Cultures of
Streptomyces lincolnensis accumulated 3-methylthioacrylic acid in amounts directly related to the concentration of methionine in the medium. The metabolite was labeled by L-(
methyl-
14C) but not by DL-(
carboxyl-
14C) methionine, indicating biosynthesis from the amino acid with loss of the carboxyl group.
S. lincolnensis mycelium contained sufficient peroxidase activity to catalyse oxidative decarboxylation of L-methionine to 3-methylthiopropionamide as the initial step of a biosynthetic sequence. The enzyme, partially purified by ammonium sulfate precipitation, chromatography on a DEAE-cellulose column and gel filtration, had a molecular weight of approximately 350, 000, a pH optimum of 6.0, with
o-dianisidine as electron donor and a K
m value of 7.5×10
-4 M with respect to hydrogen peroxide. Cultures of
S. lincolnensis supplemented with 3-(
methyl-
14C) methylthiopropionic acid gave labeled 3-methylthioacrylic acid. However, 3-(
methyl-
14C) methylthiopropionamide did not label the metabolite, suggesting that the first intermediate in the pathway may be the keto acid, which is then oxidatively decarboxylated to 3-methylthiopropionic acid.
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