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Enzyme Nomenclature
Information on EC 3.2.1.67 - galacturan 1,4-alpha-galacturonidase
for references in articles please use BRENDA:EC3.2.1.67
Word Map on EC 3.2.1.67
- 3.2.1.67
- pectin
-
polygalacturonic
- polygalacturonases
- endo-polygalacturonase
-
pectinolytic
- pectinases
- pectate
-
digalacturonic
- oligogalacturonates
- endopgs
- synthesis
-
methylesterase
- food industry
- exo-pgs
- tubingensis
- nutrition
- analysis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
3.2.1.67
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RECOMMENDED NAME
GeneOntology No.
galacturan 1,4-alpha-galacturonidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[(1->4)-alpha-D-galacturonide]n + H2O = [(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
poly[(1->4)-alpha-D-galacturonide] galacturonohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9045-35-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
1.7fold increase in production of an alkaline exo-polygalacturonase under solid-state fermentation is obtained by optimizing medium components by response surface methodology
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-
isolated from acidic wastewater sample (pH 3.0) collected from a tin mine in Yunnan province, China
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isolated from decaying vegetables in Sao Jose do Rio Preto, SP, Brazil
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effects of substrate conditioning such as initial moisture content, particle size and the addition of extra carbon sources in the production of exopolygalacturonase by Aspergillus awamori in solid state fermentation
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1.7fold increase in production of an alkaline exo-polygalacturonase under solid-state fermentation is obtained by optimizing medium components by response surface methodology
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isolated from decaying hemicellulosic material collected in the state of Sao Paulo, Brazil
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genes MpPG1, MpPG2 and MpPG3. Isozymes MpPG1 and MpPG3 correspond to exo-polygalacturonases, while isozyme MpPG2 corresponds to endo-polygalacturonase, EC 3.2.1.15
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genes MpPG1, MpPG2 and MpPG3. Isozymes MpPG1 and MpPG3 corresponds to exo-polygalacturonases, while isozyme MpPG2 corresponds to endo-polygalacturonase, EC 3.2.1.15
UniProt
isolated from acidic wastewater sample (pH 3.0) collected from a tin mine in Yunnan province, China
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isolated from decaying vegetables in Sao Jose do Rio Preto, SP, Brazil
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
isozyme protein-protein interaction network analysis, overview; isozyme protein-protein interaction network analysis, overview
physiological function
additional information
evolution
the isozyme sequences all contain a conserved domain of glycosyl hydrolase family 28/polygalacturonases; the isozyme sequences all contain a conserved domain of glycosyl hydrolase family 28/polygalacturonases
evolution
the enzyme belongs to the glycosyl hydrolase 28 family, GH28
evolution
the enzyme belongs to the glycosyl hydrolase 28 family, GH28
evolution
Klebsiella sp. Y1 CGMCC 4433
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the enzyme belongs to the glycosyl hydrolase 28 family, GH28
-
physiological function
-
polygalacturonases are pectinolytic enzymes that catalyze the hydrolysis of the plant cell-wall pectin backbone
physiological function
D1MI97, D2KKQ2
recombinant PGC2 protein can induce tissue maceration and necrosis in banana plants; recombinant PGC2 protein can induce tissue maceration and necrosis in banana plants
physiological function
the isozymes show different expression patterns suggesting different individual regulation, all are mainly regulated by fermentable carbon sources galactose and mannose; the isozymes show different expression patterns suggesting different individual regulation, all are mainly regulated by fermentable carbon sources galactose and mannose
physiological function
-
the polygalacturonase catalyzes the hydrolysis of the homo-galacturonan skeleton
physiological function
-
the enzyme plays a role in retting of Crotalaria juncea fibre
physiological function
-
polygalacturonases are pectinolytic enzymes that catalyze the hydrolysis of the plant cell-wall pectin backbone
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physiological function
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the polygalacturonase catalyzes the hydrolysis of the homo-galacturonan skeleton
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physiological function
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the enzyme plays a role in retting of Crotalaria juncea fibre
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additional information
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the multimodular enzyme consists of an N-terminal catalytic domain of pectin methylesterase, a Thr/Ser-rich linker region, and a C-terminal catalytic domain of polygalacturonase
additional information
active site cleft residue is D222, and as general acid catalyst residues D201/D223; active site cleft residue is D223, as general acid catalyst residues D202/D224, and as general base catalysts and residue H246, which is involved in the regeneration of the acid-base equilibrium of the catalytic aspartate
additional information
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active site cleft residue is D222, and as general acid catalyst residues D201/D223; active site cleft residue is D223, as general acid catalyst residues D202/D224, and as general base catalysts and residue H246, which is involved in the regeneration of the acid-base equilibrium of the catalytic aspartate
additional information
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the multimodular enzyme consists of an N-terminal catalytic domain of pectin methylesterase, a Thr/Ser-rich linker region, and a C-terminal catalytic domain of polygalacturonase
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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
(1,4-alpha-D-galacturonide)5 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)2 + (1,4-alpha-D-galacturonide)3 + (1,4-alpha-D-galacturonide)4
(1,4-alpha-D-galacturonide)n + H2O
beta-D-galacturonic acid
-
inversion of configuration during hydrolysis of alpha-1,4-linkage
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
4,5-dehydrogalacturonosyl-alpha-D-trigalacturonic acid + H2O
(1,4-alpha-D-galacturonide)3
-
4,5-unsaturated tetragalacturonic acid
-
?
