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Information on EC 3.2.1.67 - galacturan 1,4-alpha-galacturonidase
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EC Tree
3.2.1.67 galacturan 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
- fruit
- tomato
-
ripening
- lyase
- cellulase
- aspergillus
- pectate
- ethylene
-
softening
- polygalacturonic
-
methylesterase
- niger
-
firmness
-
pgips
-
erwinia
- esculentum
-
postharvest
-
pectinolytic
-
ripe
-
galacturonic
- lycopersicon
- pectinases
-
abscission
- pectinesterase
- cinerea
-
botrytis
- xylanase
-
carotovora
-
3.2.1.15
- banana
-
ripening-related
-
expansins
- chrysanthemi
-
wall-degrading
- endo-pgs
- oligogalacturonides
-
climacteric
- homogalacturonan
- pectinmethylesterase
-
firmer
-
soft-rotting
- expansum
- 1-methylcyclopropene
-
pollen-specific
-
fruit-specific
- rhamnogalacturonans
-
cell-wall-degrading
-
persea
- nutrition
-
rotten
- synthesis
- food industry
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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-D-galacturonanase
-
-
-
-
exo-D-galacturonase
-
-
-
-
Exo-PG
exo-PGU B
exo-polygalacturonanase
exo-polygalacturonase
exolytic PGase
-
-
-
-
exoPG
exoPG1
exoPG2
exoPGase
-
-
-
-
exopoly-D-galacturonase
-
-
-
-
exopolygalacturonanase
exopolygalacturonase
exopolygalacturonase B
exopolygalacturonase X
Galacturan 1,4-alpha-galacturonidase
-
-
-
-
GH28
oligogalacturonate hydrolase
pectinase
PelB
PG III
PGase
-
-
-
-
PGI
poly 1,4-alpha-D-galacturonide-galacturonohydrolase
-
-
-
-
Poly(1,4-alpha-D-galacturonide)galacturonohydrolase
-
-
-
-
poly(galacturonate)hydrolase
-
-
-
-
poly-(1-4)-alpha-D-galactosiduronate glycanohydrolase
polygalacturonase
polymethylgalacturonase
TM0437
additional information
-
the enzyme belongs to the glycosyl hydrolase family 28, GH28
exo-polygalacturonanase
Thermotoga thermophilus DSM 5069
-
-
-
exo-polygalacturonase
-
-
-
-
exoPG
-
-
-
-
exopolygalacturonase
-
-
-
-
GH28
Thermotoga thermophilus DSM 5069
-
-
-
pectinase
-
-
-
-
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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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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
-
-
-
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 + ?
-
-
-
?
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
-
-
-
?
(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
-
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
-
-
?
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 + ?
-
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 + ?
-
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
[(1->4)-alpha-D-galacturonide]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]2 + H2O
[(1->4)-alpha-D-galacturonide]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]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
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+
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
-
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE