L-スレオニンの酵素的定量法 : (予報)大腸菌によるオキシアミノ酸の嫌気的脱アミノ基反応について

概要

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Serine and threonine have been reported by many workers to be deaminated by bacterial cells to pyruvate and α-ketobutyrate respectively, as the products of anaerobic deamination. In the following study, the vacuum-dried cells of Escherichia coli were employed for studing the quantitative deamination of hydroxyamino acids. Using the dried cells being about 10-fold weight of L-threonine in the anaerobic deamination mixture, at 37°, 1_??_2 hrs. in phosphate buffer pH 7.8, a quantitative amount of α-ketobutyrate measured by the Warburg manometric apparatus with yeast carboxylase was obtained. In the case of L-serine, the anaerobic deamination product, pyruvate is slightly metabolized and could not be quantitatively recovered. DL-Threonine and DL-allothreonine were deaminated by the dried preparations but could not be quantitatively recovered in the L-form, suggesting the inhibition of L-threonine and L-allothreonine dea minase by D-threonine and D-allothreonine respectively. DL-Serine was deaminated to pyruvate and showed that the anaerobic dearnination of D-serine proceeded the deamination of L-serine. The influence of some acidic amino acids, such as cysteine and adenllie acid AMP) on this deaminating reaction were also studied (Table 4, 6). α-Ketoglutarate, the anaerobic deamination product of β-hydroxyglutamate was not detected.
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