Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase with Wide Substrate Spectrum and Excellent Organic Solvent Tolerance

2019 ◽  
Vol 190 (1) ◽  
pp. 18-29 ◽  
Author(s):  
Wei Jiang ◽  
Bai-Shan Fang
Keyword(s):  
Organic Solvent ◽  
Binding Site ◽  
Solvent Tolerance ◽  
Organic Solvent Tolerance ◽  
Site Analysis ◽  
Coenzyme Binding ◽  
Substrate Spectrum ◽  
Coenzyme Binding Site

scholarly journals Characterization and Catalytic-Site-Analysis of an Aldo-Keto Reductase with Excellent Solvent Tolerance

Catalysts ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1121
Author(s):  
Rui Pei ◽  
Weiliang Wu ◽  
Yuqian Zhang ◽  
Libing Tian ◽  
Wei Jiang ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Organic Solvent ◽  
Organic Solvents ◽  
Reaction System ◽  
Catalytic Site ◽  
Solvent Tolerance ◽  
Chiral Alcohols ◽  
High Catalytic Activity ◽  
Site Analysis ◽  
Substrate Spectrum

Aldo-keto reductases (AKRs) mediated stereoselective reduction of prochiral carbonyl compounds is an efficient way of preparing single enantiomers of chiral alcohols due to their high chemo-, enantio-, and regio-selectivity. To date, the application of AKRs in the asymmetric synthesis of chiral alcohols has been limited, due to the challenges of cloning and purifying. In this work, the aldo-keto reductase (AKR3-2-9) from Bacillus sp. was obtained, purified and proved to be NADPH-dependent. It exhibits good bioactivity and stability at 37 °C, pH 6.0. AKR3-2-9 is catalytically active on 11 pairs of substrates such as 3-methylcyclohexanone and methyl pyruvate, among which it showed the highest catalytic activity for acetylacetone. In addition, AKR3-2-9 was able to be resistant to five common organic solvents such as methanol and ethanol, it retained high catalytic activity even in a reaction system containing 10% v/v organic solvent for 6 h, which indicates its broad substrate spectrum and exceptional organic solvent tolerance. Furthermore, its three-dimensional structure was constructed and catalytic-site-analysis of the enzyme was conducted. Notably, it was capable of catalyzing the reaction of the key intermediates of duloxetine. The extensive substrate spectrum and predominant organic solvents resistance makes AK3-2-9 a promising enzyme which can be potentially applied in medicine synthesis.

scholarly journals Study of Coenzyme Binding Site of Octopine Dehydrogenase Using Analogues of NAD+

1975 ◽  
Vol 56 (1) ◽  
pp. 109-116 ◽  
Author(s):  
Anna OLOMUCKI ◽  
Francoise THOME-BEAU ◽  
Jean-Francois BIELLMANN ◽  
Guy BRANLANT
Keyword(s):  
Binding Site ◽  
Coenzyme Binding ◽  
Octopine Dehydrogenase ◽  
Coenzyme Binding Site

ABC transporters and cell wall proteins involved in organic solvent tolerance in Saccharomyces cerevisiae

2013 ◽  
Vol 165 (2) ◽  
pp. 145-152 ◽  
Author(s):  
Nao Nishida ◽  
Naoki Ozato ◽  
Ken Matsui ◽  
Kouichi Kuroda ◽  
Mitsuyoshi Ueda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Organic Solvent ◽  
Abc Transporters ◽  
Solvent Tolerance ◽  
Cell Wall Proteins ◽  
Organic Solvent Tolerance
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