A thermostable enzyme as an experimental platform to study properties of less stable homologues

Protein Eng Des Sel. 2004 Jul;17(7):553-5. doi: 10.1093/protein/gzh069. Epub 2004 Aug 27.

Abstract

The structural and functional characterization of proteins is frequently hampered by lack of stability or by insufficient assembly of oligomeric proteins in over-expression systems. Using F(1)-ATPase as a case study, we tackled this problem by introducing function-determining domains from a difficult-to-handle variety of an enzyme into a stable homologue.

MeSH terms

  • Amino Acid Sequence
  • Chloroplasts / metabolism
  • Enzyme Stability
  • Enzymes / chemistry*
  • Hot Temperature
  • Kinetics
  • Mitochondria / chemistry
  • Models, Biological
  • Molecular Sequence Data
  • Plant Proteins / chemistry
  • Protein Conformation
  • Protein Engineering / methods*
  • Proteins / chemistry
  • Proton-Translocating ATPases / chemistry*
  • Recombinant Fusion Proteins / chemistry
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Temperature

Substances

  • Enzymes
  • Plant Proteins
  • Proteins
  • Recombinant Fusion Proteins
  • Proton-Translocating ATPases