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alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
D-galacturonic acid
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-D-galacturonate + D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + galacturonate
-
-
no production of pentagalacturonate
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + galacturonate
-
-
59.3% alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + 38.7% galacturonate
-
?
apple pectin + H2O
digalacturonic acid
banana peel pectin + H2O
digalacturonic acid
carrot peel pectin + H2O
digalacturonic acid
cellulose + H2O
?
-
37.8% activity compared to polygalacturonic acid
-
-
?
citrus pectin + H2O
D-(+)-galacturonic acid + ?
citrus peel pectin + H2O
digalacturonic acid
galacturonosyl-galactonic acid + H2O
?
-
-
-
-
?
hexagalacturonate + H2O
trigalacturonate
-
-
-
?
homogalacturonan + H2O
oligogalacturonide
-
-
-
-
?
lemon protopectin + H2O
?
-
-
-
-
?
methyl digalacturonoside + H2O
?
-
-
-
-
?
oligogalacturonate + H2O
?
Fomitopsis cytisina
-
-
-
-
?
oligogalacturonic acid + H2O
?
-
affinity of OGHs increase with increasing degree of polymerization of the substrate, but the increase of the maximal rate is stopped by OGH when polymeric substrate is used. Form with pH optimum 4.6 prefers higher oligogalacturonates
-
-
?
oligogalacturonide + H2O
?
-
with a degree of polymerization of 5 and above are hydrolyzed in an endo-fashion and the enzyme appear s to possess 6-7 sugar binding sites in its active site
-
-
?
orange peel pectin + H2O
digalacturonic acid
pectic acid + H2O
galacturonic acid oligomers
pectin + H2O
galacturonic acid + digalacturonic acid + trigalacturonic acid
pectin + H2O
galacturonic acid oligomers
pectin + H2O
oligogalacturonates
-
the enzyme rapidly decreases the viscosity of polygalacturonate and 89% esterified pectin, but the amount of reducing sugars released from polygalacturonic acid is double that of the 89% esterified pectin. Activity on pectin decreases with an increase in degree of esterification
the concentration of oligogalacturonates with degree of polymerization 5 and above is initially high and decreases with time
-
?
pectin + H2O
oligogalacturonides
pentagalacturonate + H2O
trigalacturonate + digalacturonate + tetragalacturonate + galacturonate
-
-
-
?
poly-D-galacturonic acid + H2O
D-galacturonic acid
-
-
-
-
?
polygalacturonate + H2O
?
polygalacturonate + H2O
D-(+)-galacturonate
-
-
-
?
polygalacturonate + H2O
D-galacturonate
-
-
-
-
?
polygalacturonate + H2O
digalacturonic acid
-
71.5% activity compared to apple pectin
-
-
?
polygalacturonate + H2O
galacturonate
polygalacturonate + H2O
oligogalacturonates
polygalacturonate + H2O
oligogalacturonic acid + digalacturonic acid + trigalacturonic acid
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonides
polygalacturonate + H2O
tetragalacturonate + trigalacturonate
polygalacturonate + H2O
trigalacturonate
-
-
-
?
polygalacturonate + H2O
trigalacturonate + digalactuornate + D-galacturonic acid
-
-
-
-
?
polygalacturonic acid + H2O
?
polygalacturonic acid + H2O
D-(+)-galacturonic acid + ?
polygalacturonic acid + H2O
D-galacturonic acid + di-galacturonic acid + tri-galacturonic acid
-
-
-
?
polygalacturonic acid + H2O
digalacturonic acid + galacturonic acid + trigalacturonic acid
polygalacturonic acid + H2O
galacturonic acid
polygalacturonic acid + H2O
galacturonic acid + ?
polygalacturonic acid + H2O
oligogalacturonates
protopectin + H2O
?
-
-
-
-
?
protopectin + H2O
highly polymerized pectin
sodium polypectate + H2O
?
tetragalacturonate + H2O
trigalacturonate + galacturonate
-
-
-
?
trigalacturonate + H2O
?
-
-
-
?
trigalacturonic acid + H2O
?
-
-
-
?
xylan + H2O
?
-
11% activity compared to polygalacturonic acid
-
-
?
xylogalacturonan + H2O
?
-
about 50% of the extracted xylogalacturonan from watermelon fruit cell walls can be converted. All of the oligosaccharides have three unsubstituted GalA residues at their reducing ends
-
-
?
[beta-D-GalA(1-4)]10 + H2O
[beta-D-GalA(1-4)]3-7
-
-
with degree of polymerizations of 3-7
-
?
[beta-D-GalA(1-4)]3 + H2O
?
[beta-D-GalA(1-4)]4 + H2O
?
[beta-D-GalA(1-4)]5 + H2O
?
-
PG1 and PG2
-
-
?
[beta-D-GalA(1-4)]6 + H2O
?
-
is not a good substrate, no complete hydrolysis
-
-
?
additional information
?
-
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
D-galacturonic acid
Acrocylindrium sp.
-
hydrolysis is undetectable
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
D-galacturonic acid
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
D-galacturonic acid
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
D-galacturonic acid
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
D-galacturonic acid
-
at 14% of the activity with polypectate
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
D-galacturonic acid
-
at 14% of the activity with polypectate
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
D-galacturonic acid
Dipodascus klebahnii
-
no activity with digalacturonic acid
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
D-galacturonic acid
Dipodascus klebahnii SNO-3
-
no activity with digalacturonic acid
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
Acrocylindrium sp.
-
hydrolyis is undetectable
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
slight activity
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
52% of the activity with polypectate
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
52% of the activity with polypectate
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
Dipodascus klebahnii
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
Dipodascus klebahnii SNO-3
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
Acrocylindrium sp.
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
-
79% of the activity with polypectate
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
-
79% of the activity with polypectate
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
Dipodascus klebahnii
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
Dipodascus klebahnii SNO-3
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
Acrocylindrium sp.
-
-
or tetragalacturonic acid + galacturonate
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
Dipodascus klebahnii
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
Dipodascus klebahnii SNO-3
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
?
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
apple pectin + H2O
?
-
-
-
?
apple pectin + H2O
?
8% activity compared to polygalacturonate
-
-
?
apple pectin + H2O
?
-
-
-
?
apple pectin + H2O
?
8% activity compared to polygalacturonate
-
-
?
apple pectin + H2O
?
-
47.25% activity compared to polygalacturonate
-
-
?
apple pectin + H2O
?
-
47.25% activity compared to polygalacturonate
-
-
?
apple pectin + H2O
digalacturonic acid
-
100% activity
-
-
?
apple pectin + H2O
digalacturonic acid
-
100% activity
-
-
?
banana peel pectin + H2O
digalacturonic acid
-
25.8% activity compared to apple pectin
-
-
?
banana peel pectin + H2O
digalacturonic acid
-
25.8% activity compared to apple pectin
-
-
?
carrot peel pectin + H2O
digalacturonic acid
-
12.4% activity compared to apple pectin
-
-
?
carrot peel pectin + H2O
digalacturonic acid
-
12.4% activity compared to apple pectin
-
-
?
citrus pectin + H2O
?
-
-
-
-
?
citrus pectin + H2O
?
-
-
-
-
?
citrus pectin + H2O
?
-
-
-
-
?
citrus pectin + H2O
?
20-40% esterified pectin, about 80% activity compared to polygalacturonic acid
-
-
?
citrus pectin + H2O
?
50-70% esterified pectin, about 50% activity compared to polygalacturonic acid
-
-
?
citrus pectin + H2O
?
more than 85% esterified pectin, about 5% activity compared to polygalacturonic acid
-
-
?
citrus pectin + H2O
?
20-40% esterified pectin, about 80% activity compared to polygalacturonic acid
-
-
?
citrus pectin + H2O
?
50-70% esterified pectin, about 50% activity compared to polygalacturonic acid
-
-
?
citrus pectin + H2O
?
more than 85% esterified pectin, about 5% activity compared to polygalacturonic acid
-
-
?
citrus pectin + H2O
?
-
-
-
?
citrus pectin + H2O
?
28.6% activity compared to polygalacturonate
-
-
?
citrus pectin + H2O
?
-
-
-
?
citrus pectin + H2O
?
28.6% activity compared to polygalacturonate
-
-
?
citrus pectin + H2O
?
-
28% esterified citrus pectin is hydrolyzed with 52.5% activity compared to polygalacturonate, 75% esterified citrus pectin is hydrolyzed with 29.75% activity compared to polygalacturonate, and 90% esterified citrus pectin is hydrolyzed with 17.5% activity compared to polygalacturonate
-
-
?
citrus pectin + H2O
?
-
28% esterified citrus pectin is hydrolyzed with 52.5% activity compared to polygalacturonate, 75% esterified citrus pectin is hydrolyzed with 29.75% activity compared to polygalacturonate, and 90% esterified citrus pectin is hydrolyzed with 17.5% activity compared to polygalacturonate
-
-
?
citrus pectin + H2O
D-(+)-galacturonic acid + ?
-
25% activity with 6-7% esterified pectin and 22% activity with 55-70% esterified pectin, compared to polygalacturonate
-
-
?
citrus pectin + H2O
D-(+)-galacturonic acid + ?
-
25% activity with 6-7% esterified pectin and 22% activity with 55-70% esterified pectin, compared to polygalacturonate
-
-
?
citrus peel pectin + H2O
digalacturonic acid
-
85.2% activity compared to apple pectin
-
-
?
citrus peel pectin + H2O
digalacturonic acid
-
85.2% activity compared to apple pectin
-
-
?
dextrose agar + H2O
?
-
potato dextrose agar, low activity
-
-
?
dextrose agar + H2O
?
