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Cooperativity and flexibility in enzyme evolution
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DOI：10.1016/j.sbi.2017.10.020.png)
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Abstract
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Enzymes are flexible catalysts, and there has been substantial discussion about the extent to which this flexibility contributes to their catalytic efficiency. What has been significantly less discussed is the extent to which this flexibility contributes to their evolvability. Despite this, recent years have seen an increasing number of both experimental and computational studies that demonstrate that cooperativity and flexibility play significant roles in enzyme innovation. This review covers key developments in the field that emphasize the importance of enzyme dynamics not just to the evolution of new enzyme function(s), but also as a property that can be harnessed in the design of new artificial enzymes.
Keywords:
HUMAN DIHYDROFOLATE-REDUCTASE
ALKALINE-PHOSPHATASE
CATALYTIC PROMISCUITY
CONFORMATIONAL DIVERSITY
PROTEIN DYNAMICS
TRANSITION-STATE
STAPHYLOCOCCAL NUCLEASE
PHOSPHORYL-TRANSFER
SULFATASE ACTIVITY
TRANSIENT-STATE
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