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Occurrence of Taurine:-Ketoglutarate Aminotransferase in Bacterial Extracts¹

^a Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611, Japan

ABSTRACT

High activity of taurine:-ketoglutarate aminotransferase was found exclusively in cell-free extracts of Achromobacter superficialis and A. polymorph. The former was chosen for characterization of the enzymatic reaction. The enzyme activity was enhanced by addition of ß-alanine to the growth medium. The product from -ketoglutarate was identified as L-glutamate. Another product has been isolated, purified, and identified as sulfoacetaldehyde (2-oxoethanesulfonate), a deamination product from taurine, by comparison between the 2,4-dinitrophenylhydrazones of the synthetic and enzymatic products on the basis of studies by paper chromatography, by visible, infrared, and nuclear magnetic resonance spectrophotometries, and by elemental analysis. This enzymatic transamination was found to proceed stoichiometrically and reversibly as follows: NH₂·CH₂·CH₂·SO₃H + HOOC·CH₂·CH₂·CO·COOH OHC·CH₂·SO₃H + HOOC·CH₂·CH₂·CH(NH₂)·COOH.

² On leave from Department of Agricultural Chemistry, Ryukyu University, Naha, Okinawa, Japan.

¹ Dedicated to Alexander E. Braunstein on the occasion of his 70th birthday.