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Information on EC 3.2.1.67 - galacturonan 1,4-alpha-galacturonidase
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EC Tree
3.2.1.67 galacturonan 1,4-alpha-galacturonidaseIUBMB Comments
The enzyme hydrolyses the first glycosidic bond from the non-reducing end of the substrate. It is specific for saturated oligomers of D-homogalacturonan, and is unable to degrade unsaturated substrates or methyl-esterified substrates.
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Word Map
- 3.2.1.67
- pectin
- tomato
-
ripening
- cellulase
- aspergillus
- ethylene
-
softening
-
methylesterase
- polygalacturonic
- pectate
-
firmness
-
pgips
- pectinases
-
pectinolytic
- erwinia
-
postharvest
- niger
-
ripe
- esculentum
-
galacturonic
- lycopersicon
- cinerea
- carotovora
-
abscission
- xylanase
- pectinesterase
-
3.2.1.15
- botrytis
- sclerotinia
-
wall-degrading
- banana
-
expansins
-
climacteric
- chrysanthemi
-
ripening-related
- oligogalacturonides
- homogalacturonans
- pectinmethylesterase
- endo-pgs
- 1-methylcyclopropene
- persea
-
rotten
- nutrition
- synthesis
- expansum
- rhamnogalacturonan
-
methylesterification
-
firmer
-
cell-wall-degrading
- food industry
- analysis
-
pollen-specific
-
fruit-specific
-
soft-rotting
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
alkaline exo-polygalacturonase, carrot exopolygalacturonase, CbPelA, corn pollen polygalacturonase, EPG, exo polygalacturonase, exo-D-galacturonanase, exo-D-galacturonase, Exo-PG, exo-PGase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkaline exo-polygalacturonase
CbPelA
EPG
exo polygalacturonase
Exo-PG
exo-PGU B
exo-polygalacturonanase
exo-polygalacturonase
exoPG
exoPG1
exoPG2
exopolygalacturonanase
exopolygalacturonase
exopolygalacturonase B
exopolygalacturonase X
GH28
oligogalacturonate hydrolase
pectinase
PelB
PG III
PGI
poly-(1-4)-alpha-D-galactosiduronate glycanohydrolase
polygalacturonase
polymethylgalacturonase
TM0437
additional information
-
the enzyme belongs to the glycosyl hydrolase family 28, GH28
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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
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SYSTEMATIC NAME
IUBMB Comments
poly[(1->4)-alpha-D-galacturonide] non-reducing-end galacturonohydrolase
The enzyme hydrolyses the first glycosidic bond from the non-reducing end of the substrate. It is specific for saturated oligomers of D-homogalacturonan, and is unable to degrade unsaturated substrates or methyl-esterified substrates.
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CAS REGISTRY NUMBER
COMMENTARY
9045-35-6
-
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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
-
?
apple pectin + H2O
galacturonic acid
-
2% activity compared to polygalacturonic acid
-
-
?
arabinogalactan + H2O
?
-
exopolygalacturonase still contains arabanase activity, limits the usefulness on any pectic polysaccharide with arabinose residues
-
-
?
banana stem tissue + H2O
?
maceration activity
-
-
?
GalAalpha(1->4)GalAalpha(1->4)GalA + H2O
GalAalpha(1->4)GalA + D-galacturonic acid
-
-
-
-
?
methylated pectin + H2O
galacturonic acid
-
20% activity compared to polygalacturonic acid
-
-
?
polygalacturonate + H2O
D-galacturonic acid + ?
-
-
-
?
polygalacturonate + H2O
galacturonic acid
-
-
-
?
tetragalacturonic acid + H2O
galacturonic acid + trigalacturonic acid
-
modelling of substrate binidng, structure, overview
-
-
?
xylogalacturonan + H2O
xylogalacturonate
-
terminal galacturonic acid residue carries a single xylose substitution
-
?
