7v1q | pdb_00007v1q

Leifsonia Alcohol Dehydrogenases LnADH

spinqualitylabelsall models 7v1q, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.58Å Ligands: IPA, MSE, NAD, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 (DeltaTm ) and catalytic efficiency of the mutant T100R/S148I toward ketone substrates was improved by 18.7 degrees 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(-1) day(-1) chiral alcohols at 50 degrees C by only a 1 : 500 ratio of enzyme to substrate. Engineering Leifsonia Alcohol Dehydrogenase for Thermostability and Catalytic Efficiency by Enhancing Subunit Interactions.,Zhu L, Song Y, Chang C, Ma H, Yang L, Deng Z, Deng W, Qu X Chembiochem. 2021 Nov 16;22(22):3178-3183. doi: 10.1002/cbic.202100431. Epub 2021, Oct 1. PMID:34549865 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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