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. 1972 Feb;109(2):533–538. doi: 10.1128/jb.109.2.533-538.1972

Occurrence of Taurine:α-Ketoglutarate Aminotransferase in Bacterial Extracts1

Seizen Toyama a,2, Kenji Soda a
PMCID: PMC285173  PMID: 5058441

Abstract

High activity of taurine:α-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 β-alanine to the growth medium. The product from α-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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