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@article{1806139,
author = {Šindelář, Martin and Jílková, Jana and Kubala, Lukáš and Velebný, Vladimír and Turková, Kristýna},
article_location = {Amsterdam},
article_number = {December},
doi = {http://dx.doi.org/10.1016/j.colsurfb.2021.112095},
keywords = {Hyaluronidase; Hyaluronate lyase; Hyaluronan; Hyaluronic acid; Catalytic residues; Bioinformatics},
language = {eng},
issn = {0927-7765},
journal = {Colloids and Surfaces B: Biointerfaces},
title = {Hyaluronidases and hyaluronate lyases: From humans to bacteriophages},
url = {https://www.sciencedirect.com/science/article/pii/S0927776521005397#!},
volume = {208},
year = {2021}
}
TY - JOUR
ID - 1806139
AU - Šindelář, Martin - Jílková, Jana - Kubala, Lukáš - Velebný, Vladimír - Turková, Kristýna
PY - 2021
TI - Hyaluronidases and hyaluronate lyases: From humans to bacteriophages
JF - Colloids and Surfaces B: Biointerfaces
VL - 208
IS - December
SP - 112095
EP - 112095
PB - Elsevier
SN - 09277765
KW - Hyaluronidase
KW - Hyaluronate lyase
KW - Hyaluronan
KW - Hyaluronic acid
KW - Catalytic residues
KW - Bioinformatics
UR - https://www.sciencedirect.com/science/article/pii/S0927776521005397#!
N2 - Hyaluronan is a non-sulfated negatively-charged linear polymer distributed in most parts of the human body, where it is located around cells in the extracellular matrix of connective tissues and plays an essential role in the organization of tissue architecture. Moreover, hyaluronan is involved in many biological processes and used in many clinical, cosmetic, pharmaceutic, and biotechnological applications worldwide. As interest in hyaluronan applications increases, so does interest in hyaluronidases and hyaluronate lyases, as these enzymes play a major part in hyaluronan degradation. Many hyaluronidases and hyaluronate lyases produced by eukaryotic cells, bacteria, and bacteriophages have so far been described and annotated, and their ability to cleave hyaluronan has been experimentally proven. These enzymes belong to several carbohydrate-active enzyme families, share very low sequence identity, and differ in their cleaving mechanisms and in their structural and functional properties. This review presents a summary of annotated and characterized hyaluronidases and hyaluronate lyases isolated from different sources belonging to distinct protein families, with a main focus on the binding and catalytic residues of the discussed enzymes in the context of their biochemical properties. In addition, the application potential of individual groups of hyaluronidases and hyaluronate lyases is evaluated.
ER -
ŠINDELÁŘ, Martin, Jana JÍLKOVÁ, Lukáš KUBALA, Vladimír VELEBNÝ a Kristýna TURKOVÁ. Hyaluronidases and hyaluronate lyases: From humans to bacteriophages. \textit{Colloids and Surfaces B: Biointerfaces}. Amsterdam: Elsevier, 2021, roč.~208, December, s.~112095-112106. ISSN~0927-7765. Dostupné z: https://dx.doi.org/10.1016/j.colsurfb.2021.112095.
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