Information on EC 3.2.1.174 - rhamnogalacturonan rhamnohydrolase

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The expected taxonomic range for this enzyme is: Aspergillus aculeatus

EC NUMBER
COMMENTARY hide
3.2.1.174
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RECOMMENDED NAME
GeneOntology No.
rhamnogalacturonan rhamnohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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.
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
rhamnogalacturonan type I degradation I (fungi)
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SYSTEMATIC NAME
IUBMB Comments
rhamnogalacturonan oligosaccharide alpha-D-GalA-(1->2)-alpha-L-Rha hydrolase
The enzyme is part of the degradation system for rhamnogalacturonan I in Aspergillus aculeatus.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
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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
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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
show the reaction diagram
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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
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sodium acetate
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0.1 M slowly inactivates the enzyme: at 0.5 M 33% residual activity, at 1.1 M 10% residual activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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McIlvaine buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
sodium acetate buffer
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84000
-
x * 84000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 84000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
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stable
136392
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
stable for 1 h up to temperatures of 60°C in 50 mM sodium acetate buffer (pH 5)
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE