ArticleScientific reports2017
Laminarinase from Flavobacterium sp. reveals the structural basis of thermostability and substrate specificity.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Genetic mechanisms for estuarine carbohydrate degradation and linked transcriptional activity.Applied and environmental microbiology · 2026Article
- A novel acidic laminarinase derived from Jermuk hot spring metagenome.Applied microbiology and biotechnology · 2025Article
- Characterization of alginate-degrading bacteria isolated from seaweed-producing areas of South Korean territory and verification of the bacteria as plant growth-promoting biofertilizer.Microbiology spectrum · 2025Article
- Molecular insights into the hydrolysis and transglycosylation of a deep-seaApplied and environmental microbiology · 2024Article
- Metagenomic analysis of carbohydrate-active enzymes and their contribution to marine sediment biodiversity.World journal of microbiology & biotechnology · 2024Article
- Distinct roles of carbohydrate-binding modules in multidomain β-1,3-1,4-glucanase on polysaccharide degradation.Applied microbiology and biotechnology · 2023Article
- Marine microbial enzymes for the production of algal oligosaccharides and its bioactive potential for application as nutritional supplements.Folia microbiologica · 2022Review
- Simple Methods for the Preparation of Colloidal Chitin, Cell Free Supernatant and Estimation of Laminarinase.Bio-protocol · 2021Article
- Molecular cloning and characterization of a thermostable and halotolerant endo-β-1,4-glucanase from3 Biotech · 2021Article
- A set of simple methods for detection and extraction of laminarinase.Scientific reports · 2021Article
- Molecular Basis for Substrate Recognition and Catalysis by a Marine Bacterial Laminarinase.Applied and environmental microbiology · 2020Article
- Comparative Genomic Study of Polar Lichen-Associated Hymenobacter sp. PAMC 26554 and Hymenobacter sp. PAMC 26628 Reveals the Presence of Polysaccharide-Degrading Ability Based on Habitat.Current microbiology · 2020Article
- Biochemical characterization of a novel ulvan lyase fromRSC advances · 2018Article
- Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds.The Journal of biological chemistryArticle
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laminarinase from Flavobacterium sp. strain UMI-01, a new member of the glycosyl hydrolase 16 family of a marine bacterium associated with seaweeds, mainly degrades β-1,3-glucosyl linkages of β-glucan (such as laminarin) through the hydrolysis of glycosidic bonds. We determined the crystal structure of ULam111 at 1.60-Å resolution to understand the structural basis for its thermostability and substrate specificity. A calcium-binding motif located on the opposite side of the β-sheet from catalytic cleft increased its degrading activity and thermostability. The disulfide bridge Cys31-Cys34, located on the β2-β3 loop near the substrate-binding site, is responsible for the thermostability of ULam111. The substrates of β-1,3-linked laminarin and β-1,3-1,4-linked glucan bound to the catalytic cleft in a completely different mode at subsite -3. Asn33 and Trp113, together with Phe212, formed hydrogen bonds with preferred substrates to degrade β-1,3-linked laminarin based on the structural comparisons. Our structural information provides new insights concerning thermostability and substrate recognition that will enable the design of industrial biocatalysts.
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