Information on EC 3.2.1.171 - rhamnogalacturonan hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.1.171
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RECOMMENDED NAME
GeneOntology No.
rhamnogalacturonan hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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.
show the reaction diagram
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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 D-alpha-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
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Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetylated rhamnogalacturonan + H2O
?
show the reaction diagram
azurine dyed and cross-linked galactan + H2O
?
show the reaction diagram
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-
-
-
?
non-acetylated rhamnogalacturonan + H2O
?
show the reaction diagram
partially debranched sycamore rhamnogalacturonan I + H2O
rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end
show the reaction diagram
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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
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?
rhamnogalacturonan I + H2O
rhamnogalacturonan I oligosaccharides with beta-D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end
show the reaction diagram
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
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-
?
rhamnogalacturonan I + H2O
rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
rhamnogalacturonan I + H2O
rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end
show the reaction diagram
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RGase A is an enzyme implicated in the enzymatic degradation of rhamnogalacturonan I
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28.8
purified recombinant enzyme, substrate acetylated rhamnogalacturonan, pH 5.0, 40°C
75
purified recombinant enzyme, substrate non-acetylated rhamnogalacturonan, pH 5.0, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 5
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7
activity range, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 50
recombinant enzyme
additional information
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rRGase A has no distinct temperature optimum from 30 to 50°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
activity range, overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
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calculated from sequence
4.5
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isoelectric focusing
6.2
sequence calculation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44162
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x * 44162, calculated from sequence
44600
x * 44600, about, sequence calculation, x * 56000, recombinant enzyme, SDS-PAGE
50100
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x * 50100, MALDI-TOF analysis
56000
x * 44600, about, sequence calculation, x * 56000, recombinant enzyme, SDS-PAGE
59000
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x * 59000, native enzyme
62000
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x * 62000, recombinant enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 6
purified recombinant enzyme, 90 min 50% to 60% of the activity remaining
731194
6
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unstable above
708968
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
purified recombinant enzyme, stable up to
60
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2 h, enzyme retains 70% of its activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in Pichia pastoris X-33
expression in Aspergillus oryzae
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