Exploiting correlated molecular-dynamics networks to counteract enzyme activity–stability trade-off

The directed evolution of enzymes for improved activity or substrate specificity commonly leads to a trade-off in stability. We have identified an activity–stability trade-off and a loss in unfolding cooperativity for a variant (3M) of Escherichia coli transketolase (TK) engineered to accept aromati...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2018-12, Vol.115 (52), p.E12192-E12200
Hauptverfasser:	Yu, Haoran, Dalby, Paul A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aldehydes Aldehydes - chemistry Aldehydes - metabolism Biological Sciences Catalytic Domain Computer applications Computer simulation Cooperativity Correlation Correlation analysis Dimers Directed evolution Dynamic stability E coli Enzymatic activity Enzyme activity Enzyme Stability Enzymes Escherichia coli - chemistry Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Flexibility Interface stability Kinetics Molecular dynamics Molecular Dynamics Simulation Molecules Mutation Physical Sciences PNAS Plus Protein Conformation Protein Engineering Proteins Residues Simulation Substrate Specificity Substrates Tradeoffs Transketolase Transketolase - chemistry Transketolase - genetics Transketolase - metabolism
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