Preparative use of isolated CYP102 monooxygenases -: A critical appraisal
Preparative use of isolated CYP102 monooxygenases -: A critical appraisal
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DOI：
10.1016/j.jbiotec.2006.02.013
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发表时间：
2006-08-05
影响因子：
4.1
通讯作者：
Schmid, Rolf D.
中科院分区：
文献类型：
--
作者：
Eiben, Sabine;Kaysser, Leonard;Schmid, Rolf D.
分离的P450单加氧酶在酶技术中长期被忽视的催化剂。这是令人惊讶的，因为它们显示出显著的底物特异性催化反应，这代表了对经典有机化学的挑战。另一方面，许多P450单加氧酶是膜结合的，依赖于相当复杂的电子传递系统，并且需要昂贵的辅因子如NAD（P）H。它们的活动很少，稳定性也很不理想。来自CYP 102家族的细菌P450单加氧酶的使用允许克服这些障碍中的一些。它们是可溶的，并且它们的周转率高，大概是因为它们的N-末端血红素单加氧酶和它们的C-末端二黄素还原酶结构域共价连接。近年来，蛋白质工程方法已成功地用于将CYP 102单加氧酶转化为强大的生物催化剂。(c)2006 Elsevier B. V.保留所有权利。
Isolated P450 monooxygenases have for long been neglected catalysts in enzyme technology. This is surprising as they display a remarkable substrate specificity catalyzing reactions, which represent a challenge for classic organic chemistry. On the other hand, many P450 monooxygenases are membrane bound, depend on rather complicated electron transfer systems and require expensive cofactors such as NAD(P)H. Their activities are low, and stability leaves much to be desired. The use of bacterial P450 monooxygenases from CYP102 family allows overcoming some of these handicaps. They are soluble and their turnovers are high, presumably because their N-terminal heme monooxygenase and their C-terminal diflavin reductase domain are covalently linked. In recent years, protein engineering approaches have been successfully used to turn CYP102 monooxgenases into powerful biocatalysts. (c) 2006 Elsevier B.V. All rights reserved.