Multidomain chimeric enzymes as a promising alternative for biocatalysts improvement: a minireview

Mol Biol Rep. 2024 Mar 11;51(1):410. doi: 10.1007/s11033-024-09332-9.

Abstract

Searching for new and better biocatalysts is an area of study in constant development. In nature, mechanisms generally occurring in evolution, such as genetic duplication, recombination, and natural selection processes, produce various enzymes with different architectures and properties. The recombination of genes that code proteins produces multidomain chimeric enzymes that contain two or more domains that sometimes enhance their catalytic properties. Protein engineering has mimicked this process to enhance catalytic activity and the global stability of enzymes, searching for new and better biocatalysts. Here, we present and discuss examples from both natural and synthetic multidomain chimeric enzymes and how additional domains heighten their stability and catalytic activity. Moreover, we also describe progress in developing new biocatalysts using synthetic fusion enzymes and revise some methodological strategies to improve their biological fitness.

Keywords: Chimeric enzymes; Enzyme activity; Enzyme stability; Fusion enzymes; Multidomain enzymes.

Publication types

  • Review

MeSH terms

  • Biocatalysis
  • Catalysis
  • Enzymes
  • Gene Duplication*
  • Protein Engineering*
  • Recombinant Fusion Proteins / genetics

Substances

  • Recombinant Fusion Proteins
  • Enzymes