-
potato dextrose agar, low activity
-
-
?
dextrose agar + H2O
?
-
potato dextrose agar
-
-
?
dextrose agar + H2O
?
-
potato dextrose agar
-
-
?
orange peel pectin + H2O
digalacturonic acid
-
16.2% activity compared to apple pectin
-
-
?
orange peel pectin + H2O
digalacturonic acid
-
16.2% activity compared to apple pectin
-
-
?
pectate + H2O
?
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
-
-
?
pectate + H2O
?
-
-
-
-
?
pectate + H2O
?
-
-
-
-
?
pectate + H2O
?
-
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
-
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
-
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
-
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
Bacillus sp. (in: Bacteria) No. P-4-N
-
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
-
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
-
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
Saccharomyces fragilis
-
-
-
?
pectin + H2O
?
citrus pectin
-
-
?
pectin + H2O
?
citrus pectin
-
-
?
pectin + H2O
?
-
citrus pectin, hydrolysis decreases with increasing of degrees of esterification
-
-
?
pectin + H2O
?
-
citrus pectin, hydrolysis decreases with increasing of degrees of esterification
-
-
?
pectin + H2O
?
-
highly esterified
-
-
?
pectin + H2O
?
-
mango peel pectin
-
-
?
pectin + H2O
?
-
mango peel pectin
-
-
?
pectin + H2O
?
endopolygalacturonases hydrolyse the 1-4 linkages between two alpha-D-galacturonic acids of the smooth homogalacturonan regions of pectin
-
-
?
pectin + H2O
?
endopolygalacturonases hydrolyse the 1-4 linkages between two alpha-D-galacturonic acids of the smooth homogalacturonan regions of pectin. Isozyme PGI is not only the most potent but also the most tolerant enzyme to hydrolyse acetylated pectin
-
-
?
pectin + H2O
?
-
citrus or apple pectin
-
-
?
pectin + H2O
?
-
citrus or apple pectin
-
-
?
pectin + H2O
?
-
citrus or apple pectin
-
-
?
pectin + H2O
?
-
citrus pectin
-
-
?
pectin + H2O
?
-
citrus pectin
-
-
?
pectin + H2O
?
P19805
coffee pectin
-
-
?
pectin + H2O
?
P19805
coffee pectin agar plate containing 2% crude pectin from coffee mucilage
-
-
?
pectin + H2O
?
-
citrus pectin with degree of esterification of 63-66%, bad substrate for PG1 and PG2. Apple pectin with degree of esterification of 70-75%, bad substrate for PG1 and PG2
-
-
?
pectin + H2O
?
-
citrus pectin with degree of esterification of 63-66%, bad substrate for PG1 and PG2. Apple pectin with degree of esterification of 70-75%, bad substrate for PG1 and PG2
-
-
?
pectin + H2O
?
-
high activity
-
-
?
pectin + H2O
?
-
high activity
-
-
?
pectin + H2O
?
endopolygalacturonases hydrolyse the 1-4 linkages between two alpha-D-galacturonic acids of the smooth homogalacturonan regions of pectin
-
-
?
pectin + H2O
?
-
the enzyme hydrolyses the linkages between two galacturonic acid residues according to a multi-chain mechanism, at least at the early stage of the reaction. The enzyme is able to accomodate methylated galacturonic acid in its active site, but the methyl-esterification negatively affects the affinity of the enzyme
-
-
?
pectin + H2O
?
-
apple pectin, 75% degree of esterification
-
-
?
pectin + H2O
?
-
apple pectin, 75% degree of esterification
-
-
?
pectin + H2O
?
-
citrus pectin
-
-
?
pectin + H2O
?
-
citrus pectin
-
-
?
pectin + H2O
?
-
citrus pectin
-
-
?
pectin + H2O
?
-
citrus pectin
-
-
?
pectin + H2O
?
-
highly esterified
-
-
?
pectin + H2O
?
-
57% activity compared to polygalacturonic acid
-
-
?
pectin + H2O
?
-
highly esterified
-
-
?
pectin + H2O
?
-
apple pectin
-
-
?
pectin + H2O
?
-
citrus or apple pectin, highest enzyme activity with citrus pectin
-
-
?
pectin + H2O
?
-
citrus pectin with 26% and 92% degree of esterification, and apple pectin
-
-
?
pectin + H2O
?
-
citrus pectin with 26% and 92% degree of esterification, and apple pectin
-
-
?
pectin + H2O
?
-
citrus or apple pectin, highest enzyme activity with citrus pectin
-
-
?
pectin + H2O
?
-
citrus pectin, apple pectin and amylopectin, hydrolysis of different pectins is decreased with increasing of degree of esterification
-
-
?
pectin + H2O
?
-
citrus pectin, apple pectin and amylopectin, hydrolysis of different pectins is decreased with increasing of degree of esterification
-
-
?
pectin + H2O
galacturonic acid + digalacturonic acid + trigalacturonic acid
-
-
-
?
pectin + H2O
galacturonic acid + digalacturonic acid + trigalacturonic acid
-
-
-
?
pectin + H2O
galacturonic acid oligomers
-
-
-
-
?
pectin + H2O
galacturonic acid oligomers
-
-
-
-
?
pectin + H2O
oligogalacturonides
-
-
-
-
?
pectin + H2O
oligogalacturonides
-
optimum activities at 0.2% pectin
-
-
?
pectin + H2O
oligogalacturonides
-
pectin from citrus or Palicourea marcgravii, more active upon pectic substrates with a low degree of methyl esterification. The enzyme itself and the products of its action on the pectic fraction of Palicourea marcgravii elicite the production of defensive compounds in the leaves of the plant
-
-
?
pectin + H2O
oligogalacturonides
-
pectin from citrus or Palicourea marcgravii, more active upon pectic substrates with a low degree of methyl esterification. The enzyme itself and the products of its action on the pectic fraction of Palicourea marcgravii elicite the production of defensive compounds in the leaves of the plant
-
-
?
pectin + H2O
oligogalacturonides
-
optimum activities at 0.2% pectin
-
-
?
pectin + H2O
oligogalacturonides
-
-
-
-
?
pectin + H2O
oligogalacturonides
-
the two enzymes PG1 and PG2 have higher affinity towards polygalacturonate derived from sugar beet pectin than polygalacturonate derived from lime pectin. Enzymatic activity decreases with increased degree of methylation of lime pectins
-
-
?
polygalacturonan + H2O
?
-
-
-
-
?
polygalacturonan + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
is a non-processive enzyme that releases oligomers with chain lengths ranging from two to eight
-
-
?
polygalacturonate + H2O
?
Fomitopsis cytisina
-
-
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
influence of esterification degree of the substrate
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
influence of esterification degree of the substrate
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
-
-
-
?
polygalacturonate + H2O
?
-
amounts of monomer and small oligomers increase with increasing incubation times, the amount of larger oligomers decreases due to further degradation
-
-
?
polygalacturonate + H2O
galacturonate
-
-
-
-
?
polygalacturonate + H2O
galacturonate
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
Acrocylindrium sp.
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
oligouronides
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
100% activity
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
100% activity
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
higher galacturonides progressively disappear with reaction time, and monogalacturonic acid, digalacturonic acid and trigalacturonic acids remain as the end products of the hydrolysis
?
polygalacturonate + H2O
oligogalacturonates
-
-
114100, 135794, 135797, 135820, 135824, 135827, 135836, 135838, 135843, 135851, 135854 -
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
polygalacturonate is not the optimal substrate
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
liberation of digalacturonic acid, trigalacturonic acid and tetragalacturonic acid after 10 min. After 2 h, tetragalacturonic acid disappears with concomitant accumulation of galacturonate
?
polygalacturonate + H2O
oligogalacturonates
Bacillus sp. (in: Bacteria) No. P-4-N
-
-
liberation of digalacturonic acid, trigalacturonic acid and tetragalacturonic acid after 10 min. After 2 h, tetragalacturonic acid disappears with concomitant accumulation of galacturonate
?
polygalacturonate + H2O
oligogalacturonates
Bacterium aroideae
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
Dipodascus klebahnii
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
Dipodascus klebahnii SNO-3
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
the enzyme rapidly decreases the viscosity of polygalacturonate and 89% esterified pectin, but the amount of reducing sugars released from polygalacturonic acid is double that of the 89% esterified pectin
the concentration of oligogalacturonates with degree of polymerization 5 and above is initially high and decreases with time
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
highest activity
-
-
?
polygalacturonate + H2O
oligogalacturonates
100% activity
-
-
?
polygalacturonate + H2O
oligogalacturonates
highest activity
-
-
?
polygalacturonate + H2O
oligogalacturonates
100% activity
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
the enzyme exhibits endo- and exo-activity
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
nonmethoxylated polygalacturonic acid
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
Saccharomyces fragilis
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
Tetracoccosporium sp.
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonides
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonides
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonides
-
the two enzymes PG1 and PG2 have higher affinity towards polygalacturonate derived from sugar beet pectin than polygalacturonate derived from lime pectin
-
-
?
polygalacturonate + H2O
tetragalacturonate + trigalacturonate
-
very high specific activity (100% activity)
-
-
?
polygalacturonate + H2O
tetragalacturonate + trigalacturonate
-
very high specific activity (100% activity)
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
PG1 and PG2
-
-
?
polygalacturonic acid + H2O
?
-
PG1 and PG2
-
-
?
polygalacturonic acid + H2O
?
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
random hydrolysis of the alpha-1,4 glycosidic linkages
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
best substrate
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
?
-
-
-
-
?
polygalacturonic acid + H2O
D-(+)-galacturonic acid + ?
100% activity
-
-
?
polygalacturonic acid + H2O
D-(+)-galacturonic acid + ?
100% activity
-
-
?
polygalacturonic acid + H2O
digalacturonic acid + galacturonic acid + trigalacturonic acid
-
-
-
?
polygalacturonic acid + H2O
digalacturonic acid + galacturonic acid + trigalacturonic acid
-
-
-
?
polygalacturonic acid + H2O
galacturonic acid
-
-
-
-
?
polygalacturonic acid + H2O
galacturonic acid
-
-
-
-
?
polygalacturonic acid + H2O
galacturonic acid
-
best substrate
-
-
?
polygalacturonic acid + H2O
galacturonic acid
-
best substrate
-
-
?
polygalacturonic acid + H2O
galacturonic acid
Tetracoccosporium sp.
-
-
-
-
?
polygalacturonic acid + H2O
galacturonic acid + ?
-
-
-
?
polygalacturonic acid + H2O
galacturonic acid + ?
-
-
-
?
polygalacturonic acid + H2O
galacturonic acid + ?
-
-
-
?
polygalacturonic acid + H2O
galacturonic acid + ?
-
-
-
?
polygalacturonic acid + H2O
oligogalacturonates
-
-
oligosaccharides with various polymerization degrees between 1 and 4
-
?
polygalacturonic acid + H2O
oligogalacturonates
-
-
oligosaccharides with various polymerization degrees between 1 and 4
-
?
polygalacturonic acid + H2O
oligogalacturonates
-
-
-
?
polygalacturonic acid + H2O
oligogalacturonates
-
endo-PGs generate mixtures of oligogalacturonates, with oligogalacturonates of relatively high degree of polymerization produced early in the reaction and smaller oligogalacturonates accumulating later in the reaction as the endo-PG acts on the first oligogalacturonate products of higher degree of polymerization
-
-
?
polypectate + H2O
?
-
oligogalacturonides gradually disappear with the reaction time, so that monogalacturonic acid remains as the only product of the hydrolysis
-
-
?
polypectate + H2O
?
-
oligogalacturonides gradually disappear with the reaction time, so that monogalacturonic acid remains as the only product of the hydrolysis
-
-
?
polyuronide + H2O
?
-
polygalacturonase, EC 3.2.1.15 and pectinmethylesterase, EC 3.2.1.11 operate in tandem to degrade methylesterified polyuronides
-
-
?
polyuronide + H2O
?
-
high molecular mass, low methylesterified, 33%, water-soluble polyuronides from pre-ripe avocado-fruit are partially depolymerized. In contrast, middle molecular mass, highly methylesterified, 74% water-soluble polyuronides from day 2 fruit are largely resistant to the action of the enzyme. Treatment of de-esterified water-soluble polyuronides with the enzyme causes extensive molecular mass downshifts
-
-
?
polyuronide + H2O
?
-
polygalacturonase, EC 3.2.1.15 and pectinmethylesterase, EC 3.2.1.11 operate in tandem to degrade methylesterified polyuronides
-
-
?
polyuronide + H2O
?
-
high molecular mass, low methylesterified, 33%, water-soluble polyuronides from pre-ripe avocado-fruit are partially depolymerized. In contrast, middle molecular mass, highly methylesterified, 74% water-soluble polyuronides from day 2 fruit are largely resistant to the action of the enzyme. Treatment of de-esterified water-soluble polyuronides with the enzyme causes extensive molecular mass downshifts
-
-
?
protopectin + H2O
highly polymerized pectin
Dipodascus klebahnii
-
-
-
-
?
protopectin + H2O
highly polymerized pectin
Dipodascus klebahnii SNO-3
-
-
-
-
?
protopectin + H2O
highly polymerized pectin
Saccharomyces fragilis
-
-
-
?
sodium polypectate + H2O
?
-
-
-
-
?
sodium polypectate + H2O
?
-
-
-
-
?
[beta-D-GalA(1-4)]3 + H2O
?
-
PG1 and PG2
-
-
?
[beta-D-GalA(1-4)]3 + H2O
?
-
PG1 and PG2
-
-
?
[beta-D-GalA(1-4)]4 + H2O
?
-
only cleaved by PG1 and PG2 when trigalacturonic acid is present
-
-
?
[beta-D-GalA(1-4)]4 + H2O
?
-
only cleaved by PG1 and PG2 when trigalacturonic acid is present
-
-
?
additional information
?
-
endo-PG I is a polygalacturonase of endo-type
-
-
?
additional information
?
-
endo-PG I is a polygalacturonase of endo-type
-
-
?
additional information
?
-
-
the enzyme shows no non-specific hydrolysis activity against Avicel, soluble starch or carboxymethyl cellulose
-
-
?
additional information
?
-
-
the enzyme shows no non-specific hydrolysis activity against Avicel, soluble starch or carboxymethyl cellulose
-
-
?
additional information
?
-
-
cellulase-free rohament shows only macerating activity and releases cells continously without liquefaction, irrespective of the incubation period or enzyme concentration, cell walls are intact for extended periods up to 24-30 h of incubation
-
-
?
additional information
?
-
-
no activity with glucose, sugarcane bagasse, oat bran and wheat bran
-
-
?
additional information
?
-
-
no activity with glucose, sugarcane bagasse, oat bran and wheat bran
-
-
?
additional information
?
-
-
maceration of plant tissues
-
-
?
additional information
?
-
-
the enzyme is very efficient to extract pectin from lemmon protopectin and to macerate carrot tissues at pH 2.0
-
-
?
additional information
?
-
-
both N- and O-glycosylated. Recombinant PGC is modified by N-linked glycans. Asn220 is the site of glycosylation. Monosaccharide in PGC is entirely mannose
-
-
?
additional information
?
-
-
N- and O-glycosylated. N-linked glycosylation at Asn214, but O-linked glycosylation at any serine or threonine residue. N-linked glycan attached at PGA Asn214 contains a high-mannose structure of GlcNAc2Man4-9
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolytic cleavage of the polygalacturonic acid chain
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolytic cleavage of the polygalacturonic acid chain
-
-
?
additional information
?
-
-
wheat bran or wheat bran/orange bagasse mixture, endo-Pg production is highest in wheat bran/orange bagasse mixture
-
-
?
additional information
?
-
-
wheat bran or wheat bran/orange bagasse mixture, endo-Pg production is highest in wheat bran/orange bagasse mixture
-
-
?
additional information
?
-
-
the enzyme is produced inducibly in a medium containing D-galacturonic acid or pectin
-
-
?
additional information
?
-
-
no activity of PG1 and PG2 towards xylan, carboxymethylcellulose and mannan
-
-
?
additional information
?
-
-
no activity of PG1 and PG2 towards xylan, carboxymethylcellulose and mannan
-
-
?
additional information
?
-
-
the enzyme has low protopectinase activity
-
-
?
additional information
?
-
-
enzyme is involved in host penetration by the fungus
-
-
?
additional information
?
-
-
the enzyme is involved in the rotting and maceration of fresh fruit and vegetables
-
-
?
additional information
?
-
-
the enzyme is involved in the rotting and maceration of fresh fruit and vegetables
-
-
?
additional information
?
-
-
the enzyme is a factor inducing silver-leaf symptoms on apple trees
-
-
?
additional information
?
-
-
maceration of potato medullary tissue disks
-
-
?
additional information
?
-
-
no activity with alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
-
-
?
additional information
?
-
-
O2 and galacturonate negatively regulate enzyme synthesis, and glucose as carbon source affords better enzyme yield than lactose
-
-
?
additional information
?
-
-
O2 and galacturonate negatively regulate enzyme synthesis, and glucose as carbon source affords better enzyme yield than lactose
-
-
?
additional information
?
-
-
wheat bran or wheat bran/orange bagasse mixture, endo-Pg production is higher in wheat bran/orange bagasse mixture
-
-
?
additional information
?
-
-
wheat bran or wheat bran/orange bagasse mixture, endo-Pg production is higher in wheat bran/orange bagasse mixture
-
-
?
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
?
-
no activity with carboxymethyl cellulose and xylan
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose and xylan
-
-
?
additional information
?
-
no activity with carboxymethyl cellulose and xylan
-
-
?
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
?
-
the purified recombinant endo-PGA1 exhibits highest activity on substrate polygalacturonic acid, followed by pectins with different levels of esterification. Endo-PG I exhibits 77.5%, 19.4%, and 9% of the relative activity towards pectins of 34%, 70%, and 85% esterified, respectively
-
-
?
additional information
?
-
-
isozyme specific PG activity in wild-type and non-virulent phenotype conversion mutant and cleavage mode, overview
-
-
?
additional information
?
-
-
isozyme specific PG activity in wild-type and non-virulent phenotype conversion mutant and cleavage mode, overview
-
-
?
additional information
?
-
-
enzyme degrades pectic substances in orange peel
-
-
?
additional information
?
-
Saccharomyces fragilis
-
macerating activity towards potato and carrot tissues
-
-
?
additional information
?
-
-
the enzyme plays a key role in early stages of infection in head and basal rot, diseases which destroy sunflower
-
-
?
additional information
?
-
-
together with other pectinolytic enzymes the polygalacturonase is involved in the degradation of pectin
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the purified enzyme is an endo/exo-enzyme, releasing mono, di- and tri-galacturonic acids within 10 min of hydrolysis
-
-
?
additional information
?
-
-
polygalacturonase is an endo/exoenzyme, cf. EC 3.2.1.67
-
-
?
additional information
?
-
-
polygalacturonase is an endo/exoenzyme, cf. EC 3.2.1.67
-
-
?
additional information
?