arabinogalactan + H2O
?
-
exopolygalacturonase still contains arabanase activity, limits the usefulness on any pectic polysaccharide with arabinose residues
-
-
-
GalAalpha(1->4)GalAalpha(1->4)GalA + H2O
GalAalpha(1->4)GalA + D-galacturonic acid
-
-
-
-
?
tetragalacturonic acid + H2O
galacturonic acid + trigalacturonic acid
-
modelling of substrate binidng, structure, overview
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-
?
xylogalacturonan + H2O
xylogalacturonate
-
terminal galacturonic acid residue carries a single xylose substitution
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?
[(1->4)-alpha-D-galacturonide]3 + H2O
[(1->4)-alpha-D-galacturonide]2 + D-galacturonate
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
(1,4-alpha-D-galacturonide)2 + H2O
D-galacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)2 + H2O
D-galacturonic acid
-
specific substrate for exo-D-galactoronanase
-
-
?
(1,4-alpha-D-galacturonide)2 + H2O
D-galacturonic acid
-
specific substrate for exo-D-galactoronanase
-
-
?
(1,4-alpha-D-galacturonide)2 + H2O
D-galacturonic acid
-
-
-
-
?
(1,4-alpha-D-galacturonide)2 + H2O
D-galacturonic acid
-
specific substrate for exo-D-galactoronanase
-
-
?
(1,4-alpha-D-galacturonide)2 + H2O
D-galacturonic acid
-
specific substrate for exo-D-galactoronanase
-
-
?
(1,4-alpha-D-galacturonide)2 + H2O
D-galacturonic acid
-
slowly, reaction rate increases with increasing galacturonan chain length
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-
?
(1,4-alpha-D-galacturonide)3 + H2O
galacturonic acid
-
rate of activity maximal with this substrate
primary product
?
(1,4-alpha-D-galacturonide)4 + H2O
(1,4-alpha-D-galacturonide)3 + D-galacturonic acid
-
substrate of preference
-
-
?
(1,4-alpha-D-galacturonide)4 + H2O
(1,4-alpha-D-galacturonide)3 + D-galacturonic acid
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primary product galacturonic acid
?
(1,4-alpha-D-galacturonide)4 + H2O
(1,4-alpha-D-galacturonide)3 + D-galacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)4 + H2O
(1,4-alpha-D-galacturonide)3 + D-galacturonic acid
-
-
-
-
?
(1,4-alpha-D-galacturonide)4 + H2O
(1,4-alpha-D-galacturonide)3 + D-galacturonic acid
-
-
-
-
?
(1,4-alpha-D-galacturonide)5 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)2 + (1,4-alpha-D-galacturonide)3 + (1,4-alpha-D-galacturonide)4
-
-
-
-
?
(1,4-alpha-D-galacturonide)5 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)2 + (1,4-alpha-D-galacturonide)3 + (1,4-alpha-D-galacturonide)4
-
-
-
-
?
(1,4-alpha-D-galacturonide)5 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)2 + (1,4-alpha-D-galacturonide)3 + (1,4-alpha-D-galacturonide)4
-
-
-
-
?
(1,4-alpha-D-galacturonide)5 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)2 + (1,4-alpha-D-galacturonide)3 + (1,4-alpha-D-galacturonide)4
-
-
-
?
(1,4-alpha-D-galacturonide)6 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)5
-
-
-
-
?
(1,4-alpha-D-galacturonide)6 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)5
-
-
-
-
?
(1,4-alpha-D-galacturonide)6 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)5
-
-
-
-
?
(1,4-alpha-D-galacturonide)6 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)5
-
-
-
-
?
(1,4-alpha-D-galacturonide)6 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)5
-
-
-
-
?
(1,4-alpha-D-galacturonide)6 + H2O
D-galacturonic acid + (1,4-alpha-D-galacturonide)5
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products increase with time, gradually tetragalacturonic acid and trigalacturonic acid appears, exoenzyme removes monomeric units from the substrate
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
Geotrichum lactis
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-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
51% degraded
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
partial hydrolysis
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
polygalacturonic acid I, II, III
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
Yersinia enterolytica
-
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonate + digalacturonic acid + trigalacturonic acid
-
large galacturonans, release of monomeric units from the non-reducing ends of the substrate chains
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonic acid
Bacillus sp. (in: Bacteria) KSM-P443
-
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonic acid
-
carbon source, induce the production of pectolytic enzymes
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonic acid
-
carbon source, induce the production of pectolytic enzymes
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonic acid
-
-
-
?
(1,4-alpha-D-galacturonide)n + H2O
D-galacturonic acid
-
carbon source, induce the production of pectolytic enzymes
-
-
?
apple pectin + H2O
galacturonic acid + ?
-
methylation degree of 75%
-
-
?
apple pectin + H2O
galacturonic acid + ?
-
methylation degree of 75%
-
-
?
apple pectin + H2O
galacturonic acid + ?
-
the activity on citrus pectin is appreciably higher than that on apple pectin
-
-
?
apple pectin + H2O
galacturonic acid + ?
-
the activity on citrus pectin is appreciably higher than that on apple pectin
-
-
?
citric pectin + H2O
D-galacturonic acid + ?
-
higher activity of the enzyme on pectin with 26% of esterification compared to 82% esterification
-
-
?
citric pectin + H2O
D-galacturonic acid + ?
-
higher activity of the enzyme on pectin with 26% of esterification compared to 82% esterification
-
-
?
citric pectin + H2O
galacturonic acid + ?
-
methylation degrees of 34-90%
-
-
?
citric pectin + H2O
galacturonic acid + ?
-
methylation degrees of 34-90%
-
-
?
citric pectin + H2O
galacturonic acid + ?
-
the enzyme is highly specific for pectin substrates, citric pectins with a degree of esterification of 31%, 63%, and 93% result in 42.7%, 8.3%, and 0.0% relative activity rates, respectively, overview. It hydrolyzes specifically the terminal glycosidic bond of the polymer and releases galacturonic acid the only degradation product
-
-
?
citric pectin + H2O
galacturonic acid + ?
-
the enzyme releases galacturonic acid by hydrolysis of pectin with a high degree of esterification, the substrate shows 92% esterification
-
-
?
citric pectin + H2O
galacturonic acid + ?
-
the enzyme releases galacturonic acid by hydrolysis of pectin with a high degree of esterification, the substrate shows 92% esterification
-
-
?
oligo-D-galacturonate + H2O
D-galacturonic acid
-
highly specific for saturated oligogalacturonides, inactive towards unsaturated
-
?
p-nitrophenyl-alpha-D-galactopyranuronide + H2O
D-galacturonic acid + 4-nitrophenol
-
cleaves all substrates with 4-deoxy-L-threo-hexo-4-eno-pyranosyluronate unit at the nonreducing end
-
-
?
p-nitrophenyl-alpha-D-galactopyranuronide + H2O
D-galacturonic acid + 4-nitrophenol
-
cleaves all substrates with 4-deoxy-L-threo-hexo-4-eno-pyranosyluronate unit at the nonreducing end
-
?
p-nitrophenyl-alpha-D-galactopyranuronide + H2O
D-galacturonic acid + 4-nitrophenol
-
cleaves all substrates with 4-deoxy-L-threo-hexo-4-eno-pyranosyluronate unit at the nonreducing end
-
-
?
pectic acid + H2O
D-galacturonic acid + ?
