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
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ripe
- moniliforme
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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
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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
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Application on EC 3.2.1.15 - endo-polygalacturonase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
analysis
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kinetic approach in a commercial enzyme preparation under pulsed electric fields explains satisfactorily evolution of PG activity and permits obtaining valuable information about the conditions for which either inactivation or enhancement of PG activity may happen. The mechanism offers simplicity and flexibility and can explain occurrences such as flat and activation shoulders at the beginning of inactivation curves for enzymes under pulsed electric field treatments
degradation
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multiplicity of PGs that degrade the pectin component of the plant tissue in different fashions
food industry
industry
medicine
despite the significant sequence homology and the conserved surface-exposed epitopes LLP-PG represents a low-allergenic member of pollen PGs
nutrition
paper production
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endopolygalacturonase, isolated by protein purification or by cloning its gene, can lower the cationic demand of peroxide-bleached mechanical pulps and increase the effectiveness of cationic retention aids
additional information
agriculture
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PG plants exhibit enhanced resistance to the necrotrophic fungal pathogen Botrytis cinerea and to the virulent bacterial pathogen Pseudomonas syringae and have constitutively activated defense responses by releasing oligogalacturonides
agriculture
PG1 causes chlorosis and the development of yellow or brown patches scattered over the infiltrated area of the leaf
agriculture
PG2 causes the most severe symptoms like necrosis and tissue collapse as compared to other PGs
agriculture
PG3 cause no symptoms
agriculture
PG4 causes chlorosis and the development of yellow or brown patches scattered over the infiltrated area of the leaf similar to PG1
agriculture
PG5 causes chlorosis and the development of yellow or brown patches scattered over the infiltrated area of the leaf similar to PG1
agriculture
PG6 cause no symptoms
food industry
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agro-industrial wastes are suitable for polygalacturonase production
food industry
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agro-industrial wastes are suitable for polygalacturonase production
food industry
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high pressure processing can be used for selective inactivation of PG in tomato processing while keeping pectinmethylesterase intact
food industry
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properties of the enzyme may be highly beneficial during fruit processing
food industry
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the enzyme has a considerable potential for commercial application, primarily in the food and animal feedstock industries, due to features such as its optimum activity in acid medium, which remains at a high level at neutral pH, and good pH and temperature stability. The utilization of orange waste in PG production leads to an increase in yield with a reduction in process cost. Moreover, it adds value to the waste from the orange juice industry
food industry
Tetracoccosporium sp.
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the polygalacturonase has a remarkable heat-tolerance, which makes it very attractive for industrial applications
food industry
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to preserve or improve rheological properties of tomato based products, the combination of 40°C and 400MPa represents an optimal condition to reduce tomato PG activity while maintaining sufficient pectinmethylesterase activity
food industry
endo-PG I showed higher efficiency in juice clarification than the pectin lyase alone or the commercial pectinase widely used. Addition of endo-PG I at 3.4 U/ml reduces the intrinsic viscosity of apple juice by 4.5%, and increases the light transmittance by 71.8%. Endo-PG I is an interesting biocatalyst for juice clarification
food industry
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polygalacturonases are pectin substances degrading enzymes, that are widely used in juice and fruit beverages for quality improvement
food industry
P19805
the enzyme improves the elimination of coffee mucilage
food industry
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the enzyme is used for guava juice extraction and clarification. The recovery of juice of enzymatically treated pulp increases from 6% to 23%. Addition of purified enzyme increases the%T650 from 2.5 to 20.4 and °Brix from 1.9 to 4.8. The pH of the enzyme treated juice decreases from 4.5 to 3.02
food industry
the enzyme reduces the viscosity of papaya juice by 17.6% and increases its transmittance by 59.1%. Its favourable enzymatic properties make the enzyme attractive for potential applications in the juice industry
food industry
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the enzyme is able to enhance the clarification of citrus juice
food industry
the enzyme is used for grape juice clarification
food industry
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the enzyme is used for juice clarification of pear, banana and citrus
food industry
the enzyme significantly reduces the viscosities and improves the yields of fruit juices from banana, plantain, papaya, pitaya and mango
food industry
the enzyme significantly reduces the viscosity and increases the light transmittance of papaya pulp, and increases the recovery of the papaya extraction
food industry
Evansstolkia leycettana JCM 12802
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the enzyme is used for grape juice clarification
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food industry
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agro-industrial wastes are suitable for polygalacturonase production
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food industry
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the enzyme reduces the viscosity of papaya juice by 17.6% and increases its transmittance by 59.1%. Its favourable enzymatic properties make the enzyme attractive for potential applications in the juice industry
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food industry
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the enzyme is able to enhance the clarification of citrus juice
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food industry
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properties of the enzyme may be highly beneficial during fruit processing
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food industry
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the enzyme is used for guava juice extraction and clarification. The recovery of juice of enzymatically treated pulp increases from 6% to 23%. Addition of purified enzyme increases the%T650 from 2.5 to 20.4 and °Brix from 1.9 to 4.8. The pH of the enzyme treated juice decreases from 4.5 to 3.02
