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Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes
Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan. Glycoside hydrolase...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4663542/ https://www.ncbi.nlm.nih.gov/pubmed/26516868 http://dx.doi.org/10.3390/md13116566 |
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author | Viens, Pascal Lacombe-Harvey, Marie-Ève Brzezinski, Ryszard |
author_facet | Viens, Pascal Lacombe-Harvey, Marie-Ève Brzezinski, Ryszard |
author_sort | Viens, Pascal |
collection | PubMed |
description | Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan. Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level. They were also subjected to numerous site-directed mutagenesis studies, unraveling the molecular mechanisms of hydrolysis. This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms. |
format | Online Article Text |
id | pubmed-4663542 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-46635422015-12-10 Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes Viens, Pascal Lacombe-Harvey, Marie-Ève Brzezinski, Ryszard Mar Drugs Review Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan. Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level. They were also subjected to numerous site-directed mutagenesis studies, unraveling the molecular mechanisms of hydrolysis. This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms. MDPI 2015-10-28 /pmc/articles/PMC4663542/ /pubmed/26516868 http://dx.doi.org/10.3390/md13116566 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Viens, Pascal Lacombe-Harvey, Marie-Ève Brzezinski, Ryszard Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes |
title | Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes |
title_full | Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes |
title_fullStr | Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes |
title_full_unstemmed | Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes |
title_short | Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes |
title_sort | chitosanases from family 46 of glycoside hydrolases: from proteins to phenotypes |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4663542/ https://www.ncbi.nlm.nih.gov/pubmed/26516868 http://dx.doi.org/10.3390/md13116566 |
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