3.2.1.15: endo-polygalacturonase This is an abbreviated version! For detailed information about endo-polygalacturonase, go to the full flat file .
Reaction
(1,4-alpha-D-galacturonosyl)n+m +
H2O =
(1,4-alpha-D-galacturonosyl)n +
(1,4-alpha-D-galacturonosyl)m
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
Natural Substrates Products
Natural Substrates Products on EC 3.2.1.15 - endo-polygalacturonase
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polygalacturonate + H2O
oligogalacturonates
polygalacturonic acid + H2O
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additional information
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pectate + H2O
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the pollen-specific protein LLP-PG digests the 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans and may function during pollen development, germination or tube growth by pectin depolymerization. It may degrade the walls of the stylar cells to allow penetration of the pollen tube
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pectate + H2O
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pectin + H2O
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mango peel pectin
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pectin + H2O
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mango peel pectin
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pectin + H2O
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citrus or apple pectin
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pectin + H2O
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citrus or apple pectin
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pectin + H2O
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P19805
coffee pectin
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pectin + H2O
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citrus pectin with 26% and 92% degree of esterification, and apple pectin
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pectin + H2O
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citrus pectin with 26% and 92% degree of esterification, and apple pectin
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polygalacturonan + H2O
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polygalacturonan + H2O
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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the enzyme exhibits endo- and exo-activity
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonate + H2O
oligogalacturonates
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polygalacturonic acid + H2O
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polygalacturonic acid + H2O
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polyuronide + H2O
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polygalacturonase, EC 3.2.1.15 and pectinmethylesterase, EC 3.2.1.11 operate in tandem to degrade methylesterified polyuronides
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polyuronide + H2O
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polygalacturonase, EC 3.2.1.15 and pectinmethylesterase, EC 3.2.1.11 operate in tandem to degrade methylesterified polyuronides
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additional information
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the enzyme catalyzes the hydrolytic cleavage of the polygalacturonic acid chain
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additional information
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the enzyme catalyzes the hydrolytic cleavage of the polygalacturonic acid chain
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additional information
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the enzyme is produced inducibly in a medium containing D-galacturonic acid or pectin
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additional information
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enzyme is involved in host penetration by the fungus
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additional information
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the enzyme is involved in the rotting and maceration of fresh fruit and vegetables
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additional information
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the enzyme is involved in the rotting and maceration of fresh fruit and vegetables
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additional information
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the enzyme is a factor inducing silver-leaf symptoms on apple trees
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additional information
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O2 and galacturonate negatively regulate enzyme synthesis, and glucose as carbon source affords better enzyme yield than lactose
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additional information
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O2 and galacturonate negatively regulate enzyme synthesis, and glucose as carbon source affords better enzyme yield than lactose
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additional information
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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
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additional information
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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
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additional information
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isozyme specific PG activity in wild-type and non-virulent phenotype conversion mutant and cleavage mode, overview
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additional information
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isozyme specific PG activity in wild-type and non-virulent phenotype conversion mutant and cleavage mode, overview
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additional information
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the enzyme plays a key role in early stages of infection in head and basal rot, diseases which destroy sunflower
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additional information
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together with other pectinolytic enzymes the polygalacturonase is involved in the degradation of pectin
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additional information
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under saprophytic growth conditions, sspg1d, sspg3 and sspg5 expression is induced by pectin and galacturonic acid and subject to catabolite repression by glucose. Transfer of mycelia from liquid media to solid substrates induces expression of sspg1d suggesting that it may also be regulated by thigmotrophic interactions. Under pathogenic conditions, sspg1d is highly expressed during infection. sspg3 is also expressed during infection, albeit at lower level than sspg1d, whereas sspg5 is expressed only weakly
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additional information
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under saprophytic growth conditions, sspg1d, sspg3 and sspg5 expression is induced by pectin and galacturonic acid and subject to catabolite repression by glucose. Transfer of mycelia from liquid media to solid substrates induces expression of sspg1d suggesting that it may also be regulated by thigmotrophic interactions. Under pathogenic conditions, sspg1d is highly expressed during infection. sspg3 is also expressed during infection, albeit at lower level than sspg1d, whereas sspg5 is expressed only weakly
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additional information
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additional information
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inducible enzyme
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