Catalyzed by the nitrile hydratase and the amidease in Rhodococcus sp. AJ270 cells under very mild conditions, a number of alpha-aryl- and alpha-alkyl-substituted DL-glycine nitriles 1 rapidly underwent a highly enantioselective hydrolysis to afford D-(-)-alpha-amino acid amides 2 and L-(+)-alpha-amino acids 3 in high yields with excellent enantiomeric excesses in most cases. The overall enantioselectivity of the biotransformations of nitriles originated from the combined effects of a high L-enantioselective amidase and a low enantioselective nitrile hydratase. The influence of the substrates on both reaction efficiency and enantioselectivity was also discussed in terms of steric and electronic effects. Coupled with chemical hydrolysis of D-(-)-alpha-phenylglycine amide, biotransformation of DL-phenylglycine nitrile was applied in practical scale to produce both D- and L-phenylglycines in high optical purity.
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Article Synopsis
- This study focuses on improving the enzyme Fe-type Nitrile hydratase (Fe-type NHase) from Pseudomonas fluorescens by mutating a specific residue (Q86) in its substrate access tunnel, which enhanced its catalytic performance.
- The modified enzyme, PfNHase-αQ86W, demonstrated significantly increased catalytic activity towards various nitrile substrates, with a notable 17.32-fold improvement in efficiency for benzonitrile compared to the wild type.
- Structural analyses revealed changes in the enzyme's entrance tunnel and substrate-binding pocket, which contributed to a shift in substrate preference from aliphatic to aromatic nitriles, supported by molecular dynamics simulations.
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