Thiol-containing bacterial enzyme

Thiol-containing bacterial enzymes refer to a broad class of bacterial proteins and enzymes that possess active site cysteine residues or other functional thiols. These include low molecular weight (LMW) thiol-dependent oxidoreductases such as thioredoxin, glutaredoxin, mycoredoxin, bacilliredoxin, and various periplasmic disulfide bond-forming/reducing enzymes. They play central roles in maintaining the reduced state of cytoplasmic proteins through reversible S-thiolation reactions—modifying cysteine residues to protect against oxidative damage and regulate function during stress. The most studied LMW thiols involved are glutathione (in Gram-negative bacteria), mycothiol (in Actinomycetes), and bacillithiol (in Firmicutes)[1][2]. These systems help bacteria survive hostile environments—including those encountered during infection—by detoxifying reactive oxygen/nitrogen/chlorine/electrophilic species. Inhibiting these pathways is an emerging strategy for developing new antibacterial therapies due to their importance in pathogen survival under stress conditions[2].

Other names

Protein S-thiolated bacterial enzymeBacterial thiol-redox enzymeBacterial thiol-disulfide oxidoreductaseLMW thiol-dependent bacterial protein

Drugs targeting these proteins would likely act by inhibiting their redox activity or interfering with their ability to maintain reduced protein thiols and detoxify reactive species[1][2].