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Sulfhydryl-containing enzyme active sites are characterized by the presence of a thiol group (-SH), typically from a cysteine residue, within the catalytic center of an enzyme. These sulfhydryl groups are highly nucleophilic and play critical roles in catalysis, substrate binding, and regulation of enzymatic activity. They are also susceptible to modification by small molecules, inhibitors, and environmental toxins, making them important targets for pharmacological intervention and toxicity studies.
Covalent modification of cysteine residues, leading to enzyme inhibition or altered function.
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