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Information on EC 3.2.1.171 - rhamnogalacturonan hydrolase and Organism(s) Aspergillus aculeatus and UniProt Accession Q00001
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3.2.1.171 rhamnogalacturonan hydrolaseIUBMB Comments
The enzyme is part of the degradation system for rhamnogalacturonan I in Aspergillus aculeatus.
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Word Map
- 3.2.1.171
- aspergillus
- aculeatus
-
pectic
-
rgases
-
galacturonic
- galactan
- homogalacturonans
-
right-handed
- endo-polygalacturonase
- polygalacturonase
- irpex
- pectate
- lacteus
The taxonomic range for the selected organisms is: Aspergillus aculeatus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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
SYSTEMATIC NAME
IUBMB Comments
rhamnogalacturonan D-alpha-GalA-(1->2)-alpha-L-Rha hydrolase
The enzyme is part of the degradation system for rhamnogalacturonan I in Aspergillus aculeatus.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
MHR-S + H2O
?
i.e. saponified modified hairy regions of rhamnogalacturonan I, from apple pectin, residue remaining after enzymatic liquefaction of pectin
-
-
?
partially debranched sycamore rhamnogalacturonan I + H2O
rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end
endohydrolytic cleavage of the -alpha-D-GalpAa-(1->2)-alpha-L-Rhap glycosidic linkage in partially debranched sycamore rhamnogalacturonan I
backbone oligosaccharide fragments from partially debranched sycamore rhamnogalacturonan I
-
?
rhamnogalacturonan I + H2O
rhamnogalacturonan I oligosaccharides with beta-D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end
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
-
-
?
rhamnogalacturonan I + H2O
rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end
MHR-S + H2O
?
i.e. saponified modified hairy regions of rhamnogalacturonan I, from apple pectin, residue remaining after enzymatic liquefaction of pectin
-
-
?
rhamnogalacturonan I + H2O
?
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
rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end
RGase A is an enzyme implicated in the enzymatic degradation of rhamnogalacturonan I
-
-
?
rhamnogalacturonan I + H2O
rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end
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
-
-
?
rhamnogalacturonan I + H2O
?
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
rhamnogalacturonan I + H2O
?
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
rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end
RGase A is an enzyme implicated in the enzymatic degradation of rhamnogalacturonan I
-
-
?
rhamnogalacturonan I + H2O
?
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
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
rRGase A has no distinct temperature optimum from 30 to 50°C
additional information
-
rRGase A has no distinct temperature optimum from 30 to 50°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
phylogenetic and structural traits of RGI hydrolases, overview
evolution
phylogenetic and structural traits of RGI hydrolases, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RHGA_ASPAC
440
0
45962
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
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
glycoprotein
the enzyme is highly glycosylated corresponding to 5.9 kDa
glycoprotein
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pitson, S.M.; Mutter, M.; van den Broek, L.A.; Voragen, A.G.; Beldman, G.
Stereochemical course of hydrolysis catalysed by alpha-L-rhamnosyl and alpha-D-galacturonosyl hydrolases from Aspergillus aculeatus
Biochem. Biophys. Res. Commun.
242
552-559
1998
Aspergillus aculeatus (Q00001)
Petersen, T.N.; Christgau, S.; Kofod, L.V.; Kauppinen, S.; Johnson, A.H.; Larsen, S.
Crystallization and preliminary X-ray studies of rhamnogalacturonase A from Aspergillus aculeatus
Acta Crystallogr. Sect. D
53
105-107
1997
Aspergillus aculeatus (Q00001), Aspergillus aculeatus
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
Carbohydr. Res.
311
155-164
1998
Aspergillus aculeatus (Q00001)
Azadi, P.; O'Neill, M.A.; Bergmann, C.; Darvill, A.G.; Albersheim, P.
The backbone of the pectic polysaccharide rhamnogalacturonan I is cleaved by an endohydrolase and an endolyase
Glycobiology
5
783-789
1995
Aspergillus aculeatus (Q00001), Aspergillus aculeatus
Kofod, L.V.
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
J. Biol. Chem.
269
29182-29189
1994
Aspergillus aculeatus (Q00001), Aspergillus aculeatus
Petersen, T.N.; Kauppinen, S.; Larsen, S.
The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel beta helix
Structure
5
533-544
1997
Aspergillus aculeatus (Q00001), Aspergillus aculeatus
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