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J. Biochem, 1977, Vol. 81, No. 5 1375-1381
© 1977 Japanese Biochemical Society

research-article

Two {omega}-Amino Acid Transaminases from Bacillus cereus

Yoshihisa NAKANO, Hiroko TOKUNAGA1 and Shozaburo KITAOKA

Department of Agricultural Chemistry, University of Osaka Prefecture Sakai, Osaka 591

Bacillus cereus strain K-22 produced two distinct {omega}-amino acid transaminases, one catalyzing the transamination between ß-alanine and pyruvic acid and the other that between {gamma}-aminobutyric acid and {alpha}-ketoglutaric acid. The two enzymes were partially purified and separated from each other by various chromatographies. ß-Alanine : pyruvic acid transaminase and {gamma}-aminobutyric acid : {alpha}-ketoglutaric acid transaminase were induced by the addition of ß-alanine and {gamma}-aminobutyric acid, respectively, to the growth medium.

ß-Alanine transaminase showed an optimum pH of 10.0 and optimum temperature of 35°C, and its Km values for ß-alanine and pyruvic acid were both 1.1 mM. {gamma}-Aminobutyric acid, {varepsilon}-aminocaproic acid, 2-aminoethylphosphonic acid, and propylamine showed about 30–40% of the activity of ß-alanine as amino donors, and oxalacetic acid was as good an amino acceptor as pyruvic acid. The optimum pH and temperature of {gamma}-aminobutyric acid transaminase were 9.0 and 50°C, respectively, and its Km value for {gamma}-aminobutyric acid was 2.8 mM, while that for {alpha}-ketoglutaric acid was 2.3 mM. {gamma}-Aminobutyric acid and ö-aminovaleric acid were good amino donors but other {omega}-amino acids were virtually inactive with {gamma}-aminobutyric acid transaminase; {alpha}-ketoglutaric acid, and to a lesser extent glyoxylic acid, were active amino acceptors. Sulfhydryl reagents specifically activated {gamma}-aminobutyric acid transaminase.

1Present address: Tokai University School of Medicine, Isehara, Kanagawa 259-11.


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