睾丸酮假单胞菌中L-组氨酸-2-酮戊二酸转氨酶的纯化及性质
The purification and properties of L-histidine--2-oxoglutarate aminotransferase from Pseudomonas testosteroni.
作者信息
Hacking A J, Hassall H
出版信息
Biochem J. 1975 May;147(2):327-34. doi: 10.1042/bj1470327.
Abstract
- Inducible L-histidine--2-oxoglutarate aminotransferase was purified some 170-fold from extracts of Pseudomonas testosteroni. 2. The preparation showed only one major component after electrophoresis on polyacrylamide gels, though additional minor bands were observed when samples concentrated on a DEAE-cellulose column were used. 3. The molecular weight of the enzyme was found to be approx. 70000 by chromatography on Sephadex G-200. 4. The purification scheme produced enzyme that was inactive in the absence of pyridoxal 5'-phosphate. 5. The equilibrium constant for the reaction L-histidine+2-oxoglutarate equilibrium imidazolylpyruvate+L-glutamate was 0.49. 6. The reaction mechanism was Ping Pong. 7. The enzyme was shown to have only low activity towards aromatic amino acids and was highly specific for 2-oxoglutarate.
摘要
从睾丸酮假单胞菌提取物中纯化出的可诱导型L-组氨酸 - 2-酮戊二酸转氨酶约为原来的170倍。
在聚丙烯酰胺凝胶上电泳后，该制剂仅显示出一个主要成分，不过当使用在DEAE - 纤维素柱上浓缩的样品时，可观察到额外的次要条带。
通过在Sephadex G - 200上进行色谱分析，发现该酶的分子量约为70000。
纯化方案得到的酶在没有磷酸吡哆醛时无活性。
反应L-组氨酸 + 2-酮戊二酸⇌咪唑基丙酮酸 + L-谷氨酸的平衡常数为0.49。
反应机制为乒乓机制。
该酶对芳香族氨基酸仅具有低活性，并且对2-酮戊二酸具有高度特异性。
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