Kroutil Wolfgang, Mang Harald, Edegger Klaus, Faber Kurt
Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Austria.
Curr Opin Chem Biol. 2004 Apr;8(2):120-6. doi: 10.1016/j.cbpa.2004.02.005.
To improve the efficiency and applicability of biocatalytic redox-reactions for asymmetric ketone-reduction and enantioselective alcohol-oxidation catalyzed by nicotinamide-dependent dehydrogenases/reductases, several achievements for cofactor-recycling have been made during the last two years. First, the use of hydrogenases for NADPH recycling in a two enzyme system. Second, preparative transformations with alcohol dehydrogenases coupled with NADH oxidases for NAD+/NADP+ recycling. Third, an exceptional chemo-stable alcohol dehydrogenase can efficiently use i-propanol and acetone as cosubstrates for reduction and oxidation, respectively, in a single-enzyme system. Novel carbonyl reductases and dehydrogenases derived from plant cells are particularly suited for sterically demanding substrates.
为提高烟酰胺依赖性脱氢酶/还原酶催化的不对称酮还原和对映选择性醇氧化生物催化氧化还原反应的效率和适用性,在过去两年中,辅酶循环利用方面已取得多项成果。第一,在双酶体系中使用氢化酶进行NADPH循环。第二,利用醇脱氢酶与NADH氧化酶偶联进行NAD⁺/NADP⁺循环的制备性转化。第三,一种特殊的化学稳定醇脱氢酶能够在单酶体系中分别高效地将异丙醇和丙酮用作还原和氧化的共底物。源自植物细胞的新型羰基还原酶和脱氢酶特别适用于空间位阻较大的底物。