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

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 recombi...

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Bibliographic Details
Published in:Molecular biology reports 2024-12, Vol.51 (1), p.410-410, Article 410
Main Authors: García-Paz, Flor de María, Del Moral, Sandra, Morales-Arrieta, Sandra, Ayala, Marcela, Treviño-Quintanilla, Luis Gerardo, Olvera-Carranza, Clarita
Format: Article
Language:English
Subjects:
Animal Anatomy
Animal Biochemistry
Biocatalysis
Biocatalysts
Biomedical and Life Sciences
Catalysis
Cytochrome
Enzymes
Gene Duplication
Histology
Life Sciences
Mini Review
Molecular biology
Morphology
Natural selection
Protein Engineering
Proteins
Recombinant Fusion Proteins - genetics
Recombination
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Summary: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.
ISSN:0301-4851
1573-4978
DOI:10.1007/s11033-024-09332-9