Hyaluronidases and hyaluronate lyases: From humans to bacteriophages
Autor: | Vladimir Velebny, Lukáš Kubala, Jana Jilkova, Martin Sindelar, Kristyna Turkova |
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Rok vydání: | 2021 |
Předmět: |
Models
Molecular Protein family Linear polymer Hyaluronoglucosaminidase Context (language use) Extracellular matrix 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Colloid and Surface Chemistry Hyaluronidase Hyaluronate lyase Hyaluronic acid medicine Humans Bacteriophages Hyaluronic Acid Physical and Theoretical Chemistry 030304 developmental biology chemistry.chemical_classification 0303 health sciences Surfaces and Interfaces General Medicine Enzyme chemistry Biochemistry 030220 oncology & carcinogenesis Biotechnology medicine.drug |
Zdroj: | Colloids and Surfaces B: Biointerfaces. 208:112095 |
ISSN: | 0927-7765 |
Popis: | 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. |
Databáze: | OpenAIRE |
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