The Role of Charged Residues in the Structural Adaptation of Short-Chain Alcohol Dehydrogenase (SDR) from Thermophilic Organisms to High Temperatures

Abstract

Understanding the adaptation mechanisms of proteins from extremophiles has paved the way for the development of new biocatalysts resistant to an extreme proton deficit. In the present work, we study the structural adaptation of NADP-dependent short-chain alcohol dehydrogenase/reductase (SDR) to high temperatures. We present the analysis of the amino acid composition of the SDR sequences, the comparative analysis of the structural elements in the SDR from mesophiles and thermophiles, and the results of the molecular dynamics of the superthermostable short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus (TsAdh319) and its homologues.