-
-
the purified enzyme is an endo/exo-enzyme, releasing mono, di- and tri-galacturonic acids within 10 min of hydrolysis
-
-
?
additional information
?
-
-
very low activity toward non-pectic polysaccharides
-
-
?
additional information
?
-
-
very low activity toward non-pectic polysaccharides
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
inducible enzyme
-
-
?
additional information
?
-
-
the purified enzyme is able to macerate cassava tissues
-
-
?
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1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
-
50 mM, 70% inhibition
2,3-Butanedione
-
10 mM, 90% inhibition
2-Hydroxy-5-nitrobenzylbromide
-
10 mM, complete inhibition
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
Dipodascus klebahnii
-
inhibition of pectic acid liquefying activity, no inhibition of protopectinase activity
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
Dipodascus klebahnii
-
inhibition of pectic acid liquefying activity, no inhibition of protopectinase activity
antisense RNA
-
inhibits BcMF2 expression, which results in abnormal pollen tube growth and consequent reduction in male fertility. BcMF2 inhibition leads to pollen deformities with abnormal intine development and in early degradation of the anther tapetum
-
apple polygalacturonase inhibiting protein 1
-
auxin
-
either in tobacco PG or wild-type plants treated with oligogalacturonides, resistance to fungal infection is suppressed by exogenous auxin, whereas sensitivity to auxin of PG plants is reduced in different bioassays. Altered auxin sensitivity in PG plants may be due to an increased accumulation of oligogalacturonides and subsequent antagonism of auxin action
CaCl2
-
probably by calcium chelation of polygalacturonic acid
cetyltrimethylammonium bromide
-
67% inhibition at 0.5%
CHAPS
-
76.1% residual activity at 0.25% (v/v)
Citric acid
-
64% inhibition at 5 mM
diethyldicarbonate
P19805
-
Digalacturonate
competitive inhibition
EGTA
-
76.4% residual activity at 2 mM
gluconic acid delta-lactone
-
compeptitive
iodoacetamide
-
1 mM, 20% inhibition
Mersalyl acid
Dipodascus klebahnii
-
-
NaCl
-
0.3 M, complete inactivation
Ni(2+)
-
reduces activity by 50%
p-nitrophenylglyoxal
-
5 mM, complete inhibition
Phenylglyoxal
-
5 mM, complete inhibition
PMSF
-
78% inhibition at 5 mM
polygalacturonase-inhibiting protein
-
polygalacturonase-inhibiting protein 1
coinfiltration of Vitis vinifera polygalacturonase-inhibiting protein 1 and PG2 results in a substantial reduction of the symptoms inflicted by the activity of PG2 in planta. In vitro, the inhibitor neither inhibits PG2 activity nor alters the degradation profile of polygalacturonic acid by PG2 and does not physically interact with PG2
-
polygalacturonase-inhibiting protein 1 of Chorispora bungeana
-
-
-
polygalacturonase-inhibiting protein 2
-
polygalacturonase-inhibiting proteins
-
from Solanum lycopersicum stem cell wall extract, comparison of inhibition of polygalacturonases of wild-type and non-virulent phenotype conversion mutant strains of Ralstonia solanacearum by polygalacturonase-inhibiting proteins, PGIPs, from tomato stems. Polygalacturonase activity of the phenotype conversion mutant strain increases about 5 h earlier than the wild-type, and is up to 35 times higher in media supplemented with two different tomato stem extracts or polygalacturonic acid, compared to the wild-type, and generally 4-8 times higher across test media and time
-
polygalacturonic acid
-
substrate inhibition above 5 mg/ml
polypectate
-
substrate inhibition at high concentrations
potassium ferrocyanide
-
64.2% residual activity at 1 mM
Teepol
-
43% inhibition at 0.5%
-
Tris
Saccharomyces fragilis
-
-
Tween 80
-
slight inhibition
2,4-dinitrophenol
-
-
2-mercaptoethanol
P19805
-
2-mercaptoethanol
-
slight inhibition
2-mercaptoethanol
-
67.5% residual activity at 10 mM
Ag+
over 50% inhibition
Ag+
-
34% residual activity at 1 mM
Ag+
Dipodascus klebahnii
-
-
Ag+
Saccharomyces fragilis
-
-
Ag+
-
56.6% residual activity with 1mM
Al3+
-
-
Al3+
P19805
82% inhibition
Al3+
Tetracoccosporium sp.
-
-
apple polygalacturonase inhibiting protein 1
-
expressed in transgenic tobacco inhibits polygalacturonase
-
apple polygalacturonase inhibiting protein 1
-
expressed in transgenic tobacco inhibits polygalacturonases
-
apple polygalacturonase inhibiting protein 1
-
expressed in transgenic tobacco inhibits polygalacturonases
-
Ba2+
about 92% residual activity at 1 mM
Ba2+
-
91.8% residual activity at 5 mM
Ba2+
-
12% inhibition at 0.5 mM
Ba2+
-
complete inhibition at 2 mM
Ba2+
-
62.87% residual activity at 10 mM
Ba2+
-
1 mM, 25% inhibition
Ba2+
Saccharomyces fragilis
-
-
Ba2+
Tetracoccosporium sp.
-
-
Ba2+
-
96.3% residual activity with 1mM
Ca2+
over 50% inhibition
Ca2+
-
29.5% residual activity at 1 mM
Ca2+
-
strongly inhibits PG1 and PG2
Ca2+
Dipodascus klebahnii
-
-
Ca2+
-
85.1% residual activity at 1 mM
Ca2+
71.7% residual activity at 2 mM
Ca2+
strong inhibition at 5 mM
Ca2+
-
64.9% residual activity at 2 mM
Ca2+
-
71.37% residual activity at 10 mM
Ca2+
Saccharomyces fragilis
-
-
Ca2+
Tetracoccosporium sp.
-
-
Ca2+
-
66.7% residual activity with 1mM
Cd2+
-
98% inhibition at 0.5 mM
Cd2+
-
5 mM, complete inhibition
Co2+
about 75% residual activity at 1 mM
Co2+
P19805
82% inhibition
Co2+
-
98.4% residual activity at 5 mM
Co2+
Dipodascus klebahnii
-
-
Co2+
70.6% residual activity at 2 mM
Co2+
-
0.31% residual activity at 2 mM
Co2+
-
1mM completely inhibits
Cr3+
below 40% inhibition
Cr3+
-
stronger inhibitor for PG2 than for PG1
Cr3+
strong inhibition at 5 mM
Cu2+
below 40% inhibition
Cu2+
-
78% of activity reduction
Cu2+
P19805
strong inhibition of 90%
Cu2+
-
23% inhibition at 0.5 mM
Cu2+
19.7% residual activity at 2 mM
Cu2+
10.3% residual activity at 2 mM
Cu2+
strong inhibition at 5 mM
Cu2+
-
2.48% residual activity at 2 mM
Cu2+
-
complete inhibition at 10 mM
Cu2+
-
83.6% residual activity with 1mM
diethyl dicarbonate
-
at pH 6, only enzyme form E2 is protected from inhibition by 2% w/v polygalacturonate
diethyl dicarbonate
-
5 mM, complete inhibition
diethyl dicarbonate
-
complete inhibition at 0.1% (w/v)
EDTA
below 40% inhibition
EDTA
-
85.7% residual activity at 1 mM
EDTA
-
55.7% residual activity at 2 mM
EDTA
-
10 mM, complete inactivation
EDTA
-
50% inhibition at 10 mM
EDTA
-
80% residual activity at 2 mM
EDTA
-
2 mM inhibits 25% of enzyme activity
Fe2+
-
-
Fe2+
-
18% inhibition at 0.5 mM
Fe2+
91% residual activity at 2 mM
Fe2+
-
16.45% residual activity at 2 mM
Fe2+
-
84.63% residual activity at 10 mM
Fe2+
Tetracoccosporium sp.
-
-
Fe3+
-
stronger inhibitor for PG1 than for PG2
Fe3+
strong inhibition at 5 mM
Fe3+
Tetracoccosporium sp.
-
-
Fe3+
-
93.2% residual activity with 1mM
galacturonate
Dipodascus klebahnii
-
inhibition of pectic acid liquefying activity, no inhibition of protopectinase activity
Hg+
Dipodascus klebahnii
-
-
Hg+
Saccharomyces fragilis
-
-
Hg2+
-
90.5% of activity reduction
Hg2+
-
64.2% residual activity at 1 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
P19805
complete inhibition
Hg2+
-
stronger inhibitor for PG1 than for PG2
Hg2+
-
96% inhibition at 0.5 mM
Hg2+
-
0.5 mM, complete inhibition
Hg2+
Dipodascus klebahnii
-
-
Hg2+
-
complete inhibition at 10 mM
Hg2+
-
1 mM, 87% inhibition
Hg2+
Saccharomyces fragilis
-
-
Hg2+
Saccharomyces fragilis
-
HgCl2
Hg2+
-
2 mM inhibits 100% of enzyme activity
Hg2+
-
complete inhibition
Hg2+
-
46.3% residual activity with 1mM
Hg2+
-
complete inhibition at 1 mM
iodoacetic acid
P19805
-
iodoacetic acid
-
74% inhibition at 5 mM
K+
-
-
K+
-
87.5% residual activity at 2 mM
K+
-
activity level of 94.7% at 1 mM
Li+
-
-
Li+
-
83.6% residual activity with 1mM
Li+
-
activity level of 89.5% at 1 mM
Mg2+
below 40% inhibition
Mg2+
-
reduces activity by 50%
Mg2+
P19805
40% inhibition
Mg2+
-
85.3% residual activity at 5 mM
Mg2+
96.5% residual activity at 2 mM
Mg2+
-
61.24% residual activity at 10 mM
Mg2+
Tetracoccosporium sp.