[(1->4)-alpha-D-galacturonide]170 + H2O
[(1->4)-alpha-D-galacturonide]169 + D-galacturonate
[(1->4)-alpha-D-galacturonide]4 + H2O
[(1->4)-alpha-D-galacturonide]3 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(1->4)-alpha-D-galacturonide]5 + H2O
[(1->4)-alpha-D-galacturonide]4 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(1->4)-alpha-D-galacturonide]6 + H2O
[(1->4)-alpha-D-galacturonide]5 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(1->4)-alpha-D-galacturonide]7 + H2O
[(1->4)-alpha-D-galacturonide]6 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(1->4)-alpha-D-galacturonide]8 + H2O
[(1->4)-alpha-D-galacturonide]7 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(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
-
-
?
(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
-
-
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
-
-
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
Geotrichum lactis
-
-
-
-
?
(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
-
-
-
?
(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
-
-
?
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
-
-
?
citrus pectin + H2O
galacturonic acid
-
-
-
?
citrus pectin + H2O
galacturonic acid
-
citrus pectin with 26% degree of methyl esterification is a better substrate than citrus pectin with 82% degree of methyl esterification
-
-
?
citrus pectin + H2O
galacturonic acid
-
citrus pectin with 26% degree of methyl esterification is a better substrate than citrus pectin with 82% degree of methyl esterification
-
-
?
citrus pectin DE 72% + H2O
galacturonic acid
-
58.19% activity compared to citrus pectin DE 30%
-
-
?
citrus pectin DE 72% + H2O
galacturonic acid
-
58.19% activity compared to citrus pectin DE 30%
-
-
?
citrus pectin DE 85% + H2O
galacturonic acid
-
7.18% activity compared to citrus pectin DE 30%
-
-
?
citrus pectin DE 85% + H2O
galacturonic acid
-
7.18% activity compared to citrus pectin DE 30%
-
-
?
digalacturonic acid + H2O
2 galacturonic acid
-
complete hydrolysis
-
-
?
digalacturonic acid + H2O
2 galacturonic acid
-
complete hydrolysis
-
-
?
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 + ?
-
-
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
-
PGII solubilizes pectin very effective
-
-
?
pectin + H2O
galacturonic acid + ?
-
53% degree of methylation, marginal activity
-
-
?
pectin + H2O
galacturonic acid + ?
-
53% degree of methylation, marginal activity
-
-
?
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
-
incomplete hydrolysis, after 24 h incubation about 50% of the substrate is hydrolyzed
-
-
?
polygalacturonic acid + H2O
galacturonic acid
-
incomplete hydrolysis, after 24 h incubation about 50% of the substrate is hydrolyzed
-
-
?
polygalacturonic acid + H2O
galacturonic acid
-
the enzyme can only catalyze a single reaction with each substrate, with the products being D-galacturonic acid and a polymer/oligomer containing one fewer D-galacturonic acid units than the substrate that was attacked
-
-
?
polygalacturonic acid + H2O
galacturonic acid + ?
-
preferred substrate
-
-
?
trigalacturonic acid + H2O
digalacturonic acid + galacturonic acid
-
complete hydrolysis
-
-
?
trigalacturonic acid + H2O
digalacturonic acid + galacturonic acid
-
complete hydrolysis
-
-
?
trigalacturonic acid + H2O
digalacturonic acid + galacturonic acid
-
-
-
?
trigalacturonic acid + H2O
digalacturonic acid + galacturonic acid
-
-
-
?
trigalacturonic acid + H2O
digalacturonic acid + galacturonic acid
Thermotoga thermophilus
-
-
-
-
?
trigalacturonic acid + H2O
digalacturonic acid + galacturonic acid
Thermotoga thermophilus DSM 5069
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]170 + H2O
[(1->4)-alpha-D-galacturonide]169 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(1->4)-alpha-D-galacturonide]170 + H2O
[(1->4)-alpha-D-galacturonide]169 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(1->4)-alpha-D-galacturonide]2 + H2O
2 D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(1->4)-alpha-D-galacturonide]2 + H2O
2 D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(1->4)-alpha-D-galacturonide]3 + H2O
[(1->4)-alpha-D-galacturonide]2 + D-galacturonate
-
-
-
?
