A novel NADP+-dependent L-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154:: a promising enzyme for the production of double chiral aminoalcohols
A novel NADP+-dependent L-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154:: a promising enzyme for the production of double chiral aminoalcohols
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DOI：
10.1111/j.1472-765x.2006.01970.x
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发表时间：
2006-10-01
影响因子：
2.4
通讯作者：
Shimizu, S.
中科院分区：
文献类型：
--
作者：
Kataoka, M.;Nakamura, Y.;Shimizu, S.
目的：从红平红球菌（Rhodococcus erythropolis）MAK 154中分离到一种新的NADP（+）依赖的L-1-氨基-2-丙醇脱氢酶，并对其进行了结构鉴定。该酶催化多种氨基醇的NADP（+）依赖性氧化，以及氨基酮化合物的NADPH依赖性不对称还原为双手性氨基醇d-伪麻黄碱。氨基酸序列分析表明，该酶可能属于短链脱氢酶/还原酶家族。研究结果表明：该酶对氨基醇的脱氢反应具有可逆催化作用，并对还原反应具有独特的立体专一性。研究意义和影响：该酶是一种很有前途的催化剂，可用于由前手性底物合成双手性化合物d-伪麻黄碱。
Aim: A novel NADP(+)-dependent L-1-amino-2-propanol dehydrogenase was isolated from Rhodococcus erythropolis MAK154, and characterized.Methods and Results: The enzyme was inducibly produced on cultivation with aminoalcohols such as 1-amino-2-propanol, 1-amino-2-butanol and 2-amino-cyclohexanol. The enzyme catalyses the NADP(+)-dependent oxidation of several aminoalcohols, and also the NADPH-dependent asymmetric reduction of an aminoketone compound to a double chiral aminoalcohol, d-pseudoephedrine. Amino acid sequence analysis showed that the enzyme might belong to the short-chain dehydrogenase/reductase family.Conclusions: NADP(+)-dependent L-1-amino-2-propanol dehydrogenase isolated from R. erythropolis MAK154 reversibly catalysed dehydrogenation of aminoalcohols, and exhibited a unique sterospecifity for the reduction reaction.Significance and Impact of the Study: The enzyme is a promising catalyst for the production of double chiral compound, d-pseudoephedrine, from prochiral substrate.