Unraveling the molecular mechanism of polysaccharide lyases for efficient alginate degradation. [PDF]
Alginate lyases (ALs) are essential for breaking down brown macroalgae alginates, widely used naturally-occurring polysaccharides. Their molecular mechanisms remain challenging due to the lack of catalytically competent Michaelis-Menten complex structures.
Rivas-Fernández JP +12 more
europepmc +9 more sources
A hierarchical classification of polysaccharide lyases for glycogenomics [PDF]
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
exaly +6 more sources
Polysaccharide lyases are the products of various microorganisms, bacteriophage and some eukaryotes. All such enzymes cleave a hexose-1,4-alpha- or beta-uronic acid sequence by beta-elimination. They are in some examples, the only known type of enzymes degrading their polyanionic substrates.
I W Sutherland, Ian W Sutherland
exaly +5 more sources
Gellan lyases-novel polysaccharide lyases [PDF]
A number of bacterial strains capable of degrading the bacterial exopolysaccharide gellan have been isolated by standard enrichment procedures. They include several pink-pigmented Gram-negative rod-shaped bacteria. A red-pigmented Gram-positive bacillus earlier found to degrade the exopolysaccharide xanthan from Xanthomonas campestris also showed ...
I W Sutherland, Ian W Sutherland
exaly +3 more sources
An evolutionarily distinct family of polysaccharide lyases removes rhamnose capping of complex arabinogalactan proteins. [PDF]
The human gut microbiota utilizes complex carbohydrates as major nutrients. The requirement for efficient glycan degrading systems exerts a major selection pressure on this microbial community. Thus, we propose that this microbial ecosystem represents a substantial resource for discovering novel carbohydrate active enzymes.
Munoz-Munoz J +5 more
europepmc +6 more sources
Polysaccharide lyases from gellan-producing Sphingomonas spp. [PDF]
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
exaly +3 more sources
A new family of β-helix proteins with similarities to the polysaccharide lyases
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
exaly +4 more sources
Untangling the Reaction Mechanism of the Polysaccharide Lyase PL42 Using QM/MM Metadynamics Simulations. [PDF]
QM/MM metadynamics elucidates the β-elimination mechanism of the PL42 L-rhamnose-α-1,4-D-glucuronate lyase FoRham1. The GlcA +1 sugar follows a 1 C4 → 1 C4 → 1 H2 itinerary and reacts via a concerted, highly asynchronous syn β-elimination with a carbanion-like transition state. H85 acts as the catalytic base within a triad with D83 and H105.
Alonso-Gil S +3 more
europepmc +2 more sources
Structural and functional insights into Uly1040, an ulvan lyase from polysaccharide lyase family 40. [PDF]
ABSTRACT Ulvan is a major polysaccharide in marine green algae. Its oligosaccharide degradation products possess diverse bioactivities and hold considerable potential for various applications. Ulvan lyases, the key enzymes responsible for cleaving ulvan glycosidic bonds,
Wang H-Q +9 more
europepmc +3 more sources
Conformational aspects of the reaction mechanisms of polysaccharide lyases and epimerases [PDF]
D S Feingold, R Bentley
exaly +3 more sources

