In:
The FEBS Journal, Wiley, Vol. 280, No. 22 ( 2013-11), p. 5815-5828
Abstract:
Hydroxynitrile lyases ( HNL s), which catalyse the decomposition of cyanohydrins, are found mainly in plants. In vitro , they are able to catalyse the synthesis of enantiopure cyanohydrins, which are versatile building blocks in the chemical industry. Recently, HNL s have also been discovered in bacteria. Here, we report on the detailed biochemical and structural characterization of a hydroxynitrile lyase from Granulicella tundricola ( G t HNL ), which was successfully heterologously expressed in Escherichia coli . The crystal structure was solved at a crystallographic resolution of 2.5 Å and exhibits a cupin fold. As G t HNL does not show any sequence or structural similarity to any other HNL and does not contain conserved motifs typical of HNL s, cupins represent a new class of HNL s. G t HNL is metal‐dependent, as confirmed by inductively coupled plasma/optical emission spectroscopy, and in the crystal structure, manganese is bound to three histidine and one glutamine residue. G t HNL displayed a specific activity of 1.74 U·mg −1 at p H 6 with ( R )‐mandelonitrile, and synthesized ( R )‐mandelonitrile with 90% enantiomeric excess at 80% conversion using 0.5 m benzaldehyde in a biphasic reaction system with methyl tertiary butyl ether.
Type of Medium:
Online Resource
ISSN:
1742-464X
,
1742-4658
DOI:
10.1111/febs.2013.280.issue-22
Language:
English
Publisher:
Wiley
Publication Date:
2013
detail.hit.zdb_id:
2172518-4
SSG:
12
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