ArticleThe Journal of biological chemistry2014
A polysaccharide lyase from Stenotrophomonas maltophilia with a unique, pH-regulated substrate specificity.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- Enzyme-enhanced RNA isolation from biofilm-producing bacteria.Microbiology spectrum · 2026Article
- Discovery of a bacteriophage sequence in a mite genome assembly reveals bacterial contamination and opens new possibilities for exploring arthropod symbionts.Microbial genomics · 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
- Insights into putative alginate lyases from epipelagic and mesopelagic communities of the global ocean.Scientific reports · 2025Article
- Biochemical Characterization of Hyaluronate Lyase CpHly8 from an Intestinal Microorganism Clostridium perfringens G1121.Applied biochemistry and biotechnology · 2025Article
- Applying a polysaccharide lyase fromApplied and environmental microbiology · 2025Article
- Genomic and mutational analysis of Pseudomonas syringae pv. tagetis EB037 pathogenicity on sunflower.BMC microbiology · 2025Article
- Heterologous Expression and Characterization of Cellouronate (β-1,4-Glucuronan) Lyase from a Human Intestinal BacteriumJournal of applied glycoscience · 2025Article
- Pseudoalteromonas agarivorans-derived novel ulvan lyase of polysaccharide lyase family 40: Potential application of ulvan and partially hydrolyzed products in cosmetic industry.Journal of industrial microbiology & biotechnology · 2024Article
- Profiling the dynamic adaptations of CAZyme-Producing microorganisms in the gastrointestinal tract of South African goats.Heliyon · 2024Article
- Carbohydrate-active enzyme (CAZyme) discovery and engineeringRSC chemical biology · 2024Review
- Characterization of a Novel Polysaccharide Lyase Family 5 Alginate Lyase with PolyM Substrate Specificity.Foods (Basel, Switzerland) · 2022Article
- Taxonomic position, antibiotic resistance and virulence factor production by Stenotrophomonas isolates from patients with cystic fibrosis and other chronic respiratory infections.BMC microbiology · 2022Article
- Performance of halotolerant bacteria associated with Sahara-inhabiting halophytes Atriplex halimus L. and Lygeum spartum L. ameliorate tomato plant growth and tolerance to saline stress: from selective isolation to genomic analysis of potential determinants.World journal of microbiology & biotechnology · 2021Article
- Advances in the Microbiology of Stenotrophomonas maltophilia.Clinical microbiology reviews · 2021Article
- Recent progress on engineering microbial alginate lyases towards their versatile role in biotechnological applications.Folia microbiologica · 2020Review
- Exploiting fine-scale genetic and physiological variation of closely related microbes to reveal unknown enzyme functions.The Journal of biological chemistry · 2017Article
- Review
- Engineering broad-spectrum digestion of polyuronides from an exolytic polysaccharide lyase.Biotechnology for biofuels · 2016Article
- Biochemical, Kinetic, and Spectroscopic Characterization of Ruegeria pomeroyi DddW--A Mononuclear Iron-Dependent DMSP Lyase.PloS one · 2015Article
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2 authors at 1 institution in 1 country.
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Abstract
Polysaccharide lyases (PLs) catalyze the depolymerization of anionic polysaccharides via a β-elimination mechanism. PLs also play important roles in microbial pathogenesis, participating in bacterial invasion and toxin spread into the host tissue via degradation of the host extracellular matrix, or in microbial biofilm formation often associated with enhanced drug resistance. Stenotrophomonas maltophilia is a Gram-negative bacterium that is among the emerging multidrug-resistant organisms associated with chronic lung infections as well as with cystic fibrosis patients. A putative alginate lyase (Smlt1473) from S. maltophilia was heterologously expressed in Escherichia coli, purified in a one-step fashion via affinity chromatography, and activity as well as specificity determined for a range of polysaccharides. Interestingly, Smlt1473 catalyzed the degradation of not only alginate, but poly-β-D-glucuronic acid and hyaluronic acid as well. Furthermore, the pH optimum for enzymatic activity is substrate-dependent, with optimal hyaluronic acid degradation at pH 5, poly-β-D-glucuronic acid degradation at pH 7, and alginate degradation at pH 9. Analysis of the degradation products revealed that each substrate was cleaved endolytically into oligomers comprised predominantly of even numbers of sugar groups, with lower accumulation of trimers and pentamers. Collectively, these results imply that Smlt1473 is a multifunctional PL that exhibits broad substrate specificity, but utilizes pH as a mechanism to achieve selectivity.
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