-
-
Mg2+
-
2 mM inhibits 7% of enzyme activity
Mg2+
-
76.4% residual activity with 1mM
Mn2+
-
73.76% residual activity at 1 mM
Mn2+
about 55% residual activity at 1 mM
Mn2+
-
87.3% residual activity at 1 mM
Mn2+
56.9% residual activity at 2 mM
Mn2+
40.4% residual activity at 2 mM
Mn2+
-
complete inhibition at 1 mM
Mn2+
-
complete inhibition at 10 mM
Mn2+
-
1 mM, 21% inhibition
Mn2+
Saccharomyces fragilis
-
MnCl2
Mn2+
Tetracoccosporium sp.
-
-
Mn2+
-
2 mM inhibits 75% of enzyme activity
Mn2+
-
1mM completely inhibits
N-bromosuccinimide
P19805
strong inhibition of 98%
N-bromosuccinimide
-
1 mM, complete inhibition
Na+
-
90.88% residual activity at 1 mM
Na+
-
84.4% residual activity at 2 mM
Na+
-
93.5% residual activity at 10 mM
Ni2+
about 82% residual activity at 1 mM
Ni2+
-
91.5% residual activity at 5 mM
Ni2+
Tetracoccosporium sp.
-
-
Ni2+
-
89.9% residual activity with 1mM
p-chloromercuribenzoate
P19805
-
p-chloromercuribenzoate
-
80% inhibition at 0.1 mM, 94% at 0.5 mM
Pb2+
about 38% residual activity at 1 mM
Pb2+
-
97% inhibition at 0.5 mM
Pb2+
-
5 mM, complete inhibition
Pb2+
strong inhibition at 5 mM
Pb2+
Saccharomyces fragilis
-
-
PCMB
-
0.1 M, complete inactivation
PCMB
Dipodascus klebahnii
-
-
PCMB
-
45% inhibition by 0.1 mM, 65% inhibition by 0.5 mM. Inhibition can be reversed by DTT
PCMB
Saccharomyces fragilis
-
-
polygalacturonase-inhibiting protein
-
from Phaseolus vulgaris, purification of the inhibitor from hypocotyl
-
polygalacturonase-inhibiting protein
-
crystallographic analysis of the inhibitor
-
polygalacturonase-inhibiting protein
-
from bean, pear and tomato
-
polygalacturonase-inhibiting protein
-
from Phaseolus vulgaris, purification of the inhibitor from hypocotyl
-
polygalacturonase-inhibiting protein
-
from tomato
-
polygalacturonase-inhibiting protein
-
from Phaseolus vulgaris, purification of the inhibitor from hypocotyl
-
polygalacturonase-inhibiting protein
-
-
-
polygalacturonase-inhibiting protein 2
-
PGIP2, from Phaseolus vulgaris pv. Pinto, recombinantly expressed in Pichia pastoris X33, forms a complex with the enzyme from Colletotrichum lupini hindering substrate binding in the enzyme active site cleft, small angle X-ray scattering interaction analysis, and inhibition kinetics, overview
-
polygalacturonase-inhibiting protein 2
-
PGIP2, from Phaseolus vulgaris pv. Pinto, recombinantly expressed in Pichia pastoris X33, forms a complex with the enzyme from Fusarium phyllophilum hindering substrate binding in the enzyme active site cleft, residue A274 plays a key role in the interaction, small angle X-ray scattering interaction analysis, and inhibition kinetics, overview. Residue Q224 of the inhibitor is crucial for the interaction with the enzyme. Inhibitor mutant PvPGIP2.Q224K variant is unable to inhibit the enzyme, while inhibitor mutant PvPGIP2.Q224K retains unaltered inhibitory capability towards the enzyme
-
protein PPGIP2
-
polygalacturonase-inhibiting protein 2 from Phaseolus vulgaris, is an efficient inhibitor of fungal polygalacturonases. Overall sequence conservation of PGIP2 and minor variation at specific sites is necessary for high-affinity recognition of different fungal polygalacturonases
-
protein PPGIP2
-
polygalacturonase-inhibiting protein 2 from Phaseolus vulgaris, is an efficient inhibitor of fungal polygalacturonases. Overall sequence conservation of PGIP2 and minor variation at specific sites is necessary for high-affinity recognition of different fungal polygalacturonases
-
protein PPGIP2
-
polygalacturonase-inhibiting protein 2 from Phaseolus vulgaris, is an efficient inhibitor of fungal polygalacturonases. Overall sequence conservation of PGIP2 and minor variation at specific sites is necessary for high-affinity recognition of different fungal polygalacturonases
-
protein PPGIP2
-
polygalacturonase-inhibiting protein 2 from Phaseolus vulgaris, is an efficient inhibitor of fungal polygalacturonases. Overall sequence conservation of PGIP2 and minor variation at specific sites is necessary for high-affinity recognition of different fungal polygalacturonases
-
SDS
P19805
-
SDS
-
stronger inhibitor for PG1 than for PG2
SDS
30.2% residual activity at 20 mM
SDS
strong inhibition at 5 mM
SDS
-
70.4% residual activity at 0.5% (w/v)
SDS
-
complete inhibition at 5 mM
SDS
Tetracoccosporium sp.
-
-
Triton X-100
-
10% inhibition at 0.5%
Triton X-100
-
at 0.1-10%
Triton X-100
-
slight inhibition
Urea
-
8 M, complete inactivation
Zn2+
-
88.81% residual activity at 1 mM
Zn2+
P19805
47% inhibition
Zn2+
77.4% residual activity at 2 mM
Zn2+
strong inhibition at 5 mM
Zn2+
-
80.9% residual activity at 5 mM
Zn2+
-
2 mM inhibits 50% of enzyme activity
Zn2+
-
81.7% residual activity with 1mM
additional information
-
no considerable effect with Li+, Fe2+ and Rb2+
-
additional information
-
EDTA has no significant effect on the enzyme activity
-
additional information
-
KMnO4 has no effect on enzyme activity
-
additional information
-
apple fruit extract inhibits enzyme activity, enzyme expressed in transgenic tobacco and purified is not inhibited by apple polygalacturonase inhibiting protein 1
-
additional information
-
the resistant phenotype is not exhibited by transgenic tobacco plants expressing both PG and its inhibitor PvPGIP2 or by Arabidopsis plants expressing a mutagenized and inactive AnPGII (PG201)
-
additional information
-
inhibitory potency in descending order cinnamic acid, ferulic acid, p-coumaric acid, salicylic acid, and chlorgenic acid
-
additional information
-
not affected by 2-mercaptoethanol, 15% (v/v) ethanol or 100 mg/l SO2
-
additional information
-
EDTA and surfactants have no influence on enzyme activity
-
additional information
-
increased resistance of tobacco polygalacturonase plants is abolished by auxin
-
additional information
-
9 ng Phaseolus vulgaris PGIP2 determines 50% inhibition of 1 agarose diffusion unit of polygalacturonase at pH 4.7
-
additional information
-
inability of the enzyme from Fusarium phyllophilum to be inhibited by polygalacturonase-inhibiting protein 2, PGIP2, from Phaseolus vulgaris pv. Pinto and recombinatly expressed in Pichia pastoris X33, or any other polygalacturonase-inhibiting protein, small angle X-ray scattering interaction analysis of structural basis, overview
-
additional information
expression level is declined rapidly in senesced petals after flowering. At low temperature, expression is gradually decreased to very low level in petals
-
additional information
-
expression level is declined rapidly in senesced petals after flowering. At low temperature, expression is gradually decreased to very low level in petals
-
additional information
not inhibited by Tween-20, Tween-80, and Triton X-100
-
additional information
-
not inhibited by Tween-20, Tween-80, and Triton X-100
-
additional information
-
iodoacetamide, iodoacetate, dithiothreitol, 2-mercaptoethanol and Triton-X100 have no significant effect on enzyme activity
-
additional information
-
not affected by K+
-
additional information
-
PG1 and PG2 can be inactivated at room temperature in the pressure range of 300-500 MPa
-
additional information
-
reduction of the PG activity under pulsed electric fields (up to 76.5% at E = 38 kV cm-1 and t = 1100 micros)
-
additional information
Tetracoccosporium sp.
-
not inhibited by iodoacetamide and iodoacetic acid at a concentration of 1 mM
-
additional information
-
1,10-phenanthroline, Tween 20, Tween 80, Triton X-100 and SDS have no effect on enzyme activity
-
additional information
-
expression of pehA is subject to catabolite repression, which is independent of Clp and RpfF, and it is repressed under conditions of oxygen limitation or nitrogen starvation
-
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Acquired Immunodeficiency Syndrome
Isolation of Polygalacturonase-Producing Bacterial Strain from Tomatoes (Lycopersicon esculentum Mill.).
Adenocarcinoma
Gastric phenotypic expression in human gallbladder cancers revealed by pepsinogen immunohistochemistry and mucin histochemistry.
Adenocarcinoma
The histologic detection of Helicobacter pylori in seropositive subjects is affected by pathology and secretory ability of the stomach.
Anemia, Pernicious
Pepsinogens and other serum markers in pernicious anemia.
Carcinoma
Gastric phenotypic expression in human gallbladder cancers revealed by pepsinogen immunohistochemistry and mucin histochemistry.
Carcinoma
[A clinical study of pepsinogen I and II producing gastric carcinomas]
Dehydration
A pollen-specific polygalacturonase from lily is related to major grass pollen allergens.