-
-
traces of oligogalacturonic acids found
?
pectic acid + H2O
D-galacturonic acid + ?
-
2 exoforms of enzyme, PGI and PGII, prefer NaPPas substrate over pectin
-
-
?
pectic acid + H2O
D-galacturonic acid + ?
-
lytic cleavage of NaPP, degradation in vitro
-
-
?
pectic acid + H2O
D-galacturonic acid + ?
-
with ASPA, acid soluble pectid acid only galacturonic acid as product
-
-
?
pectic acid + H2O
D-galacturonic acid + ?
-
lytic cleavage of NaPP, degradation in vitro
-
-
?
pectic acid + H2O
D-galacturonic acid + ?
-
lytic cleavage of NaPP, degradation in vitro
-
-
?
pectic acid + H2O
D-galacturonic acid + ?
-
lytic cleavage of NaPP, degradation in vitro
-
-
?
pectic acid + H2O
D-galacturonic acid + ?
-
lytic cleavage of NaPP, degradation in vitro
-
-
?
pectic acid + H2O
D-galacturonic acid + ?
-
-
oligo-D-galacosiduronic acids in the first h
?
pectic acid + H2O
D-galacturonic acid + ?
-
-
oligo-D-galacosiduronic acids in the first h
?
pectin + H2O
digalacturonate + D-galacturonic acid
-
apple pectin
-
-
-
pectin + H2O
digalacturonate + D-galacturonic acid
-
-
unsaturated, digalacturonate main end product
?
pectin + H2O
digalacturonate + D-galacturonic acid
-
-
unsaturated, digalacturonate main end product
?
pectin + H2O
digalacturonate + D-galacturonic acid
-
5% activity on substrate
-
-
-
pectin + H2O
digalacturonate + D-galacturonic acid
-
5% activity on substrate
-
-
?
pectin + H2O
digalacturonate + D-galacturonic acid
-
PGII solubilizes pectin very effective
-
-
-
pectin + H2O
galacturonic acid + ?
-
the enzyme is highly specific for pectin substrates, overview. It hydrolyzes specifically the terminal glycosidic bond of the polymer and releases galacturonic acid the only degradation product
-
-
?
pectin + H2O
galacturonic acid + ?
-
the enzyme releases galacturonic acid by hydrolysis of pectin with a high degree of esterification
-
-
?
pectin + H2O
galacturonic acid + ?
-
the enzyme releases galacturonic acid by hydrolysis of pectin with a high degree of esterification
-
-
?
polygalacturonic acid + H2O
galacturonic acid + ?
-
preferred substrate
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
polypectate
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
polypectate
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
the enzyme releases monogalacturonic acid from its nonreducing end
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
the enzyme releases monogalacturonic acid from its nonreducing end, galacturonic acid is the only product of degradation
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
the enzyme releases monogalacturonic acid from its nonreducing end
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
the enzyme releases monogalacturonic acid from its nonreducing end, galacturonic acid is the only product of degradation
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
polygalacturonnic acid
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
Klebsiella sp. Y1 CGMCC 4433
polygalacturonnic acid
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
citrus polygalacturonic acid
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
the two Rhizopus oryzae exo-polygalacturonase isozymes act on galacturonic acid oligomers, isothermal titration calorimetry analysis, overview
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
citrus polygalacturonic acid
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
additional information
?
-
-
purified enzyme shows its highest hydrolytic activity with low-esterified and non-esterified substrates, releasing monogalacturonic acid from substrate
-
-
-
additional information
?
-
-
purified enzyme shows its highest hydrolytic activity with low-esterified and non-esterified substrates, releasing monogalacturonic acid from substrate
-
-
-
additional information
?
-
-
the enzyme catalyzes the hydrolytic cleavage of the polygalacturonic acid chain
-
-
-
additional information
?
-
-
the enzyme is specifically active towards the alpha-1,4-galacturonic acid linkages of galactopolysaccharides, no activity on Avicel, carboxymethyl cellulose, xylan, glucan, and soluble starch. A higher degree of pectin methylation corresponds to a lower activity of the enzyme
-
-
-
additional information
?
