further investigation into its structure and function.

Purpose of the Study:

  • To identify and characterize novel ι-CAs, specifically LCIP63 from Thalassiosira pseudonana, and explore bacterial ι-CAs like Burkholderia territorii ι-CA (BteCAι).
  • To classify ι-CAs into distinct variants based on sequence and domain analysis (COG4875 and COG4337).
  • To elucidate the structural and catalytic mechanisms of ι-CAs, particularly COG4337 variants, and their implications for CO2 hydration.

Main Methods:

  • Bioinformatic analyses were employed to identify potential ι-CA candidates, such as LCIP63.
  • Biochemical characterization was performed to assess enzyme activity, metal ion preference (Mn2+ vs. Zn2+), and inhibition by classical CA inhibitors (CAIs).
  • Sequence and domain analysis (COG4875, COG4337) were used for ι-CA classification, followed by structural analysis of COG4337 variants.

Main Results:

  • LCIP63 from T. pseudonana was confirmed as an ι-CA with manganese preference, suggesting marine adaptation.
  • Bacterial BteCAι demonstrated catalytic efficiency and sensitivity to CAIs.
  • Two ι-CA variants (COG4875 and COG4337) were identified; COG4337 variants exhibit unique structures and a novel metal-independent catalytic mechanism for CO2 hydration.

Conclusions:

  • The study reveals significant biochemical diversity within the ι-CA class, highlighting novel catalytic mechanisms and evolutionary adaptations.
  • The findings advance the understanding of carbon metabolism in diverse organisms and the complex evolution of carbonic anhydrases.
  • ι-CAs represent a potential target for developing novel antimicrobial agents due to their unique properties.