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Microbial thiol-containing enzymes are a heterogeneous group of catalytic proteins present in bacteria, fungi, and protozoa that utilize or depend on thiol (–SH) groups for their biochemical activity. These include, but are not limited to, enzymes using glutathione, mycothiol, bacillithiol, trypanothione, and ergothioneine as cofactors or substrates. Their principal biological role is the maintenance of redox balance and antioxidant defense within cells, enabling adaptation to oxidative stress and influencing microbial pathogenicity. Well-studied subclasses include glutathione-dependent oxidoreductases (such as glutathione reductase), mycothiol-dependent enzymes, and bacillithiol-dependent enzymes. They are considered attractive anti-infective drug targets due to their essentiality for pathogen survival and absence or significant divergence in human homologues. However, the lack of specificity in the term means it represents a *conceptual class* rather than a single actionable drug target, necessitating further molecular definition for precise therapeutic development[1][2][3].
Covalent modification or inhibition of essential thiol groups within the enzyme active site; Disruption of redox cycling or antioxidant defense mechanisms in microbes
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