1975 年 78 巻 5 号 p. 1105-1107
Highly purified methioninase from Pseudomonas putida, which catalyzes α, γ-elimination reactions of homocysteine and its S-substituted derivatives as well as α, β-elimination reactions of cysteine and its derivatives, was found to catalyze exchange reactions between the substituent at the γ-carbon of homocysteine substrates and exogenously added alkanethiols, forming the corresponding S-alkylhomocysteines. It also catalyzed similar β-exchange reactions between cysteine and alkanethiols. Thus, all the substrates for the methioninase-catalyzed elimination reactions also appear to be available for the exchange reactions.