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Exploring the potential impact of an expanded genetic code on protein function.

Han Xiao1, Fariborz Nasertorabi2, Sei-Hyun Choi1

  • 1Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037;

Proceedings of the National Academy of Sciences of the United States of America
|June 4, 2015
PubMed
Summary
This summary is machine-generated.

Organisms with expanded genetic codes may gain evolutionary advantages. A novel mutation using a noncanonical amino acid in TEM-1 β-lactamase enhanced enzyme efficiency, suggesting benefits of a broader amino acid repertoire.

Keywords:
beta-lactamasecatalytic activityconformational effectsevolutionary advantagenoncanonical amino acid

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • All known organisms utilize 20 canonical amino acids.
  • The evolutionary implications of organisms with additional amino acids are largely unexplored.

Purpose of the Study:

  • To investigate if incorporating noncanonical amino acids into enzymes can confer an evolutionary advantage.
  • To explore the structural and functional consequences of such modifications.

Main Methods:

  • Created a library of mutant TEM-1 β-lactamase enzymes with 10 different noncanonical amino acids at random single sites.
  • Screened mutants for enhanced activity against the antibiotic cephalexin.
  • Determined X-ray crystal structures of wild-type and mutant enzymes, including acyl-enzyme intermediates.

Main Results:

  • Identified a specific mutation, Val-216 substituted with p-acrylamido-phenylalanine (AcrF), that significantly increased catalytic efficiency (kcat) without altering substrate binding (KM).
  • Structural analysis revealed that the Val-216-AcrF mutation induces conformational changes in active site residues, lowering the activation energy for the transacylation reaction.
  • Canonical amino acid substitutions at Val-216 did not replicate the observed functional enhancement.

Conclusions:

  • An expanded genetic code, utilizing noncanonical amino acids, can provide novel solutions for protein evolution and functional enhancement.
  • The Val-216-AcrF mutation in TEM-1 β-lactamase demonstrates a pathway for improving enzyme activity through noncanonical amino acid incorporation.
  • This study provides evidence for a potential evolutionary advantage conferred by expanded amino acid repertoires in organisms.