来自链霉菌属GF3587的新型（R）-亚胺还原酶的纯化与表征
Purification and characterization of a novel (R)-imine reductase from Streptomyces sp. GF3587.
作者信息
Mitsukura Koichi, Suzuki Mai, Shinoda Sho, Kuramoto Tatsuya, Yoshida Toyokazu, Nagasawa Toru
机构信息
Department of Biomolecular Science, Faculty of Engineering, Gifu University.
出版信息
Biosci Biotechnol Biochem. 2011;75(9):1778-82. doi: 10.1271/bbb.110303. Epub 2011 Sep 7.
The (R)-imine reductase (RIR) of Streptomyces sp. GF3587 was purified and characterized. It was found to be a NADPH-dependent enzyme, and was found to be a homodimer consisting of 32 kDa subunits. Enzymatic reduction of 10 mM 2-methyl-1-pyrroline (2-MPN) resulted in the formation of 9.8 mM (R)-2-methylpyrrolidine ((R)-2-MP) with 99% e.e. The enzyme showed not only reduction activity for 2-MPN at neutral pH (6.5-8.0), but also oxidation activity for (R)-2-MP under alkaline pH (10-11.5) conditions. It appeared to be a sulfhydryl enzyme based on the sensitivity to sulfhydryl specific inhibitors. It was very specific to 2-MPN as substrate.
对链霉菌属GF3587的（R）-亚胺还原酶（RIR）进行了纯化和表征。发现它是一种依赖NADPH的酶，是由32 kDa亚基组成的同型二聚体。用该酶对10 mM 2-甲基-1-吡咯啉（2-MPN）进行酶促还原，生成了9.8 mM对映体过量值为99%的（R）-2-甲基吡咯烷（（R）-2-MP）。该酶不仅在中性pH（6.5 - 8.0）下对2-MPN具有还原活性，而且在碱性pH（10 - 11.5）条件下对（R）-2-MP具有氧化活性。基于对巯基特异性抑制剂的敏感性，它似乎是一种巯基酶。它对作为底物的2-MPN具有高度特异性。
Zotero 插件