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Understanding enzyme function evolution from a computational perspective
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DOI：10.1016/j.sbi.2017.08.003.png)
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Abstract
En 中文
In this review, we will explore recent computational approaches to understand enzyme evolution from the perspective of protein structure, dynamics and promiscuity. We will present quantitative methods to measure the size of evolutionary steps within a structural domain, allowing the correlation between change in substrate and domain structure to be assessed, and giving insights into the evolvability of different domains in terms of the number, types and sizes of evolutionary steps observed. These approaches will help to understand the evolution of new catalytic and non-catalytic functionality in response to environmental demands, showing potential to guide de novoenzyme design and directed evolution experiments.
Keywords:
DIRECTED EVOLUTION
SUBSTRATE-SPECIFICITY
ADAPTIVE EVOLUTION
SYNTHETIC BIOLOGY
PROTEIN EVOLUTION
LARGE-SCALE
TRADE-OFFS
DYNAMICS
BIOCATALYSIS
PROMISCUITY
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