کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2079233 | 1079850 | 2014 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Discovery of a novel (R)-selective bacterial hydroxynitrile lyase from Acidobacterium capsulatum Discovery of a novel (R)-selective bacterial hydroxynitrile lyase from Acidobacterium capsulatum](/preview/png/2079233.png)
Hydroxynitrile lyases (HNLs) are powerful carbon–carbon bond forming enzymes. The reverse of their natural reaction – the stereoselective addition of hydrogen cyanide (HCN) to carbonyls – yields chiral cyanohydrins, versatile building blocks for the pharmaceutical and chemical industry. Recently, bacterial HNLs have been discovered, which represent a completely new type: HNLs with a cupin fold. Due to various benefits of cupins (e.g. high yield recombinant expression in Escherichia coli), the class of cupin HNLs provides a new source for interesting, powerful hydroxynitrile lyases in the ongoing search for HNLs with improved activity, enantioselectivity, stability and substrate scope. In this study, database mining revealed a novel cupin HNL from Acidobacterium capsulatum ATCC 51196 (AcHNL), which was able to catalyse the (R)-selective synthesis of mandelonitrile with significantly better conversion (97%) and enantioselectivity (96.7%) than other cupin HNLs.
Journal: Computational and Structural Biotechnology Journal - Volume 10, Issue 16, June 2014, Pages 58–62