1 With cysteinedesulfhydrase (E. C.4.4.1.1.) from Aerobactor aerogenes, an enzyme which catalyzes the stoichiometric conversion of L-cysteine to pyruvate, ammonia and sulfide, reversibility of the degradation of L-cysteine was investigated. It was found that the enzyme also catalized the reverse reaction of $alpha$, $eta$-elimination to synthesize L-cysteine derivatives from pyruvate, ammonia and sulfides when large amounts of substrates were added to the reaction mixtures. 2. The synthetic reaction by cysteinedesulfhydrase proceeded linearly with incubation time and enzyme concentrations. The optimal pH for the synthetic reaction was 10.0. 3. The results of the isolation and identification of the products showed that the L-cysteine derivatives synthesized by this enzymatic method were identical with S-methyl-L-cysteine and S-ethyl-L-cysteine respectively.