Duodenal Ulcer
Elevated serum pepsinogen I and II levels differ as risk factors for duodenal ulcer and gastric ulcer.
Duodenal Ulcer
Increased levels of plasma ghrelin in peptic ulcer disease.
Gastritis
Diagnosis of Helicobacter pylori-induced gastritis by serum pepsinogen levels.
Gastritis
Increased levels of plasma ghrelin in peptic ulcer disease.
Gastritis
Serum and gastric mucosal pepsinogens in atrophic gastritis, particularly in type A gastritis associated with pernicious anemia in Japanese.
Gastritis
Serum pepsinogen I and II concentrations and IgG antibody to Helicobacter pylori in dyspeptic patients.
Gastritis
Serum pepsinogens I and II and stomach cancer.
Gastritis
[Dynamic monitoring of serum pepsinogen among high risk populations of gastric cancer in Zhuanghe county]
Gastritis
[Serum pepsinogen response to therapy for Helicobacter pylori associated gastro-duodenal disease]
Gastritis, Atrophic
ABC screening for gastric cancer is not applicable in a Japanese population with high prevalence of atrophic gastritis.
Gastritis, Atrophic
Serum pepsinogens I and II and stomach cancer.
Gastritis, Atrophic
[Comparative examinations of serum pepsinogen I, II and gastric area using computed radiography in the atrophic gastritis]
Gastrointestinal Diseases
Ultrasensitive detection of pepsinogen I and pepsinogen II by a time-resolved fluoroimmunoassay and its preliminary clinical applications.
Graves Disease
Persistently increased gastrin and decreased pepsinogen concentrations in serum from some patients with Graves' disease of triiodothyronine-predominant type and common type.
Hydrops Fetalis
Analysis of real-time SYBR-polymerase chain reaction cycle threshold for diagnosis of the alpha-thalassemia-1 Southeast Asian type deletion: application to carrier screening and prenatal diagnosis of Hb Bart's hydrops fetalis.
Infections
A Novel Polygalacturonase-Inhibiting Protein (PGIP) from Lathyrus sativus L. Seeds.
Infections
A retrospective study assessing the acceleration effect of type I Helicobacter pylori infection on the progress of atrophic gastritis.
Infections
A significant increase in the pepsinogen I/II ratio is a reliable biomarker for successful Helicobacter pylori eradication.
Infections
ABC Classification Is Less Useful for Older Koreans Born before 1960.
Infections
Botrytis cinerea endopolygalacturonase genes are differentially expressed in various plant tissues.
Infections
Characterization and expression of Fusarium graminearum endo-polygalacturonases in vitro and during wheat infection
Infections
Characterization of a canola C2 domain gene that interacts with PG, an effector of the necrotrophic fungus Sclerotinia sclerotiorum.
Infections
Characterization of the dry bean polygalacturonase-inhibiting protein (PGIP) gene family during Sclerotinia sclerotiorum (Sclerotiniaceae) infection.
Infections
Control of virulence gene expression by plant calcium in the phytopathogen Erwinia carotovora.
Infections
Endopolygalacturonase from Fusarium oxysporum f. sp. lycopersici: purification, characterization, and production during infection of tomato plants.
Infections
Endopolygalacturonase genes from Colletotrichum lindemuthianum: cloning of CLPG2 and comparison of its expression to that of CLPG1 during saprophytic and parasitic growth of the fungus.
Infections
Factors governing the regulation of Sclerotinia sclerotiorum cutinase A and polygalacturonase 1 during different stages of infection.
Infections
Functional analysis of Botrytis cinerea pectin methylesterase genes by PCR-based targeted mutagenesis: Bcpme1 and Bcpme2 are dispensable for virulence of strain B05.10.
Infections
Green Fluorescent Detection of Fungal Colonization and Endopolygalacturonase Gene Expression in the Interaction of Alternaria citri with Citrus.
Infections
IDL6-HAE/HSL2 impacts pectin degradation and resistance to Pseudomonas syringae pv tomato DC3000 in Arabidopsis leaves.
Infections
Isolation, expression and characterization of two single-chain variable fragment antibodies against an endo-polygalacturonase secreted by Sclerotinia sclerotiorum.
Infections
Marked decrease in serum pepsinogen II levels resulting from endoscopic resection of a large duodenal tumor.
Infections
Molecular characterization and in planta detection of Fusarium moniliforme endopolygalacturonase isoforms.
Infections
Molecular characterization of an endopolygalacturonase from Fusarium oxysporum expressed during early stages of infection.
Infections
Pectin methylesterase is induced in Arabidopsis upon infection and is necessary for a successful colonization by necrotrophic pathogens.
Infections
Polygalacturonase is a pathogenicity factor in the Claviceps purpurea/rye interaction.
Infections
Post-translational modifications of recombinant B. cinerea EPG 6.
Infections
Production of a cell wall-associated endopolygalacturonase by Colletotrichum lindemuthianum and pectin degradation during bean infection.
Infections
Proteinase inhibitor-inducing factor activity in tomato leaves resides in oligosaccharides enzymically released from cell walls.
Infections
Relationships among endo-polygalacturonase, oxalate, pH, and plant polygalacturonase-inhibiting protein (PGIP) in the interaction between Sclerotinia sclerotiorum and soybean.
Infections
Risk factors for gastric cancer and related serological levels in Fujian, China: hospital-based case-control study.
Infections
Serum pepsinogen I and II concentrations and IgG antibody to Helicobacter pylori in dyspeptic patients.
Infections
Significance of serum pepsinogens and their relationship to Helicobacter pylori infection and histological gastritis in dialysis patients.
Infections
The polygalacturonase-inhibiting protein PGIP2 of Phaseolus vulgaris has evolved a mixed mode of inhibition of endopolygalacturonase PG1 of Botrytis cinerea.
Infections
Three aspartic acid residues of polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris are critical for inhibition of Fusarium phyllophilum PG.
Infections
Type I and type II Helicobacter pylori infection status and their impact on gastrin and pepsinogen level in a gastric cancer prevalent area.
Infections
Use of green fluorescent protein to detect expression of an endopolygalacturonase gene of Colletotrichum lindemuthianum during bean infection.
Infections
[Influence of impaired renal function and Helicobacter pylori infection on serum pepsinogen concentrations]
Infertility, Male
ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE1 (ADPG1), ADPG2, and QUARTET2 are Polygalacturonases required for cell separation during reproductive development in Arabidopsis.
Liver Neoplasms
Multiplex measurement of twelve tumor markers using a GMR multi-biomarker immunoassay biosensor.
Lung Diseases
HUMAN ADENOVIRUS TYPE 4 COMPRISES TWO MAJOR PHYLOGROUPS WITH DISTINCT REPLICATIVE FITNESS AND VIRULENCE PHENOTYPES.
Lung Neoplasms
Multiplex measurement of twelve tumor markers using a GMR multi-biomarker immunoassay biosensor.
Lymphatic Metastasis
Expression of pepsinogen II in gastric cancer. Its relationship to local invasion and lymph node metastases.
Mycoses
Exploring the potential of engineering polygalacturonase-inhibiting protein as an ecological, friendly, and nontoxic pest control agent.
Mycoses
Overexpression of the grapevine PGIP1 in tobacco results in compositional changes in the leaf arabinoxyloglucan network in the absence of fungal infection.
Neoplasm Metastasis
Expression of pepsinogen II in gastric cancer. Its relationship to local invasion and lymph node metastases.
Neoplasms
Cancer development based on chronic active gastritis and resulting gastric atrophy as assessed by serum levels of pepsinogen and Helicobacter pylori antibody titer.
Neoplasms
Correlation of serum pepsinogens and gross appearances combined with histology in early gastric cancer.
Neoplasms
Expression of pepsinogen II in gastric cancer. Its relationship to local invasion and lymph node metastases.
Neoplasms
Expression of pepsinogen II with androgen and estrogen receptors in human prostate carcinoma.
Neoplasms
Expression of sialosyl-Tn in intestinal type cancer cells of human gastric cancers.
Neoplasms
Gastric phenotypic expression in human gallbladder cancers revealed by pepsinogen immunohistochemistry and mucin histochemistry.
Neoplasms
Helicobacter pylori, pepsinogen, and gastric adenocarcinoma in Hawaii.
Neoplasms
Immunochemical study and cellular localization of human pepsinogens during ontogenesis and in gastric cancers.
Neoplasms
Immunocytochemical localization of pepsinogen I and II in the human stomach.
Neoplasms
Marked decrease in serum pepsinogen II levels resulting from endoscopic resection of a large duodenal tumor.
Neoplasms
Multiplex measurement of twelve tumor markers using a GMR multi-biomarker immunoassay biosensor.
Neoplasms
Ovarian mucinous tumors frequently express markers of gastric, intestinal, and pancreatobiliary epithelial cells.
Neoplasms
Pepsinogens I and II in carcinoma of the stomach: an immunohistochemical study.
Neoplasms
Pepsinogens in gastric carcinomas.
Neoplasms
Risk factors for gastric cancer and related serological levels in Fujian, China: hospital-based case-control study.
Neoplasms
Risk of gastric cancer in asymptomatic, middle-aged Japanese subjects based on serum pepsinogen and Helicobacter pylori antibody levels.
Neoplasms
Serum pepsinogen levels in gastric cancer patients and their relationship with Helicobacter pylori infection: a prospective study.
Neoplasms
Slow moving proteinase in gastric cancer and its relationship to pepsinogens I and II. An immunohistochemical study.
Prostatic Neoplasms
Multiplex measurement of twelve tumor markers using a GMR multi-biomarker immunoassay biosensor.
Sarcoma, Avian
Characterization of bone PG II cDNA and its relationship to PG II mRNA from other connective tissues.
