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The cellular redox state is involved in regulating tyrosine phosphatase activity through the reversible oxidation of catalytic cysteine to sulfenic/sulfinic acid ( S -nitrosylation of the Cys215 residue by NO donors shields PTP1B from subsequent hydrogen peroxide-induced irreversible oxidation ( Recently, the discovery of reversible/irreversible covalent inhibitors targeting cysteine residues in and around the ATP-binding pocket of kinases has been gaining considerable attention ( Conclusion and future perspectives As shown in the Figure 4 , cysteine has different fates including the synthesis of cysteine-derived molecule, sulfur/carbon metabolic reprogramming, and venue for post-translational protein modification of various proteins or discovery of drug inhibitors

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