[(1->4)-alpha-D-galacturonide]3 + H2O
[(1->4)-alpha-D-galacturonide]2 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(1->4)-alpha-D-galacturonide]3 + H2O
[(1->4)-alpha-D-galacturonide]2 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(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
-
-
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
[(1->4)-alpha-D-galacturonide]n + H2O
[(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
the enzyme shows increasing activity on oligosaccharides with an increasing degree of polymerization. The enzyme displays specificity for saturated oligoGalpA and is unable to degrade unsaturated or methyl-esterified oligoGalpA
-
-
?
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
?
-
-
no activity with carboxymethyl cellulose and xylan
-
-
?
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
?
-
the enzyme shows low activity with xylogalacturonan
-
-
?
additional information
?
-
the enzyme shows low activity with xylogalacturonan
-
-
?
additional information
?
-
-
PGase I is an exocellular enzyme releasing galacturonic acid
-
-
?
additional information
?
-
-
no activity with xylan and carboxymethyl cellulose
-
-
?
additional information
?
-
-
no activity with xylan and carboxymethyl cellulose
-
-
?
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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
polygalacturonic acid + H2O
galacturonic acid
-
the enzyme can only catalyze a single reaction with each substrate, with the products being D-galacturonic acid and a polymer/oligomer containing one fewer D-galacturonic acid units than the substrate that was attacked
-
-
?
citrus pectin + H2O
galacturonic acid
-
citrus pectin with 26% degree of methyl esterification is a better substrate than citrus pectin with 82% degree of methyl esterification
-
-
?
citrus pectin + H2O
galacturonic acid
-
citrus pectin with 26% degree of methyl esterification is a better substrate than citrus pectin with 82% degree of methyl esterification
-
-
?
pectin + H2O
galacturonic acid + ?
-
53% degree of methylation, marginal activity
-
-
?
pectin + H2O
galacturonic acid + ?
-
53% degree of methylation, marginal activity
-
-
?
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
-
-
-
?
[(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
Al3+
Ca2+
Co2+
Cu2+
K+
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
-
Zn2+ and Co2+ have no effect on the catalysis of isoform exoPG1. Mg2+ and Mn2+ do not affect catalysis of isoform exoPG2
additional information
-
no effect by K+ and poor effects by Ca2+ and Fe3+ at 2 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-glycosylamine ammonium D-galactopyranuronate
-
of ammonium D-galactopyranuronate, competitive inhibition
D-galactopyranuronic acid
-
catabolite repression, completely inhibited, inhibitory constant 0.3 mM
Hg2+
-
isoform exoPG1 shows 50% inhibition at 1 mM, isoform exoPG2 shows 97% inhibition at 1 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
-
additional information
Thermotoga thermophilus
-
no substrate inhibition for polygalacturonate
-
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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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
High-throughput screening of Erwinia chrysanthemi pectin methylesterase variants using carbohydrate microarrays.
Acquired Immunodeficiency Syndrome
Isolation of Polygalacturonase-Producing Bacterial Strain from Tomatoes (Lycopersicon esculentum Mill.).
Dehydration
Comparative transcriptome analysis of translucent flesh disorder in mangosteen (Garcinia mangostana L.) fruits in response to different water regimes.
Dehydration
Ozone fumigation for safety and quality of wine grapes in postharvest dehydration.
Dehydration
Postharvest ethylene treatment affects berry dehydration, polyphenol and anthocyanin content by increasing the activity of cell wall enzymes in Aleatico wine grape
Infections
Action of selenium against Sclerotinia sclerotiorum: Damaging membrane system and interfering with metabolism.
Infections
Brassica napus polygalacturonase inhibitor proteins inhibit Sclerotinia sclerotiorum polygalacturonase enzymatic and necrotizing activities and delay symptoms in transgenic plants.
Infections
Brassica napus possesses an expanded set of polygalacturonase inhibitor protein genes that are differentially regulated in response to Sclerotinia sclerotiorum infection, wounding and defense hormone treatment.
Infections
Changes in cell wall pectin and pectinase activity in apple and tomato fruits during Penicillium expansum infection
Infections
Claviceps purpurea expressing polygalacturonases escaping PGIP inhibition fully infects PvPGIP2 wheat transgenic plants but its infection is delayed in wheat transgenic plants with increased level of pectin methyl esterification.
