Carbohydrate-Active Enzymes: Structure, Activity and Reaction Products 2020

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Biochemistry, Biophysics and Computational Biology".

Deadline for manuscript submissions: closed (30 November 2020) | Viewed by 3289

Special Issue Editor

Special Issue Information

Dear Colleagues,

Carbohydrate-active enzymes are responsible for both biosynthesis and breakdown of carbohydrates and glycoconjugates. They are involved in many metabolic pathways, in the biosynthesis and degradation of various biomolecules such as bacterial exopolysaccharides, starch, cellulose and lignin, and in the glycosylation of proteins and lipids. Carbohydrate-active enzymes are classified into glycoside hydrolases, glycosyltransferases, polysaccharide lyases, carbohydrate esterases, and enzymes with auxiliary activities (CAZy database, www.cazy.org). Glycosyltransferases synthesize a huge variety of complex carbohydrates with different degrees of polymerization, moieties and branching. On the other hand, complex carbohydrates breakdown is carried out by glycoside hydrolases, polysaccharide lyases and carbohydrate esterases. Their interesting reactions have attracted the attention of researchers belonging to different scientific fields ranging from basic research to biotechnology. Interest in carbohydrate-active enzymes is due not only to their ability to build and degrade biopolymers—which is highly relevant in biotechnology—but also because they are involved in bacterial biofilm formation, and in glycosylation of proteins and lipids, with important health implications.

The journals IJMS and Life will jointly be publishing a Special Issue covering the topic "Carbohydrate-Active Enzymes: Structure, Activity and Reaction Products 2020". This Special Issue aims at gathering new research results to broaden our understanding about carbohydrate-active enzymes, their mutants and their reaction products at the molecular level.

It focuses on enzymes active in the biosynthesis, modification and degradation of oligo and polysaccharides, and glycoproteins and glycolipids.

Authors are invited to submit their original research and review articles.

The following topics are relevant to this Special Issue.

  • Purification and biochemical characterization of enzymes and/or their mutants
  • Biophysical characterization of enzymes and/or their mutants;
  • Investigation of structure and function relationship by NMR and X-ray crystallography;
  • Structural and functional comparison of enzymes from different organisms;
  • Proposals of substrate binding mode and reaction mechanism of enzymes and/or their mutants;
  • Study of the functional and conformational changes of enzymes upon mutation;
  • Homology modelling of enzymes;
  • Molecular docking of substrates/products in the active site of enzymes and/or their mutants;
  • Molecular characterization of oligo and polysaccharides;
  • Enzyme engineering

Prof. Dr. Stefano Benini
Guest Editor

Manuscript Submission Information

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Biochemistry
  • X-ray crystallography
  • NMR
  • Enzyme engineering
  • Directed evolution
  • Protein Glycosylation
  • Lipid Glycosylation
  • Glycosyltransferase
  • Glycoside hydrolase
  • Polysaccharide lyase
  • Carbohydrate esterase
  • Oligosaccharide
  • Polysaccharide
  • Glycoprotein
  • Glycolipid
  • Structure and function relationship

Published Papers (1 paper)

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Research

15 pages, 2684 KiB  
Article
Biochemical Characterization of a Bifunctional Enzyme Constructed by the Fusion of a Glucuronan Lyase and a Chitinase from Trichoderma sp.
by Zeineb Baklouti, Cédric Delattre, Guillaume Pierre, Christine Gardarin, Slim Abdelkafi, Philippe Michaud and Pascal Dubessay
Life 2020, 10(10), 234; https://doi.org/10.3390/life10100234 - 8 Oct 2020
Cited by 8 | Viewed by 2924
Abstract
Bifunctional enzymes created by the fusion of a glucuronan lyase (TrGL) and a chitinase (ThCHIT42) from Trichoderma sp. have been constructed with the aim to validate a proof of concept regarding the potential of the chimera lyase/hydrolase by analyzing the functionality and the [...] Read more.
Bifunctional enzymes created by the fusion of a glucuronan lyase (TrGL) and a chitinase (ThCHIT42) from Trichoderma sp. have been constructed with the aim to validate a proof of concept regarding the potential of the chimera lyase/hydrolase by analyzing the functionality and the efficiency of the chimeric constructions compared to parental enzymes. All the chimeric enzymes, including or nor linker (GGGGS), were shown functional with activities equivalent or higher to native enzymes. The velocity of glucuronan lyase was considerably increased for chimeras, and may involved structural modifications at the active site. The fusion has induced a slightly decrease of the thermostability of glucuronan lyase, without modifying its catalytic activity regarding pH variations ranging from 5 to 8. The biochemical properties of chitinase seemed to be more disparate between the different fusion constructions suggesting an impact of the linkers or structural interactions with the linked glucuronan lyase. The chimeric enzymes displayed a decreased stability to temperature and pH variations, compared to parental one. Overall, TrGL-ThCHIT42 offered the better compromise in terms of biochemical stability and enhanced activity, and could be a promising candidate for further experiments in the field of fungi Cell Wall-Degrading Enzymes (CWDEs). Full article
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