Exohydrolysis of the alpha-L-Rha-(1->4)-alpha-D-GalA bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing beta-L-rhamnose from the non-reducing end of rhamnogalacturonan oligosaccharides
Synonyms pcrgrh78a, rg-rhamnohydrolase, rg rhamnohydrolase, rg alpha-l-rhamnopyranohydrolase, more
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Exohydrolysis of the alpha-L-Rha-(1->4)-alpha-D-GalA bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing beta-L-rhamnose from the non-reducing end of rhamnogalacturonan oligosaccharides
Exohydrolysis of the alpha-L-Rha-(1->4)-alpha-D-GalA bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing beta-L-rhamnose from the non-reducing end of rhamnogalacturonan oligosaccharides
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Exohydrolysis of the alpha-L-Rha-(1->4)-alpha-D-GalA bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing beta-L-rhamnose from the non-reducing end of rhamnogalacturonan oligosaccharides
Substrates: degalactosylated saponified modified hairy regions of xylogalacturonan, from apple pectin, residue remaining after enzymatic liquefaction of pectin, galactosyl residues removed. The activity increases 78% when tested with MHR-S without galactose substitutions, and in essence the activity of this enzyme is thus hindered by galactose substitutions Products: -
Substrates: i.e. modified hairy regions of xylogalacturonan, from apple pectin, residue remaining after enzymatic liquefaction of pectin, the enzyme is active towards MHR-S as well as unsaponified MHR Products: -
Substrates: i.e. saponified modified hairy regions of xylogalacturonan, from apple pectin, residue remaining after enzymatic liquefaction of pectin, the enzyme is active towards MHR-S as well as unsaponified MHR Products: -
Substrates: 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 Products: -
Substrates: alpha-L-Rha-(1->4)-[alpha-D-GalA-(1->2)-alpha-L-Rha]n-(1->4)-alpha-D-GalA. The enzyme is hindered when the terminal Rha residue is substituted at the 4-position by a beta-D-galactose. No particular preference of the enzyme for low or high molecular mass rhamnogalacturonan fragments Products: -
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rhamnogalacturonan I oligosaccharides with L-rhamnopyranose at the nonreducing end + H2O
beta-L-rhamnopyranose + shortened rhamnogalacturonan I oligosaccharides with beta-D-galacturonic acid at the nonreducing end
Substrates: alpha-L-Rha-(1->4)-[alpha-D-GalA-(1->2)-alpha-L-Rha]n-(1->4)-alpha-D-GalA. The enzyme acts with inversion of configaration releasing beta-L-rhamnose from the non-reducing end of rhamnogalacturonan oligosaccharides Products: -
Substrates: two oligosaccharides, RG4 (Rha-GalA-Rha-GalA: RG4) and the RG hexasaccharide (Rha-GalA-Rha-GalA-Rha-GalA: RG6), prepared from potato rhamnogalacturonan I Products: -
Substrates: two oligosaccharides, RG4 (Rha-GalA-Rha-GalA: RG4) and the RG hexasaccharide (Rha-GalA-Rha-GalA-Rha-GalA: RG6), prepared from potato rhamnogalacturonan I Products: -
Substrates: RGRH exo-enzyme catalyses the cleavage of the alpha-(1->4) glycosidic bonds between L-Rhap and D-GalpA in the non-reducing terminus, releasing single beta-L-Rhap. Enzyme RGRH requires Rhap at the non-reducing end for action Products: -
Substrates: enzyme PcRGRH78A specifically hydrolyzes rhamnogalacturonan oligosaccharides that contain rhamnose at their nonreducing ends, releasing the L-rhamnose, but it has no activity toward naringin, hesperidin,or rutin. When galactosyl rhamnogalacturonan oligosaccharides are used as substrate, PcRGRH78A releases Rha in 3.5fold greater amounts in the presence of beta-galactosidase than in its absence, indicating that PcRGRH78A preferentially acts on Rha residues without the galactose moietyat nonreducing ends Products: -
Substrates: enzyme PcRGRH78A specifically hydrolyzes rhamnogalacturonan oligosaccharides that contain rhamnose at their nonreducing ends, releasing the L-rhamnose, but it has no activity toward naringin, hesperidin,or rutin. When galactosyl rhamnogalacturonan oligosaccharides are used as substrate, PcRGRH78A releases Rha in 3.5fold greater amounts in the presence of beta-galactosidase than in its absence, indicating that PcRGRH78A preferentially acts on Rha residues without the galactose moietyat nonreducing ends Products: -
Substrates: enzyme PcRGRH78A specifically hydrolyzes rhamnogalacturonan oligosaccharides that contain rhamnose at their nonreducing ends, releasing the L-rhamnose, but it has no activity toward naringin, hesperidin,or rutin. When galactosyl rhamnogalacturonan oligosaccharides are used as substrate, PcRGRH78A releases Rha in 3.5fold greater amounts in the presence of beta-galactosidase than in its absence, indicating that PcRGRH78A preferentially acts on Rha residues without the galactose moietyat nonreducing ends Products: -
Substrates: enzyme PcRGRH78A specifically hydrolyzes rhamnogalacturonan oligosaccharides that contain rhamnose at their nonreducing ends, releasing the L-rhamnose, but it has no activity toward naringin, hesperidin,or rutin. When galactosyl rhamnogalacturonan oligosaccharides are used as substrate, PcRGRH78A releases Rha in 3.5fold greater amounts in the presence of beta-galactosidase than in its absence, indicating that PcRGRH78A preferentially acts on Rha residues without the galactose moietyat nonreducing ends Products: -
Substrates: 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 Products: -
the enzyme belongs to the glycoside hydrolase family 78, GH78, group 3. Enzyme PcRGRH78A contains a bacterial alpha-L-rhamnosidase (PF05592) domain, but shows no activity with rhamnogalacturonan oligosaccharides
the enzyme belongs to the glycoside hydrolase family 78, GH78, group 3. Enzyme PcRGRH78A contains a bacterial alpha-L-rhamnosidase (PF05592) domain, but shows no activity with rhamnogalacturonan oligosaccharides
the native extracellular enzyme is N-linked glycosylated, deglycosylation with endoglycosidase H. Fifteen asparagine residues in PcR-GRH78A are identified as possible N-glycosylation sites
the native extracellular enzyme is N-linked glycosylated, deglycosylation with endoglycosidase H. Fifteen asparagine residues in PcR-GRH78A are identified as possible N-glycosylation sites
native extracellular enzyme from Penicillium chrysogenum strain 31B and recombinant enzyme expressed in Aspergillus oryzae strain niaD300 both about 10fold by ultrafiltration, ammonium sulfate fractionation, anion exchange chromatography, and two different steps of hydrophobic interaction chromatography, followed by dialysis and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Pcrgrh78A, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant overexpression in Aspergillus oryzae strain niaD300, subcloning in Escherichia coli strain DH5alpha
Mutter, M.; Beldman, G.; Schols, H.A.; Voragen, A.G.
Rhamnogalacturonan alpha-L-rhamnopyranohydrolase. A novel enzyme specific for the terminal nonreducing rhamnosyl unit in rhamnogalacturonan regions of pectin