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A hierarchical classification of polysaccharide lyases for glycogenomics [PDF]
Biochemical Journal, 2010 Carbohydrate-active enzymes face huge substrate diversity in a highly selective manner using only a limited number of available folds. They are therefore subjected to multiple divergent and convergent evolutionary events. This and their frequent modularity render their functional annotation in genomes difficult in a number of cases.
Corinne Rancurel +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.
Philippe Michaud, J Courtois
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Conformational aspects of the reaction mechanisms of polysaccharide lyases and epimerases [PDF]
FEBS Letters, 1987 D S Feingold, R Bentley
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Polysaccharide lyases from gellan-producing Sphingomonas spp. [PDF]
Microbiology (United Kingdom), 1996 A number ofSphingomonasstrains capable of synthesizing the bacterial exopolysaccharide gellan and related polymers were shown to possess constitutive gellanase activity. In each case, the degradation of deacylated gellan was due to extracellular, eliminase-type enzymes (lyases) which cleave the sequence …ß-D-glucosyl 1,4-ß-D-glucuronosyl… in the ...
Ian W Sutherland
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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 Linhardt, Linhardt Robert J
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A new family of β-helix proteins with similarities to the polysaccharide lyases
Acta Crystallographica Section D: Biological Crystallography, 2014 Microorganisms that degrade biomass produce diverse assortments of carbohydrate-active enzymes and binding modules. Despite tremendous advances in the genomic sequencing of these organisms, many genes do not have an ascribed function owing to low sequence identity to genes that have been annotated.
Andrew Bradbury +2 more
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Analysis of Glycosaminoglycans with Polysaccharide Lyases
Current Protocols in Molecular Biology, 1999Polysaccharide lyases are a class of enzymes useful for analysis of glycosaminoglycans (GAGs) and the glycosaminoglycan component of proteoglycans (PGs). These enzymes cleave specific glycosidic linkages present in acidic polysaccharides and result in depolymerization.
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International Journal of Biological Macromolecules, 2021
Alginate and its derivatives are annually produced approximately 30,000 tons or more and are applied to various industries as they are natural polymers. The global market for alginate and its derivatives has been growing steadily. There is little research compared to other enzymes produced through biomass degradation or modification. An alginate lyase,
Hae-Rin, Jeong +4 more
openaire +2 more sources
Alginate and its derivatives are annually produced approximately 30,000 tons or more and are applied to various industries as they are natural polymers. The global market for alginate and its derivatives has been growing steadily. There is little research compared to other enzymes produced through biomass degradation or modification. An alginate lyase,
Hae-Rin, Jeong +4 more
openaire +2 more sources
Carbohydrate Research, 2004
A thio-linked disaccharide based on the structure of the glycosaminoglycan chondroitin was synthesized as a potential inhibitor of chondroitin AC lyase from Flavobacterium heparinum for structural analysis of the active site. Instead it was found to be a slow substrate, thereby demonstrating that lyases, in contrast to glycosidases, can cleave ...
Stephen Withers
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A thio-linked disaccharide based on the structure of the glycosaminoglycan chondroitin was synthesized as a potential inhibitor of chondroitin AC lyase from Flavobacterium heparinum for structural analysis of the active site. Instead it was found to be a slow substrate, thereby demonstrating that lyases, in contrast to glycosidases, can cleave ...
Stephen Withers
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