Aromatic-Mediated Carbohydrate Recognition in Processive Serratia marcescens Chitinases

The Journal of Physical Chemistry. B
Suvamay JanaChristina M Payne

Abstract

Microorganisms use a host of enzymes, including processive glycoside hydrolases, to deconstruct recalcitrant polysaccharides to sugars. Processive glycoside hydrolases closely associate with polymer chains and repeatedly cleave glycosidic linkages without dissociating from the crystalline surface after each hydrolytic step; they are typically the most abundant enzymes in both natural secretomes and industrial cocktails by virtue of their significant hydrolytic potential. The ubiquity of aromatic residues lining the enzyme catalytic tunnels and clefts is a notable feature of processive glycoside hydrolases. We hypothesized that these aromatic residues have uniquely defined roles, such as substrate chain acquisition and binding in the catalytic tunnel, that are defined by their local environment and position relative to the substrate and the catalytic center. Here, we investigated this hypothesis with variants of Serratia marcescens family 18 processive chitinases ChiA and ChiB. We applied molecular simulation and free energy calculations to assess active site dynamics and ligand binding free energies. Isothermal titration calorimetry provided further insight into enthalpic and entropic contributions to ligand binding free energy...Continue Reading

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Citations

May 14, 2020·The Journal of Biological Chemistry·Sophanit MekashaVincent G H Eijsink
Aug 17, 2019·The Journal of Biological Chemistry·Natalie C BamfordP Lynne Howell
May 12, 2021·Journal of Molecular Recognition : JMR·Robert J FalconerAnthony K Mittermaier
Feb 23, 2019·The Journal of Physical Chemistry. B·Jogi MadhuprakashMorten Sørlie

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