-
-
the enzyme is specifically active towards the alpha-1,4-galacturonic acid linkages of galactopolysaccharides, no activity on Avicel, carboxymethyl cellulose, xylan, glucan, and soluble starch. A higher degree of pectin methylation corresponds to a lower activity of the enzyme
-
-
-
additional information
?
-
-
enzyme is involved in degradation of pectic molecules during root development
-
-
-
additional information
?
-
Fomitopsis cytisina
-
no substrate: 4,5-dehydrogalacturonosyl-alpha-D-trigalacturonic acid
-
-
-
additional information
?
-
the enzyme is a strict exo-type polygalacturonase and reduces the viscosity of polygalacturonic acid (1.0%, w/v) by 15.6%
-
-
-
additional information
?
-
Klebsiella sp. Y1 CGMCC 4433
the enzyme is a strict exo-type polygalacturonase and reduces the viscosity of polygalacturonic acid (1.0%, w/v) by 15.6%
-
-
-
additional information
?
-
-
does not hydrolyze digalacturonic acid
-
-
-
additional information
?
-
-
the enzyme is a bifunctional protein that has both pectin methylesterase, EC 3.1.1.11, and polygalacturonase activities, EC 3.2.1.15 and EC 3.2.1.67, the ratio of pectin methylesterase activity to polygalacturonase activity is about 1:4
-
-
-
additional information
?
-
-
polygalacturonase is an endo/exoenzyme, cf. EC 3.2.1.15
-
-
-
additional information
?
-
-
polygalacturonase is an endo/exoenzyme, cf. EC 3.2.1.15
-
-
-
additional information
?
-
-
inversion of configuration during hydrolysis of alpha-1,4-linkage
-
-
-
additional information
?
-
-
modelling of substrate binding, and active site structure, overview
-
-
-
additional information
?
-
-
PGase I is an exocellular enzyme releasing galacturonic acid
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
pectin + H2O
galacturonic acid + ?
-
the enzyme is highly specific for pectin substrates, overview. It hydrolyzes specifically the terminal glycosidic bond of the polymer and releases galacturonic acid the only degradation product
-
-
?
pectin + H2O
galacturonic acid + ?
-
the enzyme releases galacturonic acid by hydrolysis of pectin with a high degree of esterification
-
-
?
pectin + H2O
galacturonic acid + ?
-
the enzyme releases galacturonic acid by hydrolysis of pectin with a high degree of esterification
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
the enzyme releases monogalacturonic acid from its nonreducing end
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
the enzyme releases monogalacturonic acid from its nonreducing end
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
Q5W9U0
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolytic cleavage of the polygalacturonic acid chain
-
-
-
additional information
?
-
-
enzyme is involved in degradation of pectic molecules during root development
-
-
-
additional information
?
-
-
the enzyme is a bifunctional protein that has both pectin methylesterase, EC 3.1.1.11, and polygalacturonase activities, EC 3.2.1.15 and EC 3.2.1.67, the ratio of pectin methylesterase activity to polygalacturonase activity is about 1:4
-
-
-
additional information
?
