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• W1875952581 endingPage "7306" @default.
• W1875952581 startingPage "7292" @default.
• W1875952581 abstract "The enzymatic degradation of recalcitrant polysaccharides such as cellulose (β-1,4-linked glucose) and chitin (β-1,4-linked N-acetylglucosamine) by glycoside hydrolases (GHs) is of significant biological and economical importance. In nature, depolymerization is primarily accomplished by processive GHs, which remain attached to the substrate between subsequent hydrolytic reactions. Recent computational efforts have suggested that the processive ability of a GH is directly linked to the ligand binding free energy. The contribution of individual aromatic residues in the active site of these enzymes has been extensively studied. In this study, we offer the first experimental evidence confirming correlation of binding free energy and degree of processivity and evidence that polar residues are essential for maintaining processive ability. Exchanging Thr276 with Ala in substrate binding subsite −2 in the processive ChiA of Serratia marcescens results in a decrease in both the enthalpy (2.6 and 3.8 kcal/mol) and free energy (0.5 and 2.2 kcal/mol) for the binding to the substrate (GlcNAc)6 and the inhibitor allosamidin, respectively, compared to that of the wild type. Moreover, the initial apparent processivity as measured by [(GlcNAc)2]/[GlcNAc] ratios (17.1 ± 0.4) and chitin degradation efficiency (20%) are greatly reduced for ChiA-T276A versus those of the wild type (30.1 ± 1.5 and 75%, respectively). Mutation of Arg172 to Ala reduces the level of recognition and positioning of the substrate into the active site. Molecular dynamics simulations indicate ChiA-R172A behaves like the wild type, but the dynamics of ChiA-T276A are greatly influenced by mutation, which is reflective of their influence on processivity." @default.
• W1875952581 created "2016-06-24" @default.
• W1875952581 creator A5011122791 @default.
• W1875952581 creator A5062073455 @default.
• W1875952581 creator A5067524914 @default.
• W1875952581 creator A5083669397 @default.
• W1875952581 creator A5087283503 @default.
• W1875952581 date "2015-12-02" @default.
• W1875952581 modified "2023-10-06" @default.
• W1875952581 title "Processivity, Substrate Positioning, and Binding: The Role of Polar Residues in a Family 18 Glycoside Hydrolase" @default.
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• W1875952581 doi "https://doi.org/10.1021/acs.biochem.5b00830" @default.
• W1875952581 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26503416" @default.
• W1875952581 hasPublicationYear "2015" @default.
• W1875952581 type Work @default.

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