Thiol-Containing Residues in Microbial Proteins (N/A)

Thiol-containing residues, primarily cysteines, in microbial proteins are critical for redox regulation, detoxification, and enzymatic activity. These residues are subject to a variety of modifications including disulfide bond formation, S-glutathionylation, and oxidation to sulfenic, sulfinic, or sulfonic acids. These modifications are often reversible and regulated by cellular reductase systems. Low molecular weight thiols such as glutathione and mycothiol serve as redox buffers, protecting protein thiols from irreversible damage. The reactivity of cysteine residues is influenced by their local protein environment, affecting their susceptibility to modification and subsequent impact on protein function. Targeting these residues offers therapeutic potential but requires careful consideration of potential off-target effects.

Other names

Cysteine residues in microbial proteinsProtein thiols in microbesMicrobial protein redox switches

N/A