Identification and biochemical characterization of a novel chondroitin sulfate/dermantan sulfate lyase from Photobacterium sp
| Autor: | Lu Danrong, Lin Wei, Fuchuan Li, Wenshuang Wang, Qingdong Zhang, Wang Shumin |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Time Factors
Stereochemistry Dermatan Sulfate 02 engineering and technology Biochemistry Dermatan sulfate Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Structural Biology Chondroitin sulfate Sulfate Molecular Biology Phylogeny 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology Chondroitin Lyases Photobacterium Sulfates Chondroitin Sulfates Substrate (chemistry) General Medicine 021001 nanoscience & nanotechnology HEXA biology.organism_classification Lyase Recombinant Proteins Enzyme chemistry Mutation Biocatalysis 0210 nano-technology Bacteria |
| Zdroj: | International journal of biological macromolecules. 165 |
| ISSN: | 1879-0003 |
| Popis: | Chondroitin sulfate (CS)/dermatan sulfate (DS) lyases play important roles in structural and functional studies of CS/DS. In this study, a novel CS/DS lyase (enCSase) was identified from the genome of the marine bacterium Photobacterium sp. QA16. This enzyme is easily heterologously expressed and purified as highly active form against various CS, DS and hyaluronic acid (HA). Under the optimal conditions, the specific activities of this enzyme towards CSA, CSC, CSD, CSE, DS and HA were 373, 474, 171, 172, 141 and 97 U/mg of proteins, respectively. As an endolytic enzyme, enCSase degrades HA to unsaturated hexa- and tetrasaccharides but CS/DS to unsaturated tetra- and disaccharides as the final products. Sequencing analysis showed that the structures of tetrasaccharides in the final products of CS variants were not unique but were highly variable, indicating the randomness of substrate degradation by this enzyme. Further studies showed that the smallest substrate of enCSase was octasaccharide for HA but hexasaccharide for CS/DS, which could explain why this enzyme cannot degrade HA hexa- and tetrasaccharides and CS/DS tetrasaccharides further. It is believed that enCSase may be a very useful tool for structural and functional studies and related applications of CS/DS and HA. |
| Databáze: | OpenAIRE |
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