Publications by authors named "Hao-Bo Xu"
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.
Carbonyl reductase (CR)-catalyzed bioreduction in the organic phase and the neat substrate reaction system is a lasting challenge, placing higher requirements on the performance of enzymes. Protein engineering is an effective method to enhance the properties of enzymes for industrial applications. In the present work, a single point mutation E145A on our previously constructed CR mutant LsCR , coevolved thermostability, and activity.
View Article and Find Full Text PDFBackground: Coronary atherosclerotic plaque could go through rapid progression and induce adverse cardiac events. This study aimed to evaluate the impacts of smoking status on clinical outcomes of coronary non-target lesions.
Methods: Consecutive patients with coronary heart disease who underwent two serial coronary angiographies were included.