7V1R

Leifsonia Alcohol Dehydrogenases LnADH

7V1R の概要

• エントリーDOI: 10.2210/pdb7v1r/pdb
• 分子名称: Alcohol Dehydrogenases, ISOPROPYL ALCOHOL, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: alcohol, dehydrogenases, biosynthetic protein
• 由来する生物種: Leifsonia antarctica
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 208208.29

構造登録者

Song, Y.,Qu, X. (登録日: 2021-08-05, 公開日: 2021-12-29, 最終更新日: 2023-11-29)

主引用文献

Zhu, L.,Song, Y.,Chang, C.,Ma, H.,Yang, L.,Deng, Z.,Deng, W.,Qu, X.
Engineering Leifsonia Alcohol Dehydrogenase for Thermostability and Catalytic Efficiency by Enhancing Subunit Interactions.
Chembiochem, 22:3178-3183, 2021

PubMed Abstract: Leifsonia alcohol dehydrogenase (LnADH) is a promising biocatalyst for the synthesis of chiral alcohols. However, limitations of wild-type LnADH observed for practical application include low activity and poor stability. In this work, protein engineering was employed to improve its thermostability and catalytic efficiency by altering the subunit interfaces. Residues T100 and S148 were identified to be significant for thermostability and activity, and the melting temperature (ΔT ) and catalytic efficiency of the mutant T100R/S148I toward ketone substrates was improved by 18.7 °C and 1.8-5.5-fold. Solving the crystal structures of the wild-type enzyme and T100R/S148L revealed beneficial effects of mutations on stability and catalytic activity. The most robust mutant T100R/S148I is promising for industrial applications and can produce 200 g liter  day chiral alcohols at 50 °C by only a 1 : 500 ratio of enzyme to substrate.

PubMed: 34549865
DOI: 10.1002/cbic.202100431

実験手法

X-RAY DIFFRACTION (2.81 Å)