Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with beta-D-GalA at the reducing end
Synonyms
rhamnogalacturonan hydrolase, rhamnogalacturonase a, rgase a, rg-hydrolase, endo-rhamnogalacturonase, rg hydrolase, more
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with beta-D-GalA at the reducing end
Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with beta-D-GalA at the reducing end
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Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with beta-D-GalA at the reducing end
mode of action and site of action, overview. RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products
Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with beta-D-GalA at the reducing end
mode of action and site of action, overview. RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products
dearabinosylated and partially degalactosylated saponified modified hairy regions of apple pectin. Rhamnogalacturonan hydrolase also acts with inversion of anomeric configuration during hydrolysis of alpha-D-GalpA-(1->2)-alpha-L-Rhap linkages in rhamnogalacturonan, initially releasing oligosaccharides with beta-D-GalpA at the reducing end
RGI, degrading enzymes are active on the RGI backbone of pectin and are thus strictly specific for cleaving bonds in the repetitive [(1->2)-alpha-L-Rhap-(1->4)-alpha-D-GalpA-(1->2)] structure
RGI, degrading enzymes are active on the RGI backbone of pectin and are thus strictly specific for cleaving bonds in the repetitive [(1->2)-alpha-L-Rhap-(1->4)-alpha-D-GalpA-(1->2)] structure
the enzyme is able to cleave rhamnogalacturonan oligomers which contain 5 rhamnose units or more (i.e. degree of polymerization 9) with a rhamnose unit at both nonreducing and reducing end. Its preferential cleavage site is at four units from the first nonreducing rhamnose. In hairy regions of pectin the rhamnogalacturonan stretches have to be at least 13 residues long for rhamnogalacturonan hydrolase to produce one tetramer
RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products
RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products
RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products
RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products. Aspergillus aculeatus RhgA catalyses the hydrolytic cleavage of the alpha-D-GalpA-(1->2)-alpha-L-Rhap glycosidic linkages thus releasing (oligomeric) products with Rhap at the non-reducing end
RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products. Aspergillus aculeatus RhgA catalyses the hydrolytic cleavage of the alpha-D-GalpA-(1->2)-alpha-L-Rhap glycosidic linkages thus releasing (oligomeric) products with Rhap at the non-reducing end
RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products. Aspergillus aculeatus RhgA catalyses the hydrolytic cleavage of the alpha-D-GalpA-(1->2)-alpha-L-Rhap glycosidic linkages thus releasing (oligomeric) products with Rhap at the non-reducing end
RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products
RGI, degrading enzymes are active on the RGI backbone of pectin and are thus strictly specific for cleaving bonds in the repetitive [(1->2)-alpha-L-Rhap-(1->4)-alpha-D-GalpA-(1->2)] structure
RGI, degrading enzymes are active on the RGI backbone of pectin and are thus strictly specific for cleaving bonds in the repetitive [(1->2)-alpha-L-Rhap-(1->4)-alpha-D-GalpA-(1->2)] structure
Heterobasidion irregulare is a conifer pathogen. Gene HIRHG is highly upregulated during necrotrophic infection of Norway spruce compared with growth in liquid culture, the HIRHG encoded protein is produced during fungal growth on complex carbon sources
Heterobasidion irregulare is a conifer pathogen. Gene HIRHG is highly upregulated during necrotrophic infection of Norway spruce compared with growth in liquid culture, the HIRHG encoded protein is produced during fungal growth on complex carbon sources
the enzyme belongs to the glycosyl hydrolase family 28, GH28. Phylogenetic analysis of endo-rhamnogalacturonases reveals that rhamnogalacturonase genes have been lost in most of the biotrophic and hemibiotrophic plant pathogens investigated but are common in necrotrophic pathogens and saprophytic fungi. Diversity and distribution of fungal endo-rhamnogalacturonase in fungi with different lifestyle, overview
the enzyme belongs to the glycosyl hydrolase family 28, GH28. Phylogenetic analysis of endo-rhamnogalacturonases reveals that rhamnogalacturonase genes have been lost in most of the biotrophic and hemibiotrophic plant pathogens investigated but are common in necrotrophic pathogens and saprophytic fungi. Diversity and distribution of fungal endo-rhamnogalacturonase in fungi with different lifestyle, overview
a significant amount of glycan structures is attached to the enzyme. Three potential sites for N-linked glycosylation are present in the primary structure of RGase A (amino acid positions 50, 235, and 317). Recombinant RGase A is overglycosylated by approximately 3 kDa compared with native RGase A
the enzyme is highly glycosylated: two N-linked and eighteen O-linked glycosylation sites in the structure. The glycan groups bound to RGase A are important to the stability of the crystal
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion technique, crystals diffract beyond 2.0 A resolution and belong to one of the orthorhombic space groups 12(1)2(1)2 or I222, with the unit-cell parameters a = 62.9, b = 125.4 and c = 137.0 A
structure solved by the single isomorphous replacement method including anomalous scattering to 2.0 A resolution. The enzyme folds into a large right-handed parallel beta helix, with a core composed of 13 turns of b strands. Four parallel beta sheets (PB1, PB1a, PB2 and PB3), formed by the consecutive turns, are typically separated by a residue in the conformation of a left-handed a helix
heterologous expression of the HIRHG gene in the hemibiotrophic fungus Magnaporthe oryzae increases its capacity to grow on pectin, but the transformed Magnaporthe oryzae isolates show significant less infection of rice leaves (from Oryza sativa cv. Nakdongbyeo) compared to the wild-type
heterologous expression of the HIRHG gene in the hemibiotrophic fungus Magnaporthe oryzae increases its capacity to grow on pectin, but the transformed Magnaporthe oryzae isolates show significant less infection of rice leaves (from Oryza sativa cv. Nakdongbyeo) compared to the wild-type
Mutter, M.; Renard, C.M.; Beldman, G.; Schols, H.A.; Voragen, A.G.
Mode of action of RG-hydrolase and RG-lyase toward rhamnogalacturonan oligomers. Characterization of degradation products using RG-rhamnohydrolase and RG-galacturonohydrolase
Kauppinen, S.; Christgau, S.; Andersen, L.N.; Heldt-Hansen, H.P.; Drreich, K.; Dalboge, H.: Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus