Active Site Desolvation and Thermostability Trade-Offs in the Evolution of Catalytically Diverse Triazine Hydrolases.

doi:10.1021/acs.biochem.6b00731

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Active Site Desolvation and Thermostability Trade-Offs in the Evolution of Catalytically Diverse Triazine Hydrolases.

Biochemistry - 15 Nov 2016

Sugrue Elena, Carr Paul D, Scott Colin, Jackson Colin J

Abstract excerpt

The desolvation of ionizable residues in the active sites of enzymes and the subsequent effects on catalysis and thermostability have been studied in model systems, yet little about how enzymes can naturally evolve to include active sites with highly reactive and desolvated charges is known. Variants of triazine hydrolase (TrzN) with significant differences in their active sites have been isolated from different...

Topics

Actinobacteria
Bacterial Proteins
Biocatalysis
Catalytic Domain
Crystallization
Crystallography, X-Ray
Enzyme Stability
Evolution, Molecular
Glutamic Acid
Hydrolases
Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Kinetics

Models, Molecular

Molecular Structure

Mutation

Protein Binding

Protein Domains

Temperature

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Identifiers

PMID: 27768291
DOI: 10.1021/acs.biochem.6b00731

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