7V1R

Leifsonia Alcohol Dehydrogenases LnADH

Summary for 7V1R

• Entry DOI: 10.2210/pdb7v1r/pdb
• Descriptor: Alcohol Dehydrogenases, ISOPROPYL ALCOHOL, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: alcohol, dehydrogenases, biosynthetic protein
• Biological source: Leifsonia antarctica
• Total number of polymer chains: 8
• Total formula weight: 208208.29

Authors

Song, Y.,Qu, X. (deposition date: 2021-08-05, release date: 2021-12-29, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.81 Å)