Hyaluronidases and hyaluronate lyases: From humans to bacteriophages

0551015 - BFÚ 2022 RIV NL eng J - Článek v odborném periodiku
Šindelář, Martin - Jílková, J. - Kubala, Lukáš - Velebný, V. - Turková, Kristýna
Hyaluronidases and hyaluronate lyases: From humans to bacteriophages.
Colloids and Surfaces B-Biointerfaces. Roč. 208, DEC 2021 (2021), č. článku 112095. ISSN 0927-7765. E-ISSN 1873-4367
Institucionální podpora: RVO:68081707
Klíčová slova: recombinant human hyaluronidase * bovine testicular hyaluronidase * transmembrane protein-2 tmem2 * multiple sequence alignment
Obor OECD: Biophysics
Impakt faktor: 5.999, rok: 2021
Způsob publikování: Omezený přístup
https://reader.elsevier.com/reader/sd/pii/S0927776521005397?token=B63C001E648671B6F3914EE9CD59A205B3E4831DB2E398A1F40A00EEDAB06741F85D486679B48D746754AE338B7F2A9C&originRegion=eu-west-1&originCreation=20220106121018

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.
Trvalý link: http://hdl.handle.net/11104/0326293