3.2.1.15: endo-polygalacturonase
This is an abbreviated version!
For detailed information about endo-polygalacturonase, go to the full flat file.
Word Map on EC 3.2.1.15
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3.2.1.15
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aspergillus
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pepsinogen
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polygalacturonic
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niger
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galacturonic
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tomato
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pylori
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ripening
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citrus
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helicobacter
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gastritis
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fusarium
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polygalacturonase-inhibiting
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pgips
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methylesterase
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pectinases
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botrytis
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homogalacturonan
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cinerea
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alternaria
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peach
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macer
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sclerotiorum
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rhamnogalacturonans
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softening
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exopolygalacturonase
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sclerotinia
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ripe
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moniliforme
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pectolytic
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oligogalacturonates
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carotovora
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marxianus
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methylesterified
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food industry
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wall-degrading
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pylori-positive
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purpureum
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lindemuthianum
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methylesterification
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stereum
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cochliobolus
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pectinesterase
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polyuronides
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de-esterification
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pectin-degrading
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agriculture
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lycopersici
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nutrition
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medicine
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industry
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analysis
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degradation
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paper production
- 3.2.1.15
- aspergillus
- pepsinogen
- polygalacturonic
- niger
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galacturonic
- tomato
- pylori
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ripening
- citrus
- helicobacter
- gastritis
- fusarium
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polygalacturonase-inhibiting
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pgips
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methylesterase
- pectinases
- botrytis
- homogalacturonan
- cinerea
- alternaria
- peach
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macer
- sclerotiorum
- rhamnogalacturonans
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softening
- exopolygalacturonase
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sclerotinia
-
ripe
- moniliforme
-
pectolytic
- oligogalacturonates
- carotovora
- marxianus
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methylesterified
- food industry
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wall-degrading
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pylori-positive
- purpureum
- lindemuthianum
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methylesterification
- stereum
- cochliobolus
- pectinesterase
- polyuronides
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de-esterification
-
pectin-degrading
- agriculture
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lycopersici
- nutrition
- medicine
- industry
- analysis
- degradation
- paper production
Reaction
Synonyms
ADPG1, ADPG2, Aj-PGase, alkaline endo-PG, ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE1, At1g48100, BcPeh28A, BPN3, CluPG1, D-galacturonase, endo PG, endo-D-galacturonanase, endo-D-galacturonase, endo-PG, endo-PG I, endo-pgaA, endo-polygalacturonase, endo-polygalacturonase A, endo-polygalacturonase C, endo-polygalacturonase I, endo-polygalacturonase II, endo-polygalacturonase-3, endo-TePG28b, endogalacturonase, endopectinase, endoPG, EndoPG I, endoPG II, endopolygalacturonase, endopolygalacturonase I, endopolygalacturonases, endopolygalacturonate lyase, EnPG28A, EPG, Epg1-2p, EPG4, Exo-PG, exo-polygalacturonase, FgPG, FpPG, liquifying polygalacturonase, LLP-A1.1 protein, LLP-PG, Magnaporthe oryzae density dependent germination regulator, male fertility 9, MDG1, MF9, More, MpPG2, non-acidic polygalacturonase, OGH, oligogalacturonate hydrolase, P1/P3, P2C, pectate hydrolase, pectic depolymerase, pectic hydrolase, pectin depolymerase, pectin hydrolase, pectin polygalacturonase, pectinase, pectinase SS, pectolase, pectozyme, Peh28A, PehA, PehB, PG, PG II, PG-2A, PG-3, PG1, PG2, PG28A, PG3, PG4, PG5, PG6, PG63, PG8fn, PGA, PGase, PGase SM, PGC, PGI, PGII, PGIP, PGL, Pgu1, phylendonase, poly [1, 4-alpha-D-galacturonide] glycano-hydrolase, poly-alpha-1,4-galacturonide glycanohydrolase, poly-[1,4-alpha-D-galacturonide] glycanohydrolase, polygalacturonase 1, polygalacturonase I, polygalacturonase II, polygalacturonase inhibiting protein 1, polygalacturonase p36, polygalacturonase p40, polygalacturonase-3, polygalacturonase-inhibitor-like, QRT2, QUARTET2, remanase, RPG1, ScPgu1, SpPgu1
ECTree
3.2.1.15 endo-polygalacturonaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.15 - endo-polygalacturonase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D244A
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the mutant shows significantly increased thermostability and retains activity comparable to that of the wild type enzyme
D244A/D299R
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the mutant shows catalytic activity, which is comparable to that of the wild type enzyme. The mutant shows the most pronounced shifts in temperature of maximum enzymatic activity, temperature at which 50% of the maximal activity of an enzyme is retained, and melting temperature, of about 10, 17, and 10.2°C upward, respectively, with the half-life extended by 8.4 h at 50°C and 45 min at 55°C compared to the wild type
D299R
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the mutant shows significantly increased thermostability and retains activity comparable to that of the wild type enzyme
industry
D201N
N178D
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has an activity approximately 20fold lower than the native Aspergillus niger PGII
D129K
the mutant shows increased catalytic efficiency towards trigalacturonic acid compared to the wild type enzyme
