Fachbereich Chemie, Philipps Universität Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany.
Chemistry. 2012 Aug 13;18(33):10160-72. doi: 10.1002/chem.201202163. Epub 2012 Jul 16.
Baeyer-Villiger monooxygenases (BVMOs) have been used for decades as catalysts in stereoselective Baeyer-Villiger reactions, including oxidative kinetic resolution of racemic ketones and desymmetrization of prochiral substrates with high enantioselectivity. These complement catalytic BV processes based on chiral synthetic catalysts. However, as in any enzyme-catalyzed process, limitations exist due to the often observed narrow substrate scope and/or insufficient stereoselectivity. Recent protein engineering of BVMOs in the form of directed evolution and rational design have eliminated these traditional limitations, which is the subject of this Minireview. The main focus is on phenylacetone monooxygenase (PAMO); an unusually thermostable and robust BVMO, which has a very narrow substrate scope. Protein engineering of PAMO has provided a number of mutants that display relatively wide substrate scope, high stereoselectivity, and maintained thermostability.
Baeyer-Villiger 单加氧酶 (BVMOs) 作为立体选择性 Baeyer-Villiger 反应中的催化剂已应用了数十年，包括外消旋酮的氧化动力学拆分和前手性底物的去对称化，具有高对映选择性。这些补充了基于手性合成催化剂的催化 BV 过程。然而，与任何酶催化过程一样，由于经常观察到的底物范围狭窄和/或立体选择性不足，存在限制。最近，通过定向进化和合理设计对 BVMO 进行蛋白质工程改造，消除了这些传统限制，这是本篇综述的主题。主要重点是苯乙酮单加氧酶 (PAMO)；一种异常耐热和稳健的 BVMO，其底物范围非常狭窄。PAMO 的蛋白质工程改造提供了许多突变体，它们显示出相对较宽的底物范围、高立体选择性和保持耐热性。
