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- W2593153017 abstract "Quantitative Functional Characterization of Conserved Molecular Interactions in the Active Site of Mannitol 2-Dehydrogenase James E. Lucas‡, Justin B. Siegel‡,α,β ‡ Genome Center, University of California, Davis, CA 95616, USA α Department of Chemistry, University of California, Davis, CA 95616, USA β Department of Biochemistry & Molecular Medicine, University of California, Davis, CA 95616, USA Received 5 January 2015; Accepted 2 March 2015 DOI 10.1002/pro.2669 First published online 2 April 2015 Lucas, J. E. and Siegel, J. B. (2015), Quantitative functional characterization of conserved molecular interactions in the active site of mannitol 2-dehydrogenase. Protein Science, 24: 936–945. doi:10.1002/pro.2669 The three genes encoding active site mutants E133A, E133Q, and N300A contained unexpected mutations. We have reconstructed these mutants, sequence confirmed, and assayed the correct enzyme mutants on the reported substrates. Tables and figures with kinetic data for the corrected mutants are provided. We regret this error, and would like to thank AddGene for the due diligence carried out in order to identify this mistake. Energetic changes of the measured kinetic constants between WT pfMDH and selected mutants on D-mannitol (black), D-arabitol (light gray), and meso-erythritol (dark gray). Residues are grouped as directly or indirectly involved in catalysis. Mutant labeled “Triple” is the triple mutant containing the H303A, R373A, and K381A mutations. Changes in free energy were calculated using the first order Arrhenius equation (Equation and constants provided in Supplementary Figure S5)." @default.
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- W2593153017 date "2016-02-22" @default.
- W2593153017 modified "2023-10-02" @default.
- W2593153017 title "Erratum: Quantitative functional characterization of conserved molecular interactions in the active site of mannitol 2-dehydrogenase" @default.
- W2593153017 doi "https://doi.org/10.1002/pro.2882" @default.
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