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Recent structural insights into the mechanism of lysozyme hydrolysis
Lysozyme hydrolyzes the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycans located in the bacterial cell wall. The mechanism of the hydrolysis reaction of lysozyme was first studied more than 50 years ago; however, it has not yet been fully elucidated and various...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7919404/ https://www.ncbi.nlm.nih.gov/pubmed/33645532 http://dx.doi.org/10.1107/S2059798321000346 |
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author | Tanaka, Ichiro Nishinomiya, Ryota Goto, Ryosuke Shimazaki, Shun Chatake, Toshiyuki |
author_facet | Tanaka, Ichiro Nishinomiya, Ryota Goto, Ryosuke Shimazaki, Shun Chatake, Toshiyuki |
author_sort | Tanaka, Ichiro |
collection | PubMed |
description | Lysozyme hydrolyzes the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycans located in the bacterial cell wall. The mechanism of the hydrolysis reaction of lysozyme was first studied more than 50 years ago; however, it has not yet been fully elucidated and various mechanisms are still being investigated. One reaction system that has commonly been proposed is that the lysozyme intermediate undergoes covalent ligand binding during hydrolysis. However, these findings resulted from experiments performed under laboratory conditions using fluorine-based ligands, which facilitate the formation of covalent bonds between the ligands and the catalytic side chain of lysozyme. More recently, high-resolution X-ray structural analysis was used to study the complex of lysozyme with an N-acetylglucosamine tetramer. As a result, the carboxyl group of Asp52 was found to form a relatively strong hydrogen-bond network and had difficulty binding covalently to C1 of the carbohydrate ring. To confirm this hydrogen-bond network, neutron test measurements were successfully performed to a resolution of better than 1.9 Å. |
format | Online Article Text |
id | pubmed-7919404 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-79194042021-03-10 Recent structural insights into the mechanism of lysozyme hydrolysis Tanaka, Ichiro Nishinomiya, Ryota Goto, Ryosuke Shimazaki, Shun Chatake, Toshiyuki Acta Crystallogr D Struct Biol Isdsb2019 Lysozyme hydrolyzes the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycans located in the bacterial cell wall. The mechanism of the hydrolysis reaction of lysozyme was first studied more than 50 years ago; however, it has not yet been fully elucidated and various mechanisms are still being investigated. One reaction system that has commonly been proposed is that the lysozyme intermediate undergoes covalent ligand binding during hydrolysis. However, these findings resulted from experiments performed under laboratory conditions using fluorine-based ligands, which facilitate the formation of covalent bonds between the ligands and the catalytic side chain of lysozyme. More recently, high-resolution X-ray structural analysis was used to study the complex of lysozyme with an N-acetylglucosamine tetramer. As a result, the carboxyl group of Asp52 was found to form a relatively strong hydrogen-bond network and had difficulty binding covalently to C1 of the carbohydrate ring. To confirm this hydrogen-bond network, neutron test measurements were successfully performed to a resolution of better than 1.9 Å. International Union of Crystallography 2021-02-19 /pmc/articles/PMC7919404/ /pubmed/33645532 http://dx.doi.org/10.1107/S2059798321000346 Text en © Tanaka et al. 2021 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Isdsb2019 Tanaka, Ichiro Nishinomiya, Ryota Goto, Ryosuke Shimazaki, Shun Chatake, Toshiyuki Recent structural insights into the mechanism of lysozyme hydrolysis |
title | Recent structural insights into the mechanism of lysozyme hydrolysis |
title_full | Recent structural insights into the mechanism of lysozyme hydrolysis |
title_fullStr | Recent structural insights into the mechanism of lysozyme hydrolysis |
title_full_unstemmed | Recent structural insights into the mechanism of lysozyme hydrolysis |
title_short | Recent structural insights into the mechanism of lysozyme hydrolysis |
title_sort | recent structural insights into the mechanism of lysozyme hydrolysis |
topic | Isdsb2019 |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7919404/ https://www.ncbi.nlm.nih.gov/pubmed/33645532 http://dx.doi.org/10.1107/S2059798321000346 |
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