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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

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

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.15 endo-polygalacturonase

Purification

Purification on EC 3.2.1.15 - endo-polygalacturonase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
13fold, to homogeneity by two chromatography steps
-
2 electrophoretically distinct isoenzymes
-
2 isoenzymes
-
acetone precipitation and Sephadex G-100 gel filtration
-
affinity chromatography using polygalacturonic acid as ligand. Good results with silanized porous glass or keratin coated silica gel supports
-
alginate affinity precipitation and ultrafiltration
-
ammonium sulfate precipitation and ENrich SEC 650 gel filtration
ammonium sulfate precipitation, phenyl Sepharose column chromatography, Q Sepharose column chromatography and Superdex 75 gel filtration
ammonium sulfate precipitation, Sephacryl S-200 gel filtration, and CM-Sephadex gel filtration
ammonium sulfate precipitation, Sepharose CL 6B column chromatography, and DEAE Sepharose column chromatography
-
anion exchange column chromatography
-
beta-subunit of isoenzyme 1
-
by affinity and ion exchange chromatography, partially purified
-
by ammonium sulfate precipitation and two-step anion-exchange chromatography
Tetracoccosporium sp.
-
by cation exchange chromatography
-
by centrifugation, microfiltration and ultrafiltration
-
by gel filtration
-
by gel filtration and affinity chromatographies, to homogeneity
-
by thiol chromatography
-
cation-exchange chromatographic procedure for resolution between the salt-independent pectin methylesterase and PG fraction, followed by separation between PG1 and PG2. Final separation of PG1 and PG2 by addition of acetonitrile in the mobile phase is essential. Only a Convective Interaction Media carboxymethyl disk gives satisfactory results in this step for the isolation of PG1
-
DEAE-Sepharose column chromatography and Mono-Q Sepharose column chromatography
Tetracoccosporium sp.
-
from growth medium, by ammonium sulfate precipitation, dialysis, gel filtration and ion-exchange chromatography
HiTrap Q column chromatography
-
HiTrap Q Sepharose column chromatography
isoenzyme I, II and III
Saccharomyces fragilis
-
Mono Q column chromatography, high performance liquid chromatography and Shodex KW-802.5 gel filtration
-
native enzyme 100.9fold from palm fruits to homogeneity by concanavalin A affinity chromatography
-
native enzyme 12.34fold by two different steps of gel filtration, to homogeneity
-
native enzyme 15fold by ammonium sulfate fractionation, dialysis, anion exchange and affinity chromatography
-
native enzyme 5fold from solid-state fermentation on coffee pectin by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography
P19805
native enzyme 6.5fold by ethanol precipitation and gel filtration to homogeneity
-
native enzyme 89.2fold by gel filtration and cation exchange chromatography to homogeneity
-
native enzyme 9fold by ultrafiltration, ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
-
native enzyme from culture supernatant to homogeneity by anion exchange chromatography, gel filtration, and dialysis, and cation exchange chromatography
-
native enzyme from fruits 2fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native enzyme partially 7fold by gel filtration
-
native extracellular enzyme from culture medium
-
native secreted enzyme 3.43fold from submerged fermentation by ammonium sulfate fractionation, dialysis,/and gel filtration
-
Ni-NTA column chromatography and DE52-cellulose column chromatography
Ni-NTA column chromatography, gel filtration
-
Ni-NTA resin column chromatography
one-step concentration and partial purification of PG5 by adsorption to glass fiber microfilters, 100fold. By gel filtration two PG5 fractions (PGII and PGII), 306fold
-
one-step purification at pH 6.0 by immobilized metal affinity chromatography in the presence of 2 mM (4 mM) imidazole in the equilibration buffer, final recovery of enzyme activity of 100% (50%), about 10fold (12fold) purified. 5.3 and 3.4fold purified at pH 6.0 and 8.0 on affinity column. Purification factors of 7.2 and 5.3fold by using immobilized metal chelates containing short and long spacer arms, respectively
-
partial
partially purified by ion exchange chromatography, gel filtration, and preparative isoelectrofocusing, up to 207fold
-
polygalacturonase I and II
-
Q Sepharose column chromatography, SP Sepharose column chromatography, and Superdex 75 gel filtration
-
recombinant enzyme
-
recombinant enzyme from Pichia pastoris strain GS115 by ultrafiltration, gel filtration, and anion exchange chromatography, followed by deglycosylation of the proteins by endo-beta-N-acetylglucosaminidase H
recombinant extracellular enzyme from Pichia pastoris strain X-33 culture medium by ultrafiltration and dialysis, anion and cation exchange chromatography, dialysis, and hydrophobic interaction chromatography
-
recombinant wild-type full-length enzyme and isolated catalytic polygalacturonase domain from Pichia pastoris strain GS115 by ultrafiltration, gel filtration, and anion exchange chromatography, followed by deglycosylation of the proteins by endo-beta-N-acetylglucosaminidase H
-
Superdex 75 gel filtration
to apparent homogeneity, 21fold, by gel filtration and cation-exchange chromatography
-
to homogeneity
to homogeneity by a two-step chromatography procedure
to homogeneity by two chromatographic steps using cation exchange column and gel filtration, 85fold
-
to homogeneity, 5.8fold by cation exchange chromatography and gel filtration
to homogeneity, by free flow electrophoresis in isoelectric focusing mode using precipitation, followed by gel filtration
-
to homogeneity, by low-pressure liquid chromatography system, 54.4fold
to homogeneity, by low-pressure liquid chromatography system, 6.9fold
to near homogeneity by ammonium sulphate fractionation, followed by anion-exchange, gel filtration and affinity chromatography
-