Refine search

Search Natural Substrates/ Products (Substrates)

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search
Search for synonyms (with exact matching search term)

Search term:

<< < Results 31 - 39 of 39
EC Number
Natural Substrates
Commentary (Nat. Sub.)
more
alginate lyase A1-III is a beta-D-mannuronosyl linkage-specific enzyme that acts on alginate tetrasaccharide as the minimum substrate and produces disaccharides and trisaccharides from alginate
more
alginate lyase AlgL catalyzes the cleavage of the polysaccharide alginate through a beta-elimination reaction. AlgL operates preferentially on non-acetylated alginate or its precursor mannuronan. AlgL operates as an exopolysaccharide lyase
more
AlgL is a poly-(beta-D-mannuronate) lyase that preferentially degrades deacetylated polymannuronate via a beta-elimination reaction, resulting in an unsaturated uronic acid at the nonreducing end of the molecule
more
KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage
more
the enzyme Alg17c is an exolytic alginate lyase, structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization, overview
more
the enzyme is an endolytic polymannuronate lyase
sodium alginate
-
sodium alginate
AlyA5 cleaves unsaturated units, alpha-L-guluronate or beta-D-manuronate residues, at the nonreducing end of oligo-alginates in an exolytic fashion, cf. EC 4.2.2.11
trisaccharides of alginate
oligoalginate lyase, complete depolymerization of alginate
<< < Results 31 - 39 of 39