DECARBOXYLATION OF L-METHIONINE IN PROTEUS VULGARIS AND BACILLUS SPHAERICUS

Acetone powders of Proteus vulgaris and Bacillus sphaericus ATCC 245 as well as to some lower extent washed suspensions of the fungi Claviceps purpurea and Penicillium nigricans decarboxylate L-methionine to 3-methyl-mercaptopropylamine (MMPA). Identity of the product of decarboxylation with authentic MMPA was proved by chromatographic comparison and conformance of the melting points of the picrates and DNP-derivatives. It is assumed that the decarboxylation of methionine is catalyzed by a substrate-unspecific decarboxylase of neutral amino acids. The respective enzyme in P. vulgaris would be the valine/leucine-carboxylyase (E.C. 4.1.1.14) already described by Ekladiuset al. (1957). © 1969 Springer-Verlag.