The enzyme, characterized from the phytopathogenic fungus Fusarium oxysporum, removes the rhamnosyl residue from α-L-rhamnosyl-(1→4)-D-glucuronate or (with lower activity) from oligosaccharides that contain this motif at the non-reducing end, leaving an unsaturated glucuronate residue. Among its natural substrates is the type II arabinogalactan component of gum arabic.
The expected taxonomic range for this enzyme is: Fusarium oxysporum
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SYSTEMATIC NAME
IUBMB Comments
alpha-L-rhamnosyl-(1->4)-D-glucuronate lyase
The enzyme, characterized from the phytopathogenic fungus Fusarium oxysporum, removes the rhamnosyl residue from alpha-L-rhamnosyl-(1->4)-D-glucuronate or (with lower activity) from oligosaccharides that contain this motif at the non-reducing end, leaving an unsaturated glucuronate residue. Among its natural substrates is the type II arabinogalactan component of gum arabic.
Substrates: enzyme shows trace activity with ulvan and larch wood arabinogalactan, no activity with rhamnogalacturonan-I oligosaccharides, which have Rha residues at their nonreducing end, 4-nitrophenyl-alpha-L-Rha, and quercetin 3-O-(6-O-alpha-L-rhamnopyranosyl)-beta-D-glucopyranoside Products: -
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of ligand-free and alpha-L-rhamnose-(1->4)-D-glucuronic acid-bound Rham1. The active site lies on the anterior side of the beta-propeller protein
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