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Cystathionine beta-synthase then combines homocysteine and serine to form the asymmetrical thioether cystathionine, the enzyme cystathionine gamma-lyase converts the cystathionine into cysteine and alpha-ketobutyrate. In plants and bacteria, cysteine biosynthesis also starts from serine, the enzyme O-acetylserine -lyase, using sulfide sources, converts this ester into cysteine, releasing acetate. The cysteine thiol group is nucleophilic and easily oxidized, the reactivity is enhanced when the thiol is ionized, and cysteine residues in proteins have pKa values close to neutrality, so are often in their reactive thiolate form in the cell. Because of its reactivity, the thiol group of cysteine has numerous biological functions.

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