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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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Structural Analyses of Substrate–pH Activity Pairing Observed across Diverse Polysaccharide Lyases

Biochemistry, 2023
Anionic polysaccharides found in nature are functionally and structurally diverse, and so are the polysaccharide lyases (PLs) that catalyze their degradation. Atomic superposition of various PL folds according to their cleavable substrate structure confirms the occurrence of structural convergence at PL active sites. This suggests that various PL folds
Shubhant Pandey   +2 more
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Probing the pH Effects on Sugar Binding to a Polysaccharide Lyase

The Journal of Physical Chemistry B, 2019
Polysaccharide lyases (PLs) are an important class of proteins that are excreted from bacteria to degrade sugars in the extracellular matrix of the host. The PL from S. maltophilia (Smlt1473) was found to have pH-specific degradation of three varying polysaccharides: alginate, celluronic acid, and hyaluronic acid (J. Biol. Chem. 2014, 289, 18022-18032).
Sook Wong   +3 more
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Polysaccharide Lyase: Molecular Cloning of Gellan Lyase Gene and Formation of the Lyase from a Huge Precursor Protein inBacillussp. GL1

Archives of Biochemistry and Biophysics, 1998
A bacterium, Bacillus sp. GL1, produced constitutively the extracellular polysaccharide-degrading enzyme (gellan lyase) with a molecular mass of 140 kDa. A genomic DNA library of the bacterium was constructed in Escherichia coli using the cosmid vector, Charomid 9-36.
W, Hashimoto   +3 more
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Polyuronic acid degradation by polysaccharide lyase family 7

Acta Crystallographica Section A Foundations and Advances, 2022
M. Vuillemin   +12 more
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Polysaccharide Lyases

2017
S. Chakraborty   +3 more
openaire   +1 more source

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