-
-
PGase I is an exocellular enzyme releasing galacturonic acid
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Na+
additional information
Ca2+
-
Ca2+ enhances the stability of enzyme, and its activity by 10% at 2 mM and 10 mM, and by 30% at 5 mM
additional information
-
no effect by K+ and poor effects by Ca2+ and Fe3+ at 2 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-glycosylamine
-
of ammonium D-galactopyranuronate, competitive inhibition
-
D-galactopyranuronic acid
-
catabolite repression, completely inhibited, inhibitory constant 0.3 mM
additional information
-
activity on pectin decreases with an increase in degree of esterification
-
additional information
-
no inhibition by Cu2+ and Na+, poor inhibition by K+
-
additional information
-
polygalacturonase-inhibiting protein from stem extract of healthy and Ralstonia solanacearum-inoculated plants of tomato genotype King Kong2 inhibits exopolygalacturonase with increasing inhibition with higher quantities of plant extract
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HgCl2
-
0.01 mM, 3.4fold increase in activity, exo-PG2, no effect with exo-PG1
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the apparent Km-value with apple pectin as substrate is 1.82 mg/ml
-
additional information
additional information
-
kinetics in presence and absence of Ca2+, overview
-
additional information
additional information
-
1.79 mg/ml with [(1->4)-alpha-D-galacturonide]n for recombinant wild-type full-length enzyme, and 1.26 mg/ml with [(1->4)-alpha-D-galacturonide]n for recombinant catalytic polygalacturonase domain, pH 5.0, 50°C
-
additional information
additional information
-
1.58 mg/ml with [(1->4)-alpha-D-galacturonide]n at pH 5.5, 60°C
-
additional information
additional information
-
0.083 mg/ml with polygalacturonic acid at pH 4.8, 45°C
-
additional information
additional information
thermodynamic parameters of a series of galacturonic acid oligomers binding to isozyme RPG15, overview
-
additional information
additional information
-
thermodynamic parameters of a series of galacturonic acid oligomers binding to isozyme RPG15, overview
-
additional information
additional information
-
2.7 mg/ml with citrus polygalacturonic acid, pH 5.0, 50°C
-
additional information
additional information
-
6.7 mg/ml with [(1->4)-alpha-D-galacturonide]n, pH 4.0, 50°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2022
[(1->4)-alpha-D-galacturonide]n
-
pH 5.0, 50°C, recombinant catalytic polygalacturonase domain
4068
[(1->4)-alpha-D-galacturonide]n
-
pH 5.0, 50°C, recombinant wild-type full-length enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
58.7 mg/ml/s with [(1->4)-alpha-D-galacturonide]n, pH 4.0, 50°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47
purified recombinant His-tagged enzyme, substrate [(1->4)-alpha-D-galacturonide]n, pH 6.0, 40°C
additional information
-
with pectin as substrate: wild-type strain 97.8 U/ml, mutant strain M3 105.0 U/ml, mutant strain GH56 105.2 U/ml, and mutant strain Guserbiot 2.230 95.1 U/ml. Mutant strain M3 yields of enzyme activity is 1111.7 U/g on sugar beet and 142.1 U/g on apple pomace, while the wild-type strain gives 718.1 U/g and 240.0 U/g for sugar beet and apple pomace, respectively. Comprisons with commercial pectinases, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
4.5
4.5 - 5.5
4.8
5.2
5.3
5.5
5.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
3 - 10
-
the enzyme shows the highest activity between pH 4.5 and pH 5.5, and more than 80% between pH 5.0 and pH 6.5. At pH 3.0-4.5, the enzyme shows about 73% activity, at pH 10.0 44% activity
4.5 - 6
5 - 8
-
pH 5.0: about 50% of maximal activity, pH 8.0: about 55% of maximal activity
4.5 - 6
-
pH 4.5: about 75% of maximal activity, pH 6: about 80% of maximal activity
4.5 - 6
-
pH 4.5: about 75% of maximal activity, pH 6: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
45
50
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 65
-
35°C: about 65% of maximal activity, 65°C: about 50% of maximal activity
45 - 65
45 - 65
-
45°C: about 75% of maximal activity, 65°C: about 55% of maximal activity
45 - 65
-
45°C: about 65% of maximal activity, 65°C: about 65% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is produced during the whole growth phase
additional information
-
exo-polygalacturonase production carried out in solid-state fermentation is maximal using wheat bran/orange bagasse mixture
-
exo-polygalacturonase production carried out in solid-state fermentation is maximal using wheat bran/orange bagasse mixture
-
-
exoolygalacturonase production carried out in solid-state fermentation is maximal using wheat bran/sugar cane bagasse/orange bagasse mixture
-
exoolygalacturonase production carried out in solid-state fermentation is maximal using wheat bran/sugar cane bagasse/orange bagasse mixture
-
the isozymes show different expression patterns dependent on the medium composition, overview; the isozymes show different expression patterns dependent on the medium composition, overview
additional information
-
on solid-state fermentation carried out in culture media containing sugar cane bagasse and orange bagasse in proportions of 30% and 70% w/w at 45°C for 4 days
additional information
-
on solid-state fermentation carried out in culture media containing sugar cane bagasse and orange bagasse in proportions of 30% and 70% w/w at 45°C for 4 days
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
predicted presence of a putative signal peptide at residues 1-24
-
additional information
Klebsiella sp. Y1 CGMCC 4433
-
predicted presence of a putative signal peptide at residues 1-24
-
-
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