Chapter

Dynamics in Enzyme Catalysis

Volume 337 of the series Topics in Current Chemistry pp 41-67

Date:

Protein Conformational Disorder and Enzyme Catalysis

  • Cindy SchulenburgAffiliated withLaboratory of Organic Chemistry, ETH Zürich
  • , Donald HilvertAffiliated withLaboratory of Organic Chemistry, ETH Zürich Email author 

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Abstract

Though lacking a well-defined three-dimensional structure, intrinsically unstructured proteins are ubiquitous in nature. These molecules play crucial roles in many cellular processes, especially signaling and regulation. Surprisingly, even enzyme catalysis can tolerate substantial disorder. This observation contravenes conventional wisdom but is relevant to an understanding of how protein dynamics modulates enzyme function. This chapter reviews properties and characteristics of disordered proteins, emphasizing examples of enzymes that lack defined structures, and considers implications of structural disorder for catalytic efficiency and evolution.

Graphical Abstract

https://static-content.springer.com/image/chp%3A10.1007%2F128_2012_411/MediaObjects/272904_1_En_411_Figa_HTML.gif

Keywords

Dynamics Evolution Intrinsic disorder Protein function Protein structure