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J Bacteriol. 1970 December; 104(3): 1286-1293
Copyright © 1970 American Society for Microbiology. All Rights Reserved.

Dissimilation of Methionine by Achromobacter starkeyi¹

^a Departmento de Microbiologia, Escuela Nacional de Ciencias Biologicas, Instituto Politecnico Nacional, Mexico 17, D.F.
^b Department of Biochemistry and Microbiology, College of Agriculture and Environmental Science, Rutgers, The State University, New Brunswick, New Jersey 08903

ABSTRACT

Methionine was decomposed by some bacteria which were isolated from soil. The sulfur of the methionine was liberated as methanethiol, and part of this became oxidized to dimethyl disulfide. Detailed studies with one of these cultures, Achromobacter starkeyi, indicated that the first step in methionine decomposition was its oxidadative deamination to -keto--methyl mercaptobutyrate by a constitutive amino acid oxidase. The following steps were carried out by inducible enzymes, the synthesis of which was inhibited by chloramphenicol. -Keto--methyl mercaptobutyrate was split producing methanethiol and -keto butyrate which was oxidized to propionate. The metabolism of propionate was similar to that described for animal tissues; the propionate was carboxylated to succinate via methyl malonyl coenzyme A, and the succinate was metabolized through the Krebs cycle.

¹ Paper of the Journal Series, New Jersey Agricultural Experiment Station, New Brunswick, N.J.

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