2-氧代醛脱氢酶的纯化及其对特殊胺类的依赖性。
Purification of 2-oxoaldehyde dehydrogenase and its dependence on unusual amines.
作者信息
Dunkerton J, James S P
出版信息
Biochem J. 1975 Sep;149(3):609-17. doi: 10.1042/bj1490609.
Abstract
- 2-Oxoaldehyde dehydrogenase was purified from sheep liver and gave one band on polyacrylamide-gel electrophoresis. 2. The enzyme was completely dependent for its activity on the presence of Tris or one of a number of related amines, all of general structure: (See article). When more than one R group was hydrogen no enzyme activity was observed. 3. Only one of these amines is known to exist in living tissues and large concentrations of all amines were required for maximum activity. L-2-Aminopropan-1-ol was the most effective amine on the basis of substrate Km and Vmax. values and the amine Km values. 4. The enzyme was activated by phosphate which lowered the Km values for methylglyoxal, amine and NAD+. 5. The pH optimum of the enzyme was 9.3 and there was no activity at pH values below 7.8. A search for activators that might produce activity at pH 7.4 proved unsuccessful. 6. The enzyme was inhibited by rather large concentrations of barbiturates (6-46 mM) and nitro-alcohol analogues of the activating amines (66-139 mM).
摘要
- 从羊肝中纯化出2-氧代醛脱氢酶，其在聚丙烯酰胺凝胶电泳上呈现一条带。2. 该酶的活性完全依赖于Tris或多种相关胺类中的一种的存在，这些胺类的一般结构为：（见文章）。当不止一个R基团为氢时，未观察到酶活性。3. 已知这些胺类中只有一种存在于活组织中，且最大活性需要所有胺类的高浓度。基于底物Km和Vmax值以及胺类Km值，L-2-氨基丙醇是最有效的胺类。4. 该酶被磷酸盐激活，磷酸盐降低了甲基乙二醛、胺类和NAD⁺的Km值。5. 该酶的最适pH为9.3，在pH值低于7.8时无活性。寻找可能在pH 7.4产生活性的激活剂未成功。6. 该酶受到相当高浓度的巴比妥酸盐（6 - 46 mM）和激活胺类的硝基醇类似物（66 - 139 mM）的抑制。
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