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| Main Authors: | , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
International journal of biological macromolecules
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/40057069/ |
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| _version_ | 1868266234545438720 |
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| author | Wei, Quanfeng Li, Zhenhua Liang, Min Shen, Naikun Pan, Lixia Jiang, Mingguo Yang, Dengfeng |
| author_facet | Wei, Quanfeng Li, Zhenhua Liang, Min Shen, Naikun Pan, Lixia Jiang, Mingguo Yang, Dengfeng Wei, Quanfeng Li, Zhenhua Liang, Min Shen, Naikun Pan, Lixia Jiang, Mingguo Yang, Dengfeng |
| collection | PubMed - marine biology |
| contents | Discovery and characterization of a novel alginate lyase PeAly15 and its truncated protein DUF4962 domain from Paenibacillus elgii HSFD1: Elucidation the molecular mechanism of endolytic mode. Wei, Quanfeng Li, Zhenhua Liang, Min Shen, Naikun Pan, Lixia Jiang, Mingguo Yang, Dengfeng Paenibacillus Polysaccharide-Lyases Bacterial Proteins Protein Domains Alginates Oligosaccharides Hydrolysis Amino Acid Sequence Substrate Specificity Exolytic alginate lyases belonging to the PL15 family consist of two distinct domains: DUF4962 and Hepar_II_III. However, the specific functional roles of these domains have been scarcely investigated. In this study, we identified a novel alginate lyase, designated PeAly15, through comprehensive genomic analysis of the alginate-degrading bacterium Paenibacillus elgii HSFD1. To accurately investigate the functional roles of each domain, we obtained three proteins: the full-length PeAly15-FULL and two truncated proteins, PeAly15-DUF and PeAly15-Hepar. HPLC and LC-MS analyses of the enzymatic hydrolysis products revealed that PeAly15-FULL is an unusual endolytic alginate lyase, predominantly producing oligosaccharides with degrees of polymerization (DP) of 2 and 3. Intriguingly, unlike other members of the PL15 family, PeAly15-DUF exhibited extensive endolytic activity as a single domain, yielding a mixture of oligosaccharides ranging from ΔDP2 to ΔDP6. In contrast, PeAly15-Hepar demonstrated no activity towards sodium alginate, suggesting that it may serve solely a structural role. These findings provide novel insights into the endolytic mechanism of the PL15 family and its constituent domains. |
| format | Artículo científico |
| id | pubmed_40057069 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | International journal of biological macromolecules |
| record_format | pubmed |
| spellingShingle | Discovery and characterization of a novel alginate lyase PeAly15 and its truncated protein DUF4962 domain from Paenibacillus elgii HSFD1: Elucidation the molecular mechanism of endolytic mode. Wei, Quanfeng Li, Zhenhua Liang, Min Shen, Naikun Pan, Lixia Jiang, Mingguo Yang, Dengfeng Paenibacillus Polysaccharide-Lyases Bacterial Proteins Protein Domains Alginates Oligosaccharides Hydrolysis Amino Acid Sequence Substrate Specificity Discovery and characterization of a novel alginate lyase PeAly15 and its truncated protein DUF4962 domain from Paenibacillus elgii HSFD1: Elucidation the molecular mechanism of endolytic mode. Wei, Quanfeng Li, Zhenhua Liang, Min Shen, Naikun Pan, Lixia Jiang, Mingguo Yang, Dengfeng Paenibacillus Polysaccharide-Lyases Bacterial Proteins Protein Domains Alginates Oligosaccharides Hydrolysis Amino Acid Sequence Substrate Specificity Exolytic alginate lyases belonging to the PL15 family consist of two distinct domains: DUF4962 and Hepar_II_III. However, the specific functional roles of these domains have been scarcely investigated. In this study, we identified a novel alginate lyase, designated PeAly15, through comprehensive genomic analysis of the alginate-degrading bacterium Paenibacillus elgii HSFD1. To accurately investigate the functional roles of each domain, we obtained three proteins: the full-length PeAly15-FULL and two truncated proteins, PeAly15-DUF and PeAly15-Hepar. HPLC and LC-MS analyses of the enzymatic hydrolysis products revealed that PeAly15-FULL is an unusual endolytic alginate lyase, predominantly producing oligosaccharides with degrees of polymerization (DP) of 2 and 3. Intriguingly, unlike other members of the PL15 family, PeAly15-DUF exhibited extensive endolytic activity as a single domain, yielding a mixture of oligosaccharides ranging from ΔDP2 to ΔDP6. In contrast, PeAly15-Hepar demonstrated no activity towards sodium alginate, suggesting that it may serve solely a structural role. These findings provide novel insights into the endolytic mechanism of the PL15 family and its constituent domains. |
| title | Discovery and characterization of a novel alginate lyase PeAly15 and its truncated protein DUF4962 domain from Paenibacillus elgii HSFD1: Elucidation the molecular mechanism of endolytic mode. |
| topic | Paenibacillus Polysaccharide-Lyases Bacterial Proteins Protein Domains Alginates Oligosaccharides Hydrolysis Amino Acid Sequence Substrate Specificity |
| url | https://pubmed.ncbi.nlm.nih.gov/40057069/ |