Infections
Comparative genomic and transcriptomic analyses reveal different pathogenicity-related genes among three eucalyptus fungal pathogens.
Infections
Effects of Calcium Salts on Growth, Polygalacturonase Activity, and Infection of Peach Fruit by Monilinia fructicola.
Infections
Effects of calcium salts on growth, polygalacturonase activity, and infection of peach fruit by Monilinia fructicola.
Infections
Influence of phytic acid and its metal complexes on the activity of pectin degrading polygalacturonase
Infections
Influence of phytic acid and its metal complexes on the activity of pectin degrading polygalacturonase.
Infections
Interaction of Sclerotinia sclerotiorum with Brassica napus: cloning and characterization of endo- and exo-polygalacturonases expressed during saprophytic and parasitic modes.
Infections
Mechanism of Cell Wall Polysaccharides Modification in Harvested 'Shatangju' Mandarin (Citrus reticulate Blanco) Fruit Caused by Penicillium italicum.
Infections
Natural resistance against pre- and post-harvest pathogens in Sardinian pears germoplasm.
Infections
Pectin induced transcriptome of a Rhizoctonia solani strain causing sheath blight disease in rice reveals insights on key genes and RNAi machinery for development of pathogen derived resistance.
Infections
Polygalacturonase gene pgxB in Aspergillus niger is a virulence factor in apple fruit.
Infections
Polygalacturonase inhibiting protein: isolation, developmental regulation and pathogen related expression in Panax ginseng C.A. Meyer.
Infections
Polygalacturonase Isozymes Produced by Phomopsis cucurbitae in Relation to Postharvest Decay of Cantaloupe Fruit.
Infections
Polygalacturonase isozymes produced by Phomopsis cucurbitae in relation to postharvest decay of cantaloupe fruit.
Infections
Polygalacturonase-inhibiting protein 2 of Phaseolus vulgaris inhibits BcPG1, a polygalacturonase of Botrytis cinerea important for pathogenicity, and protects transgenic plants from infection.
Infections
Production, characterization, and identification using proteomic tools of a polygalacturonase from Fusarium graminearum.
Infections
Pyramiding PvPGIP2 and TAXI-III But Not PvPGIP2 and PMEI Enhances Resistance Against Fusarium graminearum.
Infections
Structure and expression of two polygalacturonase genes of Claviceps purpurea oriented in tandem and cytological evidence for pectinolytic enzyme activity during infection of rye.
Infections
The Erwinia chrysanthemi phoP-phoQ operon plays an important role in growth at low pH, virulence and bacterial survival in plant tissue.
Infections
The key iron assimilation genes ClFTR1, ClNPS6 were crucial for virulence of Curvularia lunata via initiating its appressorium formation and virulence factors.
Infections
The pH signaling transcription factor PacC is required for full virulence in Penicillium digitatum.
Infections
Use of transgenic plants to study the role of ethylene and polygalacturonase during infection of tomato fruit by Colletotrichum gloeosporioides.
Infections
[Role of a protein inhibitor of polygalacturonase in ripening of apples and their resistance of infection with Monilia fructigena, the causative agent of fruit rot]
Infertility
ps-2, the gene responsible for functional sterility in tomato, due to non-dehiscent anthers, is the result of a mutation in a novel polygalacturonase gene.
Infertility, Male
iTRAQ-based proteomic analysis of fertile and sterile flower buds from a genetic male sterile line 'AB01' in Chinese cabbage (Brassica campestris L. ssp. pekinensis).
Mite Infestations
Study of defense-related gene expression in grapevine infested by Colomerus vitis (Acari: Eriophyidae).
Mycoses
Gene encoding polygalacturonase inhibitor in apple fruit is developmentally regulated and activated by wounding and fungal infection.
Neoplasms
Immunochemical study and cellular localization of human pepsinogens during ontogenesis and in gastric cancers.
Plant Diseases
Paper-based colorimetric sensor for easy and simple detection of polygalacturonase activity aiming for diagnosis of Allium white rot disease.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE