Inside Cover: Mutagenesis of an Asn156 Residue in a Surface Region of  S ‐Selective Hydroxynitrile Lyase from  Baliospermum montanum  Enhances Catalytic Efficiency and Enantioselectivity (ChemBioChem 13/2015) | Zendy

Kawahara Nobuhiro | Zendy; Asano Yasuhisa | Zendy

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Inside Cover: Mutagenesis of an Asn156 Residue in a Surface Region of S ‐Selective Hydroxynitrile Lyase from Baliospermum montanum Enhances Catalytic Efficiency and Enantioselectivity (ChemBioChem 13/2015)

Author(s) -

Kawahara Nobuhiro,

Asano Yasuhisa

Publication year - 2015

Publication title -

chembiochem

Language(s) - English

Resource type - Reports

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.201581302

Subject(s) - enantiomer , chemistry , mutagenesis , catalysis , lyase , catalytic efficiency , residue (chemistry) , stereochemistry , cover (algebra) , site directed mutagenesis , enantiomeric excess , docking (animal) , enzyme , biochemistry , enantioselective synthesis , mutation , mutant , gene , mechanical engineering , medicine , nursing , engineering

The inside cover picture shows the crystal structure of hydroxynitrile lyase from Baliospermum montanum ( Bm HNL) complex with ( S )‐mandelonitrile by docking simulation. See the paper by N. Kawahara and Y. Asano for details on the improved catalytic efficiency of Bm HNL and improved enantiomeric excess of the product, ( S )‐mandelonitrile, by mutagenesis at Asn156. More details can be found in the Full Paper by N. Kawahara and Y. Asano on page 1891 in Issue 13, 2015 . (DOI: 10.1002/cbic.201500225 ).

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