来自睾丸酮假单胞菌的尿刊酸酶的纯化及性质
The purification and properties of urocanase from Pseudomonas testosteroni.
作者信息
Hacking A J, Bell M V, Hassall H
出版信息
Biochem J. 1978 Apr 1;171(1):41-50. doi: 10.1042/bj1710041.
Urocanase (urocanate hydratase, EC 4.2.1.49) purified from Pseudomonas testosteroni has a mol.wt. of 118000 determined by sedimentation-equilibrium analysis. Ultracentrifugation in 6M-guanidine hydrochloride and polyacrylamide-gel electrophoresis in sodium dodecyl sulphate show that the enzyme consists of two identical or very similar subunits. It is, like urocanase isolated from other sources, inhibited by reagents that react with carbonyl groups. Although urocanase from Ps. testosteroni is strongly inhibited by NaBH4, no evidence could be obtained for the presence of covalently bound 2-oxobutyrate as a prosthetic group; this is in contrast with findings elsewhere for urocanase from Pseudomonas putida. Urocanase from Ps. testosteroni does not contain pyridoxal 5'-phosphate as a coenzyme and in this respect is similar to all urocanases studied in purified form.
从睾丸酮假单胞菌中纯化得到的尿刊酸酶（尿刊酸水合酶，EC 4.2.1.49），通过沉降平衡分析测定其分子量为118000。在6M盐酸胍中进行超速离心以及在十二烷基硫酸钠中进行聚丙烯酰胺凝胶电泳表明，该酶由两个相同或非常相似的亚基组成。与从其他来源分离的尿刊酸酶一样，它受到与羰基反应的试剂的抑制。尽管来自睾丸酮假单胞菌的尿刊酸酶受到硼氢化钠的强烈抑制，但未获得证据表明存在共价结合的2-氧代丁酸作为辅基；这与其他地方关于恶臭假单胞菌尿刊酸酶的研究结果形成对比。来自睾丸酮假单胞菌的尿刊酸酶不含有磷酸吡哆醛作为辅酶，在这方面与所有以纯化形式研究的尿刊酸酶相似。
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