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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
openaire   +2 more sources

An engineered polysaccharide lyase to combat harmful algal blooms

Biochemical Engineering Journal, 2018
Abstract A growing global population and industrialization have come at the cost of induced climate change and pollution of natural resources, resulting in formation of toxic algal blooms in fresh water sources. In the US alone, these blooms cost an estimated $1.5 billion dollars each year to remediate.
Evan Eckersley, Bryan W. Berger
openaire   +1 more source

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
openaire   +2 more sources

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
openaire   +2 more sources

A Structural Basis for Depolymerization of Alginate by Polysaccharide Lyase Family-7

Journal of Molecular Biology, 2005
Alginate lyases depolymerize alginate, a heteropolysaccharide consisting of alpha-L-guluronate and beta-D-mannuronate, through a beta-elimination reaction. Their structure/function relationships are expected to provide information valuable to future industrial alginate processing and drug design for Pseudomonas aeruginosa alginate biofilm-dependent ...
Masayuki, Yamasaki   +4 more
openaire   +2 more sources

Polyuronic acid degradation by polysaccharide lyase family 7

Acta Crystallographica Section A Foundations and Advances, 2022
M. Vuillemin   +12 more
openaire   +1 more source

Polysaccharide Lyases

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

ATP-citrate lyase (ACLY) in lipid metabolism and atherosclerosis: An updated review

Progress in Lipid Research, 2020
Xiaojun Feng, Suo-wen Xu, Ai-Zong Shen
exaly  

An R2R3 MYB transcription factor confers brown planthopper resistance by regulating the phenylalanine ammonia-lyase pathway in rice

Proceedings of the National Academy of Sciences of the United States of America, 2020
Yuqiang Liu, Ling Jiang, Jianmin Wan
exaly  

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