Premium
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 ).