Thiol-containing protein or Thiol-containing enzyme (None; abbreviations are generally family/enzyme specific (e.g., GPx for glutathione peroxidase))

Thiol-containing proteins and enzymes comprise a highly diverse group of biomolecules defined by the presence of sulfhydryl (thiol) groups, typically on cysteine residues or as part of co-factors such as coenzyme A[1][6]. These groups are essential for regulating protein structure via disulfide bond formation, participating in redox reactions for antioxidant defense, driving enzymatic catalysis, and acting in cell signaling. The class includes key examples like glutathione and cysteine proteases, which are critical for maintaining cellular homeostasis, mediating protein turnover, and protecting against oxidative stress[1][2][4]. Because the term "Thiol-containing proteins and enzymes" encompasses a vast set of molecular entities—rather than a single target—it is not suitable as a specific therapeutic target name. Precise identification should specify the family (e.g., "Cysteine protease," "Glutathione peroxidase") to provide actionable biomedical information[4][6].

Other names

Thiol proteinsSulfhydryl proteinsMercaptan proteinsCysteine proteases

Covalent modification by reactive small molecules (alkylation, oxidation) - Inhibition via active-site blockade (protease inhibitors) - Disruption of disulfide bonds by reducing agents - Chelation of metals interfering with function