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Discovery of a novel (R)-selective bacterial hydroxynitrile lyase from Acidobacterium capsulatum.

Abstract：

: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_name

Comput Struct Biotechnol J

journal_title

Computational and structural biotechnology journal

authors

Wiedner R,Gruber-Khadjawi M,Schwab H,Steiner K

doi

10.1016/j.csbj.2014.07.002

subject

Has Abstract

pub_date

2014-07-08 00:00:00

pages

58-62

issue

16

issn

2001-0370

pii

S2001-0370(14)00011-7

journal_volume

10

pub_type

杂志文章

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