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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Modulating Enzyme Function via Dynamic Allostery within Biliverdin Reductase B.

Jasmina S Redzic1, Michael R Duff2, Ashley Blue3

  • 1Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, Denver, CO, United States.

Frontiers in Molecular Biosciences
|June 7, 2021
PubMed
Summary
This summary is machine-generated.

Biliverdin reductase B (BLVRB) enzymes use dynamic, evolutionarily changed sites distant from the active site to control cellular redox regulation. Mutations at these sites globally modulate enzyme motions and coenzyme binding, impacting function.

Keywords:
NMRallosterycouplingdynamicsenzymereductase

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Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Dynamics

Background:

  • Biliverdin reductase B (BLVRB) enzymes are crucial for cellular redox regulation, catalyzing NADPH-dependent flavin reduction.
  • The roles of enzyme dynamics and allostery in BLVRB function remain largely unexplored.

Purpose of the Study:

  • To investigate the influence of enzyme dynamics and allosteric regulation on BLVRB activity.
  • To identify specific residues that modulate BLVRB's global motions and catalytic function.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) relaxation studies to analyze inherent protein dynamics.
  • Relaxation And Single Site Multiple Mutations (RASSMM) approach to assess functional and dynamic effects of mutations.
  • Comparative analysis of evolutionarily distinct BLVRB homologues.

Main Results:

  • A residue (T164) 15 Å from the active site exhibits inherent dynamics and can control global micro-millisecond motions.
  • Mutagenic effects at T164 correlate with evolutionary changes and modulate coenzyme binding.
  • Distal, evolutionarily modified sites act as dynamic regulators of BLVRB function.

Conclusions:

  • Enzyme dynamics and allosteric regulation are critical for BLVRB function.
  • Evolutionary adaptations at distal sites fine-tune enzyme activity by modulating protein dynamics and coenzyme binding.
  • BLVRB's global dynamics comprise coupled motions intrinsically linked to its catalytic role.