Trimethylamine dehydrogenase from a methylotrophic bacterium. I. Isolation and steady-state kinetics.
Trimethylamine dehydrogenase from a methylotrophic bacterium. I. Isolation and steady-state kinetics.
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来自甲基营养细菌的三甲胺脱氢酶。
DOI：
10.1016/0005-2744(76)90319-3
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发表时间：
1976
期刊：
影响因子：
--
通讯作者：
J. Mallinson
中科院分区：
文献类型：
--
作者：
D. J. Steenkamp;J. Mallinson
1.三甲胺脱氢酶的分离(EC 1.5。99.7)从受限制的兼性甲硫氨酸到电泳均一性。2.沉淀平衡超速离心法测得该酶的相对分子质量和亚基相对分子质量为146800，十二烷基硫酸钠凝胶电泳法测得两个不同亚基的相对分子质量为70000-80000。3.初始速度研究表明，酶反应按乒乓机理进行。4.通过使用替代底物二乙胺及其产物乙醛和乙胺作为产物抑制剂、在吩嗪甲硫酸盐加入前乙胺的释放以及酶-两碳单元复合体的存在作为酶的稳定形式的分析，获得了进一步的动力学证据。5.初步描述了三甲胺脱氢酶的特殊基团及其光降解产物的一些性质。
1. The isolation of trimethylamine dehydrogenase (EC 1.5. 99.7) from a restricted facultative methylotroph to electrophoretic homogeneity is described. 2. The molecular weight and subunit molecular weights were found to be 146800 for the enzyme by sedimentation equilibrium ultracentrifugation and 70000-80000 for the two non-identical subunits by sodium dodecyl sulphate gel electrophoresis. 3. Initial velocity studies indicate that the enzymatic reaction proceeds by a Ping-Pong mechanism. 4. Further kinetic evidence was obtained by analysis of product inhibition patterns using the alternate substrate diethylamine and the products acetaldehyde and ethylamine as product inhibitors, for the release of ethylamine before the addition of phenazine methosulphate and for the existence of an enzyme-two-carbon unit complex as a stable form of the enzyme. 5. Some properties of the unusual prosthetic group of trimethylamine dehydrogenase and its photodegradation product are described in preliminary form.