Abstract
1. L-Tyrosine-${\alpha}$-ketoglutaric transaminase and p-hydroxyphenylpyruvic acid oxidase are distributed in Aspergillus oryzae. 2. L-Tyrosine oxidation in extracts of acetone powder, cell free extract and culture liquid of Aspergillus oryzae cultivated in the shaking culture are considerably accelerated by the addition of ${\alpha}$-ketoglutaric acid and then formation of glutamic acid was identified by chromatography method. 3. The roles of ${\alpha}$-ketoglutaric acid and pyridoxal phosphate have been shown to be an amino group acceptor in a transamination reaction. 4. Enzyme systems of an extracts of acetone powder and cell free extract also rapidly oxidized L-tyrosine and p-hydroxyphenlpyruvic acid to homogentisic acid. 5. The optimum pH for L-tyrosine-${\alpha}$-ketoglutaric acid transaminase was pH values of 6.0 and 6.5, and that for p-hydroxyphenylpyruvic acid oxidase was at pH values of 7.5.
1. Aspergillus oryzae의 균체에는 L-tyrosine-${\alpha}$-ketoglutaric acid transaminase와 p-hydroxyphenlypyruvic acid oxidase가 존재해 있다. 2. L-Tyrosine 산화효소는 액침배양한 Aspergillus oryzae의 acetone powder, cell free extract 및 배양액에도 존재하며 L-tyrosine은 ${\alpha}$-ketoglutaric acid의 첨가로 더욱 빨리 전환되었다. 3. ${\alpha}$-Ketoglutaric acid와 pyridoxal phosphate는 transamination의 amino기의 수용체로 생각되었다. 4. 이들 효소계는 L-tyrosine와 p-hydroxyphenlypyruvic acid를 homogentisic acid로 산화시켰다. 5. Ascorbic acid는 p-hydroxyphenlypyruvic가 homogentisic acid로 산화되는데 특별한 역할을 하는 것 같다. 6. L-Tyrosine-${\alpha}$-ketoglutaric acid transaminase와 p-hydroxyphenlypyruvic acid oxidase의 최적 pH는 각 각 pH $6.0{\sim}6.5$와 pH 7.5이었다.