D192A
PG2 mutant causes no symptoms, lacks PG activity and is unable to cause symptoms in plant tissue upon infiltration
D203A
PG1 mutant, causes chlorotic symptoms with scattered yellow or brown patches to a similar extent as the wild-type PG1
A274T
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site-directed mutagenesis, the mutation causes a marked loss of inhibition by PvPGIP2 of 150fold
K116E
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site-directed mutagenesis, the mutant shows no inhibition by PvPGIP2
L303E
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site-directed mutagenesis, the mutant enzyme is inhibited by Inhibitor mutant PvPGIP2.Q224K in contrast to the wild-type enzyme
N121K
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site-directed mutagenesis, the mutation only slightly affects inhibition by PvPGIP2
Q124P
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site-directed mutagenesis, the mutation only slightly affects inhibition by PvPGIP2
S120N
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site-directed mutagenesis, the mutation only slightly affects inhibition by PvPGIP2
S120N/N121K/S122D
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site-directed mutagenesis, the triple mutant is inhibited with a 25fold reduced efficiency by PvPGIP2
S122D,
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site-directed mutagenesis, the mutation only slightly affects inhibition by PvPGIP2
H58Y
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the mutant shows improved thermostability and catalytic efficiency compared to the wild type enzyme
H58Y/T71Y/T304Y
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the mutant shows improved thermostability and catalytic efficiency compared to the wild type enzyme
T304Y
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the mutant shows improved thermostability and catalytic efficiency compared to the wild type enzyme
T71Y
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the mutant shows improved thermostability and catalytic efficiency compared to the wild type enzyme
additional information
industry
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the enzyme is suitable for application as a textile bioscouring agent
industry
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the enzyme is suitable for application as a textile bioscouring agent
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D201N
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inactive, point mutation in the catalytic site that causes complete loss of enzymatic activity
additional information
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under normal growing conditions, single adpg2 mutants appear similar to wild-type plants in terms of pod shatter and also produce monad pollen. Reduced pod shatter in adpg2-1 and adpg2-2 plants (and in double mutants with qrt2) when watering is ceased before overall plant senescence is complete. Siliques of the double-mutants adpg1-1 adpg2-1 and adpg1-2 adpg2-2 exhibit a more severe phenotype than do those of the adpg1 single mutants and fail to dehisce even if compressed. In terms of pod shatter and seed abscission, adpg2 qrt2 double mutants are similar to adpg2 single mutants, double mutants lacking both ADPG1 and QRT2 appear identical to adpg1 single mutants, and the adpg1-1 adpg2-1 qrt2-2 and adpg1-2 adpg2-2 qrt2-3 triple mutants resemble the adpg1 adpg2 double mutants
additional information
amino acids S191/D240 of PGI are unique in binding the pectin backbone and are possibly crucial for its specificity. D240 and R96 of PGI work as crampons to favour the sliding of the substrate
additional information
amino acids S191/D240 of PGI are unique in binding the pectin backbone and are possibly crucial for its specificity. D240 and R96 of PGI work as crampons to favour the sliding of the substrate
additional information
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amino acids S191/D240 of PGI are unique in binding the pectin backbone and are possibly crucial for its specificity. D240 and R96 of PGI work as crampons to favour the sliding of the substrate
additional information
amino acids S234/S91 of PGII are unique in binding the pectin backbone and are possibly crucial for its specificity
additional information
amino acids S234/S91 of PGII are unique in binding the pectin backbone and are possibly crucial for its specificity
additional information
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amino acids S234/S91 of PGII are unique in binding the pectin backbone and are possibly crucial for its specificity
additional information
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immobilization of the partially purified native enzyme, the sodium alginate immobilized polygalacturonase exhibits more stability to changes in pH than the temperature. Activity of the immobilized polygalacturonase is reduced to 34.56% and 14.81% of the initial activity after the second and third catalytic cycles, respectively, half-life is 10 min at pH 4.5, 40°C
additional information
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immobilization of the partially purified native enzyme, the sodium alginate immobilized polygalacturonase exhibits more stability to changes in pH than the temperature. Activity of the immobilized polygalacturonase is reduced to 34.56% and 14.81% of the initial activity after the second and third catalytic cycles, respectively, half-life is 10 min at pH 4.5, 40°C
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additional information
when PehA is inactivated, Burkholderia glumae retains rice virulence comparable to that of the wild-type parent strain
additional information
when PehA is inactivated, Burkholderia glumae retains rice virulence comparable to that of the wild-type parent strain
additional information
when PehB is inactivated, Burkholderia glumae retains rice virulence comparable to that of the wild-type parent strain
additional information
when PehB is inactivated, Burkholderia glumae retains rice virulence comparable to that of the wild-type parent strain
additional information
amino acids S245/V89 of PG are unique in binding the pectin backbone and are possibly crucial for its specificity
additional information
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mutant that lacks the endoPG homolog gene MGG_08938. The pathogenicity, mycelial growth, and appressorium formation of the MGG_08938 null mutant are comparable with those of the wild-type strain, whereas germination of conidia in a highly concentrated suspension of conidia is affected
additional information
Pyricularia oryzae P2-R
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mutant that lacks the endoPG homolog gene MGG_08938. The pathogenicity, mycelial growth, and appressorium formation of the MGG_08938 null mutant are comparable with those of the wild-type strain, whereas germination of conidia in a highly concentrated suspension of conidia is affected
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additional information
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in mutant MH172 with cloned pehA, MH172(pRKpeh), wild-type-level polygalacturonase activity is restored
additional information
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mutants pghAxc and pghBxc and double mutant, which show lower hydrolytic activities compared to the wild-type, especially the pghAxc mutant and the double mutant. The wild-type causes distinctive necrosis symptoms compared with the mutants and the double mutant, all of which elicite weak symptoms with a minor wilt in both dip- and spray-inoculation assays. Mutant-complemented strains of both pghAxc and pghBxc are able to elicit the same distinctive necrosis symptoms as the wild-type. No differences between the wild-type and the mutants using the infiltration method
additional information
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in mutant MH172 with cloned pehA, MH172(pRKpeh), wild-type-level polygalacturonase activity is restored
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