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Retracted: Chemoenzymatic Method for Enantioselective Synthesis of ( R )‐2‐Phenylglycine and ( R )‐2‐Phenylglycine Amide from Benzaldehyde and KCN Using Difference of Enzyme Affinity to the Enantiomers
Author(s) -
Kawahara Nobuhiro,
Asano Yasuhisa
Publication year - 2018
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201801254
Subject(s) - nitrilase , chemistry , benzaldehyde , strecker amino acid synthesis , enantioselective synthesis , amide , enantiomer , hydrolysis , biocatalysis , enantiomeric excess , yield (engineering) , organic chemistry , stereochemistry , catalysis , reaction mechanism , materials science , metallurgy
In general, enzymatic and chemoenzymatic methods for asymmetric synthesis of α‐amino acids are performed using highly enantioselective enzymes. The enzymatic reactions using α‐aminonitrile as a starting material have been performed using reaction conditions apart from the chemical Strecker synthesis. We developed a new chemoenzymatic method for the asymmetric synthesis of α‐amino acids from aldehydes and KCN by performing Strecker synthesis and nitrilase reaction in the same reaction mixture. Nitrilase AY487533 that showed rather low enantioselectivity in hydrolysis of 2‐phenylglycinonitrile (2PGN) to 2‐phenylglycine (2PG) was utilized in the hydrolysis of aminonitrile formed from benzaldehyde and KCN via 2PGN by Strecker synthesis, preferentially synthesizing ( R )‐2PG with more than 95 % yield and enantiomeric excess (ee). The method was also utilized for the synthesis of ( R )‐2‐phenylglycine amide (( R )‐2PGNH 2 ) from benzaldehyde and KCN by the chemoenzymatic reaction in the presence of a mutated nitrilase AY487533W186A, which catalyzes the conversion of 2PGN to 2PGNH 2 .