面包酵母葡萄糖6-磷酸脱氢酶在溶液中及共价连接到琼脂糖上时所催化反应的稳态动力学的动力学机制。
Kinetic mechanism from steady-state kinetics of the reaction catalysed by baker's-yeast glucose 6-phosphate dehydrogenase in solution and covalently attached to sepharose.
作者信息
Gould B J, Goheer M A
出版信息
Biochem J. 1976 Aug 1;157(2):389-93. doi: 10.1042/bj1570389.
Abstract
- The reaction catalysed by glucose 6-phosphate dehydrogenase (D-glucose 6-phosphate-NADP+ oxidoreductase, EC 1.1.1.49) from baker's yeast was studied in 42mM-glycylglycine buffer, pH7.4 at 25 degrees C, by initial-velocity studies and by the use of NADPH as a product inhibitor. 2. The reactions catalysed by both the soluble enzyme and a stable enzyme covalently attached to CNBr-activated Sepharose 4B probably follow an ordered reaction mechanism with NADP+ and NADPH as the leading reactants. 3. The kinetic constants obtained for the soluble enzyme lere: KNADP+m, 19 muM; KNADP+s, 23 muM; KNADPHs, 15 muM. Similar values were obtained for the immobilized enzyme. 4. The assay of the immobilized enzyme was done by using a micro packed-bed recirculation reactor, and the advantages of this technique are discussed.
摘要
- 在25℃、pH7.4的42mM甘氨酰甘氨酸缓冲液中，通过初速度研究并使用NADPH作为产物抑制剂，对面包酵母中的葡萄糖6-磷酸脱氢酶（D-葡萄糖6-磷酸-NADP +氧化还原酶，EC 1.1.1.49）催化的反应进行了研究。2. 可溶性酶和共价连接到CNBr活化的琼脂糖凝胶4B上的稳定酶所催化的反应可能遵循以NADP +和NADPH作为主要反应物的有序反应机制。3. 可溶性酶的动力学常数如下：KNADP + m，19μM；KNADP + s，23μM；KNADPHs，15μM。固定化酶也获得了类似的值。4. 使用微填充床循环反应器对固定化酶进行了测定，并讨论了该技术的优点。
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