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food industry
Penicillium oxalicum CZ1028
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the enzyme significantly reduces the viscosities and improves the yields of fruit juices from banana, plantain, papaya, pitaya and mango
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food industry
Penicillium oxalicum CZ1028
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the enzyme significantly reduces the viscosity and increases the light transmittance of papaya pulp, and increases the recovery of the papaya extraction
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food industry
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the enzyme has a considerable potential for commercial application, primarily in the food and animal feedstock industries, due to features such as its optimum activity in acid medium, which remains at a high level at neutral pH, and good pH and temperature stability. The utilization of orange waste in PG production leads to an increase in yield with a reduction in process cost. Moreover, it adds value to the waste from the orange juice industry
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food industry
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polygalacturonases are pectin substances degrading enzymes, that are widely used in juice and fruit beverages for quality improvement
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food industry
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agro-industrial wastes are suitable for polygalacturonase production
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industry
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thermostable nature of the polygalacturonase with a high pH range for activity makes it an industrially important enzyme
industry
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the enzyme is developed a feasible strategy to achieve a rapid benign of the bioscouring process with the wettability properties of cotton fabrics
industry
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the enzyme is developed a feasible strategy to achieve a rapid benign of the bioscouring process with the wettability properties of cotton fabrics
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industry
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thermostable nature of the polygalacturonase with a high pH range for activity makes it an industrially important enzyme
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nutrition
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application in extraction of juice from certain fruits and vegetables
nutrition
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application in extraction of juice from certain fruits and vegetables
nutrition
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potential application of the enzyme in fruit juice extraction
nutrition
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the enzyme is very efficient to extract pectin from lemmon protopectin and to macerate carrot tissues at pH 2.0. These properties make the enzyme an interesting biocatalyst for industrial applications under highly acidic conditions
nutrition
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potential application of the enzyme in fruit juice extraction
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nutrition
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application in extraction of juice from certain fruits and vegetables
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additional information
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besides their role in recycling organic matter, saprobiotic enzymes like endopolygalacturonase may also play an important role in the induction of defensive mechanisms in wild plants by enhancing their non-specific resistance against pathogens
additional information
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function of polygalacturonase in the colonization of plant material rather than in the destruction of plant
additional information
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18 polygalacturonase genes identified in strain 99-880. Ancestral form of polygalacturonase in fungi is endolytic and exolytic function evolved later
additional information
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ADPG1 and ADPG2 are essential for silique dehiscence. ADPG2 and QRT2 contribute to floral organ abscission, while all three genes contribute to anther dehiscence
additional information
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BcMF2 (Brassica campestris male fertility 2) gene may encode a new polygalacturonase with an important role in pollen wall development, possibly via regulation of pectins dynamic metabolism
additional information
endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
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endoPG genes play important roles in the pathogenesis of Phytophthora parasitica. Each gene causes specific effects, varying from no symptoms to dwarfism, necrosis, leaf curl, silvery leaf, and cracks in leaf stalks. Appearance of these effects depends on the expression of a endoPG protein with a normal active site in the apoplast. Each gene plays a distinct role in the decomposition of plant cell wall
additional information
may be involved in cotton petal development and senescence, and in response to cold stress
additional information
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may be involved in cotton petal development and senescence, and in response to cold stress
additional information
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PehA is the major but not the sole polygalacturonase, it plays a minor role in Xanthomonas campestris virulence
additional information
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polygalacturonase genes can be efficiently induced in planta and are required for the full virulence of Xanthomonas campestris pv. campestris to Arabidopsis. Polygalacturonase is secreted via the type II secretion system in an Xps-dependent manner
additional information
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tobacco and Arabidopsis polygalacturonase plants inoculated with Botrytis cinerea are more resistant to microbial pathogens and have constitutively activated defense responses
additional information
Rhizopus arrhizus 99-880
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18 polygalacturonase genes identified in strain 99-880. Ancestral form of polygalacturonase in fungi is endolytic and exolytic function evolved later
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additional information
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PehA is the major but not the sole polygalacturonase, it plays a minor role in Xanthomonas campestris virulence
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additional information
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besides their role in recycling organic matter, saprobiotic enzymes like endopolygalacturonase may also play an important role in the induction of defensive mechanisms in wild plants by enhancing their non-specific resistance against pathogens
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