Information on EC 3.2.1.82 - exo-poly-alpha-galacturonosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.2.1.82
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RECOMMENDED NAME
GeneOntology No.
exo-poly-alpha-galacturonosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of pectic acid from the non-reducing end, releasing digalacturonate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pectin degradation II
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-58-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
protein complex with polygalacturonate hydrolase activity
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Manually annotated by BRENDA team
grown on citrus fruit pectin
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
citric pectin + H2O
?
show the reaction diagram
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PGase I is an exocellular enzyme releasing galacturonic acid as its principal hydrolysis product, it hydrolyzes digalacturonate, and it shows a higher affinity towards poly(1,4-alpha-D-galactosiduronate) than citric pectin
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-
?
D-galacturonan + H2O
digalacturonate
show the reaction diagram
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-
-
-
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oligogalacturonate + H2O
digalacturonate
show the reaction diagram
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-
?
pectate + H2O
digalacturonate
show the reaction diagram
pectin + H2O
?
show the reaction diagram
pectin + H2O
digalacturonate
show the reaction diagram
poly(1,4-alpha-D-galactosiduronate) + H2O
?
show the reaction diagram
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i.e. PGA, PGase I is an exocellular enzyme releasing galacturonic acid as its principal hydrolysis product, it hydrolyzes digalacturonate, and it shows a higher affinity towards PGA than citric pectin
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-
?
polygalacturonate + H2O
digalacturonate
show the reaction diagram
polygalacturonic acid + H2O
?
show the reaction diagram
additional information
?
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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
citric pectin + H2O
?
show the reaction diagram
-
PGase I is an exocellular enzyme releasing galacturonic acid as its principal hydrolysis product, it hydrolyzes digalacturonate, and it shows a higher affinity towards poly(1,4-alpha-D-galactosiduronate) than citric pectin
-
-
?
pectin + H2O
digalacturonate
show the reaction diagram
poly(1,4-alpha-D-galactosiduronate) + H2O
?
show the reaction diagram
-
i.e. PGA, PGase I is an exocellular enzyme releasing galacturonic acid as its principal hydrolysis product, it hydrolyzes digalacturonate, and it shows a higher affinity towards PGA than citric pectin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
0.4 mM Ca2+ shifts the optimal temperature from 50C to 55C, the activity is 1.2fold higher than the maximal activity without Ca2+ at 50C
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CaCl2
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at 1 mM causes 21% inhibition of PGI, at 5 mM causes 35% inhibition of PGI
CoCl2
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at 1 mM causes 19% inhibition of PGI, at 5 mM causes 45% inhibition of PGI
CuSO4
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at 1 mM causes 27% inhibition of PGI, at 5 mM causes 48% inhibition of PGI
HgCl2
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at 1 mM causes 17% inhibition of PGI, at 5 mM causes 48% inhibition of PGI
MgCl2
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at 1 mM causes 8% inhibition of PGI, at 5 mM causes 22% inhibition of PGI
MnCl2
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at 1 mM causes 57% inhibition of PGI, at 5 mM causes complete inhibition of PGI
NiCl2
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at 1 mM causes 10% inhibition of PGI, at 5 mM causes 37% inhibition of PGI
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55
citric pectin
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pH 6.8, 37C
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0.05
D-galacturonan
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1002
nonagalacturonate
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0.55
poly(1,4-alpha-D-galactosiduronate)
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pH 6.8, 37C
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1159
trigalacturonate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
53.4 - 160.2
Pectin
85.4
polygalacturonic acid
Aspergillus niger
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PGI
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34.7
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cell-free broth of PGI
186.6
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PGI and PGII
418.6
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12fold purified PGI
500
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purified native enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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D-galacturonan
6.6
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tetragalacturonate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
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D-galacturonan
3 - 8
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activity range, profile, overview
3.5 - 8
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PGI
7 - 10
pH 7.0: about 55% of maximal activity, pH 10.0: about 35% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
Tris-HCl buffer in presence of Ca2+
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
30 - 65
30C: about 30% of maximal activity, 65C: about 30% of maximal activity
40 - 70
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activity decreases rapidly at higher temperatures
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
isoelectrofocusing, pH-gradient 3.5-9.5
7.6
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isoelectic focusing of PGI
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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gel filtration of PGI
42000
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1 * 42000, SDS-PAGE
43000
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gel filtration
58000 - 65000
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sedimentation equilibrium
67000
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SDS-PAGE of purified protein
68000
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activity-stained SDS-PAGE
74200
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predicted by DNA sequencing
79000
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SDS-PAGE of recombinant protein
105000
x * 105000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 105000, SDS-PAGE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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PGase I is an N-glycosidated monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of an in a native form (solved to 2.19 A resolution) and a digalacturonic acid product complex (solved to 2.10 A resolution). The enzyme is crystallized in space group P2(1) by the hanging-drop, vapor-diffusion method at 18C in 20% (w/v) PEG 4000, 0.1 M nickel sulfate, 0.1 M sodium acetate, pH 4.2
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8 - 8
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purified native enzyme, stable
710031
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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PGI is stable up to 30C
50
pH 7.0, 15 min, stable up to
65
pH 7.0, 15 min, about 90% loss of activity
80
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purified native enzyme, loss of 90% activity after 30 min, pH 4.8
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, PGI in liquid form, 2 weeks
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4C, PGI in powder form, 9 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 200fold by ammonium sulfate fractionation, dialysis, and gel filtration
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PGI and PGII purified by gel filtration, PGI 12fold purified to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
the YeGH28 construct is then transformed into BL21 DE3 star cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
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