Engineered control of enzyme structural dynamics and function

David D. Boehr, Rebecca N. D'Amico, Kathleen F. O'Rourke

Research output: Contribution to journalReview article

7 Citations (Scopus)

Abstract

Enzymes undergo a range of internal motions from local, active site fluctuations to large-scale, global conformational changes. These motions are often important for enzyme function, including in ligand binding and dissociation and even preparing the active site for chemical catalysis. Protein engineering efforts have been directed towards manipulating enzyme structural dynamics and conformational changes, including targeting specific amino acid interactions and creation of chimeric enzymes with new regulatory functions. Post-translational covalent modification can provide an additional level of enzyme control. These studies have not only provided insights into the functional role of protein motions, but they offer opportunities to create stimulus-responsive enzymes. These enzymes can be engineered to respond to a number of external stimuli, including light, pH, and the presence of novel allosteric modulators. Altogether, the ability to engineer and control enzyme structural dynamics can provide new tools for biotechnology and medicine.

Original languageEnglish (US)
Pages (from-to)825-838
Number of pages14
JournalProtein Science
Volume27
Issue number4
DOIs
StatePublished - Apr 2018

Fingerprint

Structural dynamics
Enzymes
Catalytic Domain
Protein Engineering
Post Translational Protein Processing
Biotechnology
Articular Range of Motion
Catalysis
Modulators
Medicine
Proteins
Ligands
Light
Amino Acids
Engineers

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Boehr, David D. ; D'Amico, Rebecca N. ; O'Rourke, Kathleen F. / Engineered control of enzyme structural dynamics and function. In: Protein Science. 2018 ; Vol. 27, No. 4. pp. 825-838.
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Engineered control of enzyme structural dynamics and function. / Boehr, David D.; D'Amico, Rebecca N.; O'Rourke, Kathleen F.

In: Protein Science, Vol. 27, No. 4, 04.2018, p. 825-838.

Research output: Contribution to journalReview article

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