{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tian M"],"funding":["Natural Science Foundation of Guangxi Province"],"pagination":["9916-9927"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11429652"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["46(9)"],"pubmed_abstract":["Dermatan sulfate and chondroitin sulfate are dietary supplements that can be utilized as prophylactics against thrombus formation. Low-molecular-weight dermatan sulfate (LMWDS) is particularly advantageous due to its high absorbability. The enzymatic synthesis of low-molecular-weight dermatan sulfates (LMWDSs) using chondroitin B lyase is a sustainable and environmentally friendly approach to manufacturing. However, the industrial application of chondroitin B lyases is severely hampered by their low catalytic activity. To improve the activity, a semi-rational design strategy of engineering the substrate-binding domain of chondroitin B lyase was performed based on the structure. The binding domain was subjected to screening of critical residues for modification using multiple sequence align"],"journal":["Current issues in molecular biology"],"pubmed_title":["Engineering of Substrate-Binding Domain to Improve Catalytic Activity of Chondroitin B Lyase with Semi-Rational Design."],"pmcid":["PMC11429652"],"funding_grant_id":["2021GXNSFAA196005"],"pubmed_authors":["Wang YL","Tian M","Yu S","Li YN","Zhang YW","Ma XL","Xu YY"],"additional_accession":[]},"is_claimable":false,"name":"Engineering of Substrate-Binding Domain to Improve Catalytic Activity of Chondroitin B Lyase with Semi-Rational Design.","description":"Dermatan sulfate and chondroitin sulfate are dietary supplements that can be utilized as prophylactics against thrombus formation. Low-molecular-weight dermatan sulfate (LMWDS) is particularly advantageous due to its high absorbability. The enzymatic synthesis of low-molecular-weight dermatan sulfates (LMWDSs) using chondroitin B lyase is a sustainable and environmentally friendly approach to manufacturing. However, the industrial application of chondroitin B lyases is severely hampered by their low catalytic activity. To improve the activity, a semi-rational design strategy of engineering the substrate-binding domain of chondroitin B lyase was performed based on the structure. The binding domain was subjected to screening of critical residues for modification using multiple sequence align","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Sep","modification":"2026-04-21T03:24:46.565Z","creation":"2025-04-04T19:38:41.192Z"},"accession":"S-EPMC11429652","cross_references":{"pubmed":["39329943"],"doi":["10.3390/cimb46090591"]}}