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Polysaccharide lyases

Applied Biochemistry and Biotechnology, 1987
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.
R J, Linhardt   +2 more
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Polysaccharide Lyases: Recent Developments as Biotechnological Tools

Critical Reviews in Biotechnology, 2003
Polysaccharide 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.
P, Michaud   +3 more
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Action pattern of polysaccharide lyases on glycosaminoglycans

Glycobiology, 1994
The 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.
K A, Jandik, K, Gu, R J, Linhardt
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The first structure of pectate lyase belonging to polysaccharide lyase family 3

Acta Crystallographica Section D Biological Crystallography, 2001
The crystal structure of a highly alkaline low molecular weight pectate lyase (Pel-15) was determined at 1.5 A resolution by the multiple isomorphous replacement (MIR) method. This is the first pectate lyase structure from polysaccharide lyase family 3.
M, Akita   +4 more
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Study of a novel glycoconjugate, thiopeptidoglycan, and a novel polysaccharide lyase, thiopeptidoglycan lyase

International Journal of Biological Macromolecules, 2011
A typical filamentous bacterium, Sphaerotilus natans, secretes a thiolic glycoconjugate which is assembled into a microtube, so called sheath. The glycoconjugate is known to consist of a pentasaccharide-dipeptide repeating unit, but its chemical structure has not been completely elucidated.
Keiko, Kondo   +8 more
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Posttranslational processing of polysaccharide lyase: maturation route for gellan lyase in Bacillus sp. GL1

Archives of Biochemistry and Biophysics, 2004
Cells of Bacillus sp. GL1 extracellularly secrete a gellan lyase with a molecular mass of 130 kDa responsible for the depolymerization of a heteropolysaccharide (gellan), although the gene is capable of encoding a huge protein with a molecular mass of 263 kDa.
Osamu, Miyake   +5 more
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A New Member of Family 11 Polysaccharide Lyase, Rhamnogalacturonan Lyase (CtRGLf) from Clostridium thermocellum

Molecular Biotechnology, 2016
A thermostable, alkaline rhamnogalacturonan lyase (RG lyase) CtRGLf, of family 11 polysaccharide lyase from Clostridium thermocellum was cloned, expressed, purified and biochemically characterised. Both, the full-length CtRGLf (80 kDa) protein and its truncated derivative CtRGL (63.9 kDa) were expressed as soluble proteins and displayed maximum ...
Arun, Dhillon   +7 more
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Analysis of Glycosaminoglycans with Polysaccharide Lyases

Current Protocols in Molecular Biology, 1999
Polysaccharide 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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Bacteriophage-associated lyase activity against Klebsiella serotype K64 capsular polysaccharide

Carbohydrate Research, 1987
Bacteriophage phi 64 possesses a lyase that depolymerises the capsular polysaccharide of Klebsiella K64 into a hexasaccharide having an unsaturated derivative of glucuronic acid at the non-reducing end (1). The unsaturated hex-4-enuronic acid residue generated was characterised spectroscopically (u.v. and n.m.r.) and by g.l.c.-m.s.
N, Ravenscroft   +2 more
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Characterization of an organic solvent-tolerant polysaccharide lyase from Microbulbifer thermotolerans DAU221

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
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