Whole genome sequencing and functional annotation of <i>Fusarium oxysporum</i> f. sp. <i>lentis</i> to unravel virulence and secondary metabolite biosynthesis gene clusters. [PDF]
Kharte S +13 more
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Direct Preparation of Alginate Oligosaccharides from Brown Algae by an Algae-Decomposing Alginate Lyase AlyP18 from the Marine Bacterium Pseudoalteromonas agarivorans A3. [PDF]
Sun XH +7 more
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Profiling the Genomes and Secreted Effector Proteins in <i>Phytopythium vexans</i> Global Strains. [PDF]
Villanueva O, Nguyen HDT, Ellouze W.
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Inhibition of chondroitin sulphate-degrading enzyme Chondroitinase ABC by dextran sulphate. [PDF]
Dalal S, Pathak R, Moh EXS, Packer NH.
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Discovery of two novel Flavobacterium species with potential for complex polysaccharide degradation. [PDF]
Lian XD +5 more
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A Low-Temperature-Active Pectate Lyase from a Marine Bacterium for Orange Juice Clarification. [PDF]
Bai Y +5 more
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Exploring marine glycans: structure, function, and the frontier of chemical synthesis. [PDF]
Mardhekar S, Luong P, Seeberger PH.
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Polysaccharide lyases (or eliminases) are a class of enzymes (EC 4.2.2.-) that act to cleave certain activated glycosidic linkages present in acidic polysaccharides. These enzymes act through an eliminase mechanism, rather than through hydrolysis, resulting in unsaturated oligosaccharide products.
Robert J. Linhardt +2 more
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Action pattern of polysaccharide lyases on glycosaminoglycans
Glycobiology, 1994The action pattern of polysaccharide lyases on glycosaminoglycan substrates was examined using viscosimetric measurements and gradient polyacrylamide gel electrophoresis (PAGE). Heparin lyase I (heparinase, EC 4.2.2.7) and heparin lyase II (no EC number) both acted on heparin in a random endolytic fashion.
Robert J. Linhardt +2 more
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Polysaccharide Lyases: Recent Developments as Biotechnological Tools
Critical Reviews in Biotechnology, 2003Polysaccharide lyases, which are polysaccharide cleavage enzymes, act mainly on anionic polysaccharides. Produced by prokaryote and eukaryote organisms, these enzymes degrade (1,4) glycosidic bond by a beta elimination mechanism and have unsaturated oligosaccharides as major products.
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