Stomach Neoplasms
Expression of pepsinogen II in gastric cancer. Its relationship to local invasion and lymph node metastases.
Stomach Neoplasms
Expression of sialosyl-Tn in intestinal type cancer cells of human gastric cancers.
Stomach Neoplasms
Helicobacter pylori infection, serum pepsinogen level and gastric cancer: a case-control study in Japan.
Stomach Neoplasms
Risk factors for gastric cancer and related serological levels in Fujian, China: hospital-based case-control study.
Stomach Neoplasms
Serum pepsinogens I and II and stomach cancer.
Stomach Neoplasms
Slow moving proteinase in gastric cancer and its relationship to pepsinogens I and II. An immunohistochemical study.
Stomach Neoplasms
Statistical analysis of serum pepsinogen I (PG I) and II (PG II) levels, PG I/PG II ratios and serum gastrin levels in a general population.
Stomach Neoplasms
[Studies on the cut-off value of serum pepsinogen abnormality for screening chronic atrophic gastritis and gastric carcinoma]
Stomach Ulcer
Elevated serum pepsinogen I and II levels differ as risk factors for duodenal ulcer and gastric ulcer.
Stomach Ulcer
Increased levels of plasma ghrelin in peptic ulcer disease.
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D244A
-
the mutant shows significantly increased thermostability and retains activity comparable to that of the wild type enzyme
D244A/D299R
-
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
-
the mutant shows significantly increased thermostability and retains activity comparable to that of the wild type enzyme
D180E
-
0.01% of wild type activity, Km-values change minimally
D180N
-
0.08% of wild type activity, Km-values change minimally
D201E
-
0.01% of wild type activity, Km-values change minimally
D202E
-
0.6% of wild type activity, Km-values change minimally
D202N
-
0.01% of wild type activity, Km-values change minimally
H223A
-
enzyme has only 0.5% of wild type activity, no effect of Km-value
K258N
-
0.8% of wild type activity, 10fold decrease in Km-values
N178D
-
has an activity approximately 20fold lower than the native Aspergillus niger PGII
R256N
-
14% of wild type activity, 10fold decrease in Km-values
D129K
the mutant shows increased catalytic efficiency towards trigalacturonic acid compared to the wild type enzyme
D129R
the mutant shows about wild type activity and stability
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
A365P
the mutant shows about 70% of wild type activity
D395N
the mutant shows about 10% of wild type activity
E364Q
the mutant shows about 20% of wild type activity
E364Q/E366Q
the mutant shows about 60% of wild type activity
H150A
the mutant shows about 20% of wild type activity
K253A
the mutant shows about 50% of wild type activity
K88A
the mutant shows about 1% of wild type activity
P339A
the mutant shows about 5% of wild type activity
P348A
the mutant shows about 80% of wild type activity
P352A
the mutant shows about 35% of wild type activity
P355A
the mutant shows about 30% of wild type activity
P358A
the mutant shows about 7% of wild type activity
R220A
the mutant shows about 10% of wild type activity
A274T
-
site-directed mutagenesis, the mutation causes a marked loss of inhibition by PvPGIP2 of 150fold
K116E
-
site-directed mutagenesis, the mutant shows no inhibition by PvPGIP2
K310T
-
site-directed mutagenesis
L303E
-
site-directed mutagenesis, the mutant enzyme is inhibited by Inhibitor mutant PvPGIP2.Q224K in contrast to the wild-type enzyme
N121K
-
site-directed mutagenesis, the mutation only slightly affects inhibition by PvPGIP2
Q124P
-
site-directed mutagenesis, the mutation only slightly affects inhibition by PvPGIP2
S120N
-
site-directed mutagenesis, the mutation only slightly affects inhibition by PvPGIP2
S120N/N121K/S122D
-
site-directed mutagenesis, the triple mutant is inhibited with a 25fold reduced efficiency by PvPGIP2
S122D,
-
site-directed mutagenesis, the mutation only slightly affects inhibition by PvPGIP2
S363K
-
site-directed mutagenesis
H234K
-
enzymatic activity is abolished
L303E
-
site-directed mutagenesis
S237G
-
activity is reduced to 48% of the wild-type activity
S240G
-
activity is reduced to 6% of the wild-type activity
T274A
-
site-directed mutagenesis
L303E
-
site-directed mutagenesis
-
T274A
-
site-directed mutagenesis
-
K370M
-
no significant difference from wild-type enzyme
K370R
-
no significant difference from wild-type enzyme
K370T
-
no significant difference from wild-type enzyme
N371I
-
enzyme is entirely unstable
N371T
-
enzyme is entirely unstable
N373Y/V374D
-
nearly wild-type levels of secretion and stability
V374A
-
minor effect on both secretion and protein stability
V374D
-
severe effect on both secretion and protein stability
H58Y
-
the mutant shows improved thermostability and catalytic efficiency compared to the wild type enzyme
H58Y/T71Y/T304Y
-
the mutant shows improved thermostability and catalytic efficiency compared to the wild type enzyme
T304Y
-
the mutant shows improved thermostability and catalytic efficiency compared to the wild type enzyme
T71Y
-
the mutant shows improved thermostability and catalytic efficiency compared to the wild type enzyme
industry
-
the enzyme is suitable for application as a textile bioscouring agent
industry
-
the enzyme is suitable for application as a textile bioscouring agent
-
D201N
-
0.01% of wild type activity, Km-values change minimally
D201N
-
inactive, point mutation in the catalytic site that causes complete loss of enzymatic activity
additional information
-
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
-
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
-
amino acids S234/S91 of PGII are unique in binding the pectin backbone and are possibly crucial for its specificity
additional information
-
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
-
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
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
-
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
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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
-
in mutant MH172 with cloned pehA, MH172(pRKpeh), wild-type-level polygalacturonase activity is restored
additional information
-
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
-
in mutant MH172 with cloned pehA, MH172(pRKpeh), wild-type-level polygalacturonase activity is restored
-
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10 - 30
-
the enzyme remains stable for 2 h at 10-30°C and shows about 50% and 25% activity after 2 h at 40°C and 60°C, respectively
2 - 75
-
polygalacturonase is highly active at 20 and 37°C but is also detectable at 2, 50, and 75°C. No activity is detected following incubation in boiling water for 15 s
20 - 40
-
stable up to, 90-100% activity remaining after 120 min
20 - 65
about 10% relative activity at 20°C, about 30% relative activity at 30°C, about 40% relative activity at 40°C, about 70% relative activity at 50°C, about 60% relative activity at 60°C, about 40% relative activity at 65°C
25
-
purified enzyme, half-life is 3 h
30 - 50
-
the enzyme retains about 90%, 80%, 75% and 10% activity after 7 h at 30°C, 35°C, 40°C, and 50°C, respectively
30 - 56
-
the enzyme retains about 90% activity after 30 min at 30-45°C. The activity drops to about 70%, 40% and less than 10% after 30 min at 45°C, 50°C and 55°C, respectively. The melting temperature is 56°C
30 - 60
the enzyme activity remains stable (more than 90% activity) after 30 min between 30 and 60°C
35 - 45
purified recombinant enzyme, pH 6.0, 1 h without substrate, completely stable
35 - 70
the enzyme retains more than 50% of its activity after incubation at 35-70°C for 60 min, but no activity remains after incubation at 70°C for 2 h
37 - 49
-
purified enzyme, pH 3.0-6.5, 10 h, stable at
38
-
pH 5.5, 15 min, stable up to
4
-
purified enzyme, half-life is 104 h
40 - 50
-
purified enzyme, pH 9.0, 60 min, stable
45
the enzyme retains more than 90% of the initial activity after incubation at 45°C for 1 h
50 - 75
-
thermal treatment at 50°C does not have a significant effect on the activity of polygalacturonase in tomato juice, at temperatures between 50 and 75°C, thermal treatment results in partial enzyme inactivation, isoform PG2 is heat-labile and is totally inactivated after a 5 min treatment at 65°C. Thermosonication enhances the inactivation kinetics of isoform PG2 4fold at 60°C while the enhancement decreases to 2.3fold at 75°C
57
-
50% inactivation after 5 min, polygalacturonase II
60 - 100
-
the enzyme shows full polygalacturonase activity for up to 30 min at 60°C after which it experiences a sharp drop, the polygalacturonase retains full activity at 80°C for 5 min and has 50% activity at 70°C at 30 min. The enzyme is stable for 15 min at 70°C, while at 90°C for 15 min 35% activity remains. The least polygalacturonase enzyme activity is recorded at 100°C and 10 min (40%). After this, no activity is recorded
60 - 70
-
inactivation within 12 min
60 - 80
the enzyme retains about 70%, 40% and 10% activity after 1 h at 60°C, 70°C and 80°C, respectively
78
-
50% inactivation after 5 min, polygalacturonase I
100
-
5 min, complete inactivation
100
-
the purified enzyme is heat labile as boiling for 5 min reduces approximately 80% of activity
100
-
5 min, complete inactivation
30
-
stable up to 30°C, exhibits 49% of its activity at 20°C, stability decreases rapidly above 60°C
30
-
about 40% inactivation of polygalacturonase I after 60 min, about 10% inactivation of polygalacturonase II after 60 min
30
Saccharomyces fragilis
-
pH 5.0, stable up to
30
Saccharomyces fragilis
-
2 h, soluble and immobilized enzyme, stable
30
-
approximately stable up to 30°C for 60 min of incubation. Activity of enzyme is gradually decreased with increasing temperature and time
40
Acrocylindrium sp.
