Exchange reactions catalyzed by methioninase from Pseudomonas putida.
Highly purified methioninase from Pseudomonas putida, which catalyzes alpha, gamma-elimination reactions of homocysteine and its S-substituted derivatives as well as alpha, beta-elimination reactions of cysteine and its derivatives, was found to catalyze exchange reactions between the substituent at the gamma-carbon of homocysteine substrates and exogenously added alkanethiols, forming the corresponding S-alkylhomocysteines. It also catalyzed similar beta-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.
D013437:Carbon-Sulfur Lyases / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism; D005001:Ethionine / Q000378:metabolism; D006711:Homocystine / Q000378:metabolism; D008190:Lyases / Q000378:metabolism*; D008715:Methionine / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology*; D013438:Sulfhydryl Compounds / Q000378:metabolism
D013438:Sulfhydryl Compounds; D006711:Homocystine; D008715:Methionine; D008190:Lyases; D013437:Carbon-Sulfur Lyases; D003545:Cysteine; D005001:Ethionine