Gates of Enzymes

Authors

Gora, A., Brezovský, J., Damborský, J.

Source

Chemical Reviews 113

Abstract

Enzymes are very efficient catalysts that are essential for the functioning of living organisms. The low efficiency of biocatalysts produced de novo relative to those that have evolved naturally demonstrates that our understanding of enzymatic catalysis is still incomplete. The dynamic motion of enzymes during catalytic events is one of the many aspects of protein chemistry that are currently insufficiently well understood. On one hand, proteins need to have well-defined and organized structures in order to maintain stable functionality in the intracellular environment. On the other hand, some degree of flexibility is often required for catalytic activity. Molecular dynamics simulations have provided key insights into the importance of protein dynamics in catalysis, such as the observation of substrate access and product exit pathways that cannot be identified by inspecting crystal structures.10 Csermely et al. recently reported that mutations in regions that affect protein dynamics, such as hinge regions that are important in substrate binding, can have dramatic effects on catalytic activity.11 In this review, we highlight the role of protein gates as another class of highly dynamic structures that play key roles in protein function.

Source

Gora, A., Brezovský, J., Damborský, J.: Gates of Enzymes, Chemical Reviews, 113, 5871–5923, 2013.
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