3.2.1.174: rhamnogalacturonan rhamnohydrolase
This is an abbreviated version!
For detailed information about rhamnogalacturonan rhamnohydrolase, go to the full flat file.
Word Map on EC 3.2.1.174
-
3.2.1.174
-
aspergillus
-
nonreducing
-
aculeatus
-
pectin
-
oligosaccharides
-
p-nitrophenyl
-
hesperidin
-
hairy
-
hydrolases
-
lyases
-
oligomers
-
naringin
- 3.2.1.174
- aspergillus
-
nonreducing
- aculeatus
- pectin
- oligosaccharides
- p-nitrophenyl
- hesperidin
-
hairy
- hydrolases
- lyases
- oligomers
- naringin
Reaction
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
alpha-L-rhamnosidase, PcRGRH78A, RG alpha-L-rhamnopyranohydrolase, RG rhamnohydrolase, RG-rhamnohydrolase, RGI exo-hydrolase, RGI hydrolase, RGI rhamnohydrolase, RGRH
ECTree
Advanced search results
Substrates Products
Substrates Products on EC 3.2.1.174 - rhamnogalacturonan rhamnohydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REACTION DIAGRAM
degalactosylated MHR-S + H2O
beta-L-rhamnose + ?
-
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
-
-
?
MHR + H2O
beta-L-rhamnose + ?
-
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
-
-
?
MHR-S + H2O
beta-L-rhamnose + ?
-
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
-
-
?
rhamnogalacturonan I + H2O
beta-L-rhamnose + ?
-
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
-
-
?
rhamnogalacturonan I + H2O
L-rhamnose + ?
-
Aspergillus aculeatus RGRH is active on the nonreducing end Rhap-linkage in RGI fragments
-
-
?
rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end + H2O
beta-L-rhamnopyranose + shortened rhamnogalacturonan I oligosaccharides with beta-D-galacturonic acid at the reducing end and at the nonreducing end
-
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
-
-
?
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
-
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
-
-
?
L-rhamnose + ?
two oligosaccharides, RG4 (Rha-GalA-Rha-GalA: RG4) and the RG hexasaccharide (Rha-GalA-Rha-GalA-Rha-GalA: RG6), prepared from potato rhamnogalacturonan I
-
-
?
rhamnogalacturonan oligosaccharide + H2O
L-rhamnose + ?
two oligosaccharides, RG4 (Rha-GalA-Rha-GalA: RG4) and the RG hexasaccharide (Rha-GalA-Rha-GalA-Rha-GalA: RG6), prepared from potato rhamnogalacturonan I
-
-
?
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?