-
stable up to
40
-
about 55% inactivation of polygalacturonase I after 60 min, about 50% inactivation of polygalacturonase II after 60 min
40
-
pH 5.0, 30 min, stable below
40
purified recombinant enzyme, stable up to
40
Saccharomyces fragilis
-
2 h, soluble and immobilized enzyme, 25% loss of activity
40
-
15 min, PG1 loses about 30% of its activity, PG2 loses about 10% of its activity
40 - 60
-
the enzyme retains more than 60% of its initial activity after incubation at 40°C for 180 min. The enzyme rapidly loses activity at 50°C and 60°C
40 - 60
the enzyme retains 100%, 100%, 80% and 30% activity after 1 h at 40°C, 50°C, 55°C, and 60°C, respectively
40 - 60
-
the enzyme remains stable for 2 h at 40°C and loses about 40% an 90% of its initial activity after 2 h at 50°C and 60°C, respectively. The enzyme is completely inactive after 3 h at 60 or 70°C
50
-
pH 4.5, stable below
50
-
complete inactivation of polygalacturonase I after 10 min, complete inactivation of polygalacturonase II after 40 min
50
-
50% activity remaining after 120 min
50
-
the enzyme presents a half-life of 2 h at 50°C. The enzyme is fully thermostable up to 45°C, whereas 25% of the initial activity is retained after 210 min of incubation at 50°C
50
P19805
purified enzyme, half-life is 4 h
50
Dipodascus klebahnii
-
pH 5.0, stable up to
50
-
24 h, about 10% loss of activity
50
-
14 h, 50% loss of activity
50
-
rapid decrease of stability above
50
purified recombinant enzyme, 60 min, loss of 40% activity
50
-
purified enzyme, pH 4.0-5.0, 120 min, stable, rapid inactivation above
50
Saccharomyces fragilis
-
pH 5.0, 15 min, stable up to
50
Saccharomyces fragilis
-
2 h, soluble and immobilized enzyme, complete inactivation
50
Saccharomyces fragilis
-
pH 5.0, 15 min, complete loss of activity
50
-
5 min, PG2 and PG1 are stable
50
-
the purified enzyme is 100% stable at 50°C for 1 h, half-life of 10 min at 60°C. At 60°C, enzymatic activity decreases to only 20% of original activity after 1 h
50
-
15 min, PG1 loses about 80% of its activity, PG2 loses about 10% of its activity
50 - 60
-
the enzyme is thermally stable at 50-60°C for 1 h
50 - 60
-
purified enzyme, completely stable for 1 h at 50°C. At 55°C and 60°C, the activity decreases by 55% and 90%, respectively. After 50 min inactivation at 60°C
55
purified recombinant enzyme, pH 6.0, 1 h without substrate,loss of 70% activity
55
-
after 50 min of incubation in citrus pectin, it maintains 80% of its activity, half-life at 90 min. Half-life in orange waste is only 10 min
55
-
15-18% loss of activity per h
55
-
8.7 h: 50% loss of activity
55
-
30 min, complete inactivation at or above
55
-
10 min, complete inactivation
55
-
100% recovery of activity after 2 h
55
-
30 min, loses activity above
55
Saccharomyces fragilis
-
30 min, 50% loss of activity
55
-
5 min, PG1 is stable, PG2 loses about 35% of its activity
55
-
purified enzyme, pH 5.5, without substrate, 1 h, stable
60
-
purified enzyme, pH 9.0, 60 min, loss of 80% activity
60
the enzyme retains more than 90% activity after 30 min at 60°C
60
-
purified enzyme, pH 5.0, stable up to
60
-
pH 5.5, 15 min, complete loss of activity
60
-
1 h, more than 90% loss of activity per h
60
-
complete inactivation after 6 min
60
-
purified recombinant proteins, pH 5.0, the wild-type full-length enzyme is completely stable up to, the catalytic domain of polygalacturonase loses 30% within 1 h
60
-
the enzyme shows a high level of thermostability in the presence of substrate with a residual activity of 48 and 31% at 60°C after 2 and 3 h of incubation. Residual activity of 5% even after 6 h of incubation at 80°C
60
purified recombinant enzyme, 5 min, loss of 95% activity
60
-
above, purified enzyme, pH 5.0, 48.2% activity remaining after 10 min
60
-
20 min, complete and irreversible inactivation
60
-
inactivation in 20 min
60
-
5 min, complete loss of activity of enzyme form PG2, about 5% loss of activity of enzyme form PG1
60
Tetracoccosporium sp.
-
halflife is 63.01 min
60
-
15 min, PG1 loses about 90% of its activity, PG2 loses about 20% of its activity
65
-
10 min, complete loss of activity
65
-
polygalacturonase II, complete inactivation after 5 min
70
-
purified enzyme, pH 5.0, loss of 52% activity
70
-
30 min, stable up to
70
-
above, purified enzyme, pH 5.0, 9.3% activity remaining after 10 min
70
Saccharomyces fragilis
-
30 min, complete loss of activity
70
-
15 min, PG1 loses about 95% of its activity, PG2 loses about 85% of its activity
75
-
pH 5.0, 30 min, enzyme loses most of its activity
80
-
50% activity after 1.6 h at 50°C, 50% activity after 33 min at 55°C, 96% loss of activity after 30 min at 80°C
80
-
5 min, 80% of the activity remains
80
-
purified enzyme, pH 5.0, loss of 90% activity
80
-
20 min, 80% loss of activity
80
-
20 min, 82% loss of activity
90
-
5 h, complete loss of activity
90
-
complete inactivation of polygalacturonase II after 5 min
additional information
Acrocylindrium sp.
-
polygalacturonic acid protects the enzyme from heat inactivation
additional information
-
PG1 is stable at 50°C, at 70°C stability is drastically reduced. PG2 is a very sensitive enzyme, its half-life time at 50°C is in the range of min and at 70°C the enzyme is inactivated within 1 min
additional information
the enzyme is thermolabile, being completely inactivated if kept at 50°C for 2 h
additional information
-
the enzyme is thermolabile, being completely inactivated if kept at 50°C for 2 h
additional information
-
removal of large amounts of carbohydrate does not affect heat stability
additional information
-
thermal and high-pressure inactivation kinetics of purified PG2 at pH 4.4
additional information
-
inactivation at around 55°C corresponds to PG2 and at around 80°C corresponds to PG1. After 5 min at 90°C almost complete inactivation
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analysis
-
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
-
multiplicity of PGs that degrade the pectin component of the plant tissue in different fashions
medicine
despite the significant sequence homology and the conserved surface-exposed epitopes LLP-PG represents a low-allergenic member of pollen PGs
paper production
-
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
agriculture
-
MDG1 is dispensable in the pathogenicity on rice
agriculture
-
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
agriculture
-
MDG1 is dispensable in the pathogenicity on rice
-
food industry
-
agro-industrial wastes are suitable for polygalacturonase production
food industry
-
agro-industrial wastes are suitable for polygalacturonase production
food industry
-
high pressure processing can be used for selective inactivation of PG in tomato processing while keeping pectinmethylesterase intact
food industry
-
properties of the enzyme may be highly beneficial during fruit processing
food industry
-
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.
-
the polygalacturonase has a remarkable heat-tolerance, which makes it very attractive for industrial applications
food industry
-
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
-
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
-
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
-
the enzyme is able to enhance the clarification of citrus juice
food industry
the enzyme is used for grape juice clarification
food industry
-
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
-
the enzyme is used for grape juice clarification
-
food industry
-
agro-industrial wastes are suitable for polygalacturonase production
-
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
-
the enzyme is able to enhance the clarification of citrus juice
-
food industry
-
properties of the enzyme may be highly beneficial during fruit processing
-
food industry
-
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 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
-
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
-
polygalacturonases are pectin substances degrading enzymes, that are widely used in juice and fruit beverages for quality improvement
-
food industry
-
agro-industrial wastes are suitable for polygalacturonase production
-
industry
-
thermostable nature of the polygalacturonase with a high pH range for activity makes it an industrially important enzyme
industry
-
the enzyme is developed a feasible strategy to achieve a rapid benign of the bioscouring process with the wettability properties of cotton fabrics
industry
-
the enzyme is developed a feasible strategy to achieve a rapid benign of the bioscouring process with the wettability properties of cotton fabrics
-
industry
-
thermostable nature of the polygalacturonase with a high pH range for activity makes it an industrially important enzyme
-
nutrition
-
application in extraction of juice from certain fruits and vegetables
nutrition
-
application in extraction of juice from certain fruits and vegetables
nutrition
-
potential application of the enzyme in fruit juice extraction
nutrition
-
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
-
potential application of the enzyme in fruit juice extraction
-
nutrition
-
application in extraction of juice from certain fruits and vegetables
-
additional information
-
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
-
function of polygalacturonase in the colonization of plant material rather than in the destruction of plant
additional information
-
18 polygalacturonase genes identified in strain 99-880. Ancestral form of polygalacturonase in fungi is endolytic and exolytic function evolved later
additional information
-
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
-
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
-
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
-
may be involved in cotton petal development and senescence, and in response to cold stress
additional information
-
PehA is the major but not the sole polygalacturonase, it plays a minor role in Xanthomonas campestris virulence
additional information
-
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
-
tobacco and Arabidopsis polygalacturonase plants inoculated with Botrytis cinerea are more resistant to microbial pathogens and have constitutively activated defense responses
additional information
-
18 polygalacturonase genes identified in strain 99-880. Ancestral form of polygalacturonase in fungi is endolytic and exolytic function evolved later
-
additional information
-
PehA is the major but not the sole polygalacturonase, it plays a minor role in Xanthomonas campestris virulence
-
additional information
-
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
-