Bacterial γ-carbonic anhydrases.

Abstract

Carbonic anhydrases (CAs) are a ubiquitous family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide to bicarbonate and protons, playing pivotal roles in a variety of biological processes including respiration, calcification, acid-base balance, and CO2 fixation. Recent studies have expanded the understanding of CAs, particularly the γ-class from diverse biological sources such as pathogenic bacteria, extremophiles, and halophiles, revealing their unique structural adaptations and functional mechanisms that enable operation under extreme environmental conditions. This chapter discusses the comprehensive catalytic mechanism and structural insights from X-ray crystallography studies, highlighting the molecular adaptations that confer stability and activity to these enzymes in harsh environments. It also explores the modulation mechanism of these enzymes, detailing how different modulators interact with the active site of γ-CAs. Comparative analyzes with other CA classes elucidate the evolutionary trajectories and functional diversifications of these enzymes. The synthesis of this knowledge not only sheds light on the fundamental aspects of CA biology but also opens new avenues for therapeutic and industrial applications, particularly in designing targeted inhibitors for pathogenic bacteria and developing biocatalysts for industrial processes under extreme conditions. The continuous advancement in structural biology promises further insights into this enzyme family, potentially leading to novel applications in medical and environmental biotechnology.