Crystal Structure of Family 14 Polysaccharide Lyase with pH-dependent Modes of Action [PDF]
Journal of Biological Chemistry, 2009 The Chlorella virus enzyme vAL-1 (38 kDa), a member of polysaccharide lyase family 14, degrades the Chlorella cell wall by cleaving the glycoside bond of the glucuronate residue (GlcA) through a beta-elimination reaction. The enzyme consists of an N-terminal cell wall-attaching domain (11 kDa) and a C-terminal catalytic module (27 kDa).
Kohei Ogura +5 more
openalex +4 more sources
Proceedings of the National Academy of Sciences of the United States of America, 2002 Simon J. Charnock +4 more
openalex +2 more sources
Polysaccharide lyases from gellan-producing Sphingomonas spp. [PDF]
Microbiology, 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 ...
I. Sutherland, L. Kennedy
semanticscholar +3 more sources
Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacterium Catenovulum sp. CCB-QB4 [PDF]
PeerJ, 2021 Background Oligosaccharides from polysaccharides containing uronic acids are known to have many useful bioactivities. Thus, polysaccharide lyases (PLs) and glycoside hydrolases (GHs) involved in producing the oligosaccharides have attracted interest in ...
Go Furusawa +2 more
doaj +2 more sources
Structural analyses of ‘substrate-pH of activity’ pairing observed in Polysaccharide lyases [PDF]
, 2023 AbstractAnionic polysaccharides found in nature are functionally and structurally diverse, and so are the polysaccharide lyases (PLs) which catalyse their degradation. Atomic superposition of various PL folds according to their cleavable substrate structure confirm the occurrence of structural convergence at PL active sites.
Shubhant Pandey +2 more
openalex +2 more sources
Ulvan Lyases Isolated from the Flavobacteria Persicivirga ulvanivorans Are the First Members of a New Polysaccharide Lyase Family [PDF]
Journal of Biological Chemistry, 2011 Pi Nyvall Collén +4 more
openalex +2 more sources
Substrate recognition and catalysis of polysaccharide lyases [PDF]
Acta Crystallographica Section A Foundations of Crystallography, 2009 Sine Larsen +9 more
openalex +2 more sources
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.
D. Close, S. D’Angelo, A. Bradbury
semanticscholar +4 more sources
From structure to function: Smlt1473, a pH-dependent polysaccharide lyase [PDF]
Acta Crystallographica Section A Foundations and Advances, 2017 Shubhant Pandey +4 more
openalex +2 more sources
A Polysaccharide Lyase from Stenotrophomonas maltophilia with a Unique, pH-regulated Substrate Specificity [PDF]
Journal of Biological Chemistry, 2013 Polysaccharide lyases (PLs) catalyze the depolymerization of anionic polysaccharides via a β-elimination mechanism. PLs also play important roles in microbial pathogenesis, participating in bacterial invasion and toxin spread into the host tissue via degradation of the host extracellular matrix, or in microbial biofilm formation often associated with ...
Logan C. MacDonald, Bryan W. Berger
openalex +3 more sources