Number of the records: 1  

Hyaluronidases and hyaluronate lyases: From humans to bacteriophages

  1. 1.
    SYSNO ASEP0551015
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleHyaluronidases 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) ORCID
    Number of authors5
    Article number112095
    Source TitleColloids and Surfaces B-Biointerfaces. - : Elsevier - ISSN 0927-7765
    Roč. 208, DEC 2021 (2021)
    Number of pages12 s.
    Publication formOnline - E
    Languageeng - English
    CountryNL - Netherlands
    Keywordsrecombinant human hyaluronidase ; bovine testicular hyaluronidase ; transmembrane protein-2 tmem2 ; multiple sequence alignment
    Subject RIVBO - Biophysics
    OECD categoryBiophysics
    Method of publishingLimited access
    Institutional supportBFU-R - RVO:68081707
    UT WOS000709747600001
    EID SCOPUS85114385081
    DOI10.1016/j.colsurfb.2021.112095
    AnnotationHyaluronan 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.
    WorkplaceInstitute of Biophysics
    ContactJana Poláková, polakova@ibp.cz, Tel.: 541 517 244
    Year of Publishing2022
    Electronic addresshttps://reader.elsevier.com/reader/sd/pii/S0927776521005397?token=B63C001E648671B6F3914EE9CD59A205B3E4831DB2E398A1F40A00EEDAB06741F85D486679B48D746754AE338B7F2A9C&originRegion=eu-west-1&originCreation=20220106121018
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.