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Hyaluronidases and hyaluronate lyases: From humans to bacteriophages
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SYSNO ASEP 0551015 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Hyaluronidases and hyaluronate lyases: From humans to bacteriophages Author(s) Šindelář, Martin (BFU-R) ORCID
Jílková, J. (CZ)
Kubala, Lukáš (BFU-R) RID, ORCID
Velebný, V. (CZ)
Turková, Kristýna (BFU-R) ORCIDNumber of authors 5 Article number 112095 Source Title Colloids and Surfaces B-Biointerfaces. - : Elsevier - ISSN 0927-7765
Roč. 208, DEC 2021 (2021)Number of pages 12 s. Publication form Online - E Language eng - English Country NL - Netherlands Keywords recombinant human hyaluronidase ; bovine testicular hyaluronidase ; transmembrane protein-2 tmem2 ; multiple sequence alignment Subject RIV BO - Biophysics OECD category Biophysics Method of publishing Limited access Institutional support BFU-R - RVO:68081707 UT WOS 000709747600001 EID SCOPUS 85114385081 DOI 10.1016/j.colsurfb.2021.112095 Annotation 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. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2022 Electronic address https://reader.elsevier.com/reader/sd/pii/S0927776521005397?token=B63C001E648671B6F3914EE9CD59A205B3E4831DB2E398A1F40A00EEDAB06741F85D486679B48D746754AE338B7F2A9C&originRegion=eu-west-1&originCreation=20220106121018
Number of the records: 1