Enzyme Engineering: From Chemically Induced Modifications to Genetic Code Expansion

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (30 November 2021) | Viewed by 4381

Special Issue Editors


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Guest Editor
Children’s Cancer Institute, Lowy Cancer Research Centre, UNSW Sydney, Sydney, NSW, Australia
Interests: protein engineering; chemical biology; proteomics and drug discovery

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Guest Editor
Department Biochemistry, Federal University of Santa Catarina, Florianópolis 88040-900, Brazil
Interests: protein chemistry, protein engineering and drug discovery

Special Issue Information

Dear Colleagues,

Enzyme engineering has become extremely important for biocatalytic processes, which is observed by the amount of research that has been dedicated to this field in the past decade. This interest is due to the intrinsic features of enzymes and their advantages over chemical catalysts such as high productivity, specificity, and catalytic efficiency, but it is also faced with high cost and low stability issues. These drawbacks have propelled the development of several methods to tackle these problems while also avoiding the cost and waste associated with single-use and throwaway practices. Traditional methods of enzyme engineering have enabled the production of stable and highly efficient enzymes as well as entirely new functionalities, but they have also started to concede space to more advanced approaches. Recent efforts have focused on induced chemical modifications and genetic code expansion to install new catalytic modalities, expand acceptable substrates, and increase thermostability amongst other features. This Special Issue aims to cover the progress and trends in traditional enzyme engineering, new chemical methods to modify and modulate enzyme activity and structure, genetic code expansion by insertion of noncannocial amino acids (ncAA), and other strategies to develop innovative biocatalysts.

Dr. Jean Bertoldo
Prof. Dr. Hernán Terenzi
Guest Editors

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Keywords

  • Noncanonical amino acids (ncAAs)
  • Genetic code expansion
  • Directed evolution
  • Site-directed mutagenesis
  • Posttranslational chemical mutagenesis
  • New enzyme modalities
  • Site-specific protein modification
  • Unnatural amino acids (UAAs)
  • Protein functionalization
  • Reusable biocatalysts

Published Papers (1 paper)

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Review

20 pages, 1534 KiB  
Review
Protein Modifications: From Chemoselective Probes to Novel Biocatalysts
by Tomás Bohn Pessatti, Hernán Terenzi and Jean Borges Bertoldo
Catalysts 2021, 11(12), 1466; https://doi.org/10.3390/catal11121466 - 30 Nov 2021
Cited by 5 | Viewed by 3149
Abstract
Chemical reactions can be performed to covalently modify specific residues in proteins. When applied to native enzymes, these chemical modifications can greatly expand the available set of building blocks for the development of biocatalysts. Nucleophilic canonical amino acid sidechains are the most readily [...] Read more.
Chemical reactions can be performed to covalently modify specific residues in proteins. When applied to native enzymes, these chemical modifications can greatly expand the available set of building blocks for the development of biocatalysts. Nucleophilic canonical amino acid sidechains are the most readily accessible targets for such endeavors. A rich history of attempts to design enhanced or novel enzymes, from various protein scaffolds, has paved the way for a rapidly developing field with growing scientific, industrial, and biomedical applications. A major challenge is to devise reactions that are compatible with native proteins and can selectively modify specific residues. Cysteine, lysine, N-terminus, and carboxylate residues comprise the most widespread naturally occurring targets for enzyme modifications. In this review, chemical methods for selective modification of enzymes will be discussed, alongside with examples of reported applications. We aim to highlight the potential of such strategies to enhance enzyme function and create novel semisynthetic biocatalysts, as well as provide a perspective in a fast-evolving topic. Full article
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