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67% esterified citrus pectin
?
-
-
-
-
?
89% esterified citrus pectin
?
-
-
-
-
?
apple pectin
unsaturated digalacturonic acid + unsaturated trigalacturonic acid
-
-
-
?
apple pectin
unsaturated oligogalacturonides
citrus pectin
unsaturated digalacturonic acid + unsaturated trigalacturonic acid
-
-
-
?
citrus pectin
unsaturated oligogalacturonate
citrus pectin
unsaturated oligogalacturonides
citrus pectin
unsaturated tetragalacturonate
citrus peel pectin
unsaturated oligogalacturonides
de-esterified pectin
4,5-unsaturated oligogalacturonates
PEL can randomly catalyze the apha(1-4) linkages of de-esterified pectin by beta-elimination
-
-
?
esterified pectin
?
94% esterified pectin. 97% of the activity with polygalacturonic acid
-
?
esterified pectin
unsaturated tetragalacturonic acid
lime pectin
?
-
with 75% methyl esterification
-
?
methyl esterified pectin
?
-
citrus pectin, 7% methylation
-
-
?
methylated pectin
?
-
-
-
?
methylated pectin
unsaturated oligogalacturonides + ?
oligogalacturonate
unsaturated digalacturonate
oligogalacturonic acid
?
-
the enzyme acts on polygalacturonic acids and oligogalacturonic acids over digalacturonic acid and better on the larger galacturonic acids until at least DP8
-
?
pectic acid
oligouronides of heterogeneous size
pectic biomass
unsaturated oligo-galacturonides + ?
pectin
unsaturated oligogalacturonides
pentagalacturonic acid
saturated digalacturonic acid + unsaturated trigalacturonic acid + saturated trigalacturonic acid + unsaturated digalacturonic acid
polygalacturonate
unsaturated 4,5-digalacturonate + unsaturated 4,5-trigalacturonate
polygalacturonate
unsaturated 4,5-digalacturonate + unsaturated 4,5-trigalacturonate + ?
polygalacturonate
unsaturated digalacturonic acid + unsaturated trigalacturonic acid
-
-
-
?
polygalacturonate
unsaturated galacturonic acid polymer
-
-
-
-
?
polygalacturonate
unsaturated galacturonides
polygalacturonate
unsaturated oligo-galacturonides
polygalacturonate
unsaturated oligogalacturonides
polygalacturonate
unsaturated polygalacturonic acid
-
-
-
-
?
polygalacturonate
unsaturated tetragalacturonate
polygalacturonate
unsaturated tetragalacturonic acid
polygalacturonate
unsaturated trigalacturonate + unsaturated oligogalacturonates
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
major product
-
?
polygalacturonate
unsaturated trigalacturonic acid + unsaturated tetragalacturonic acid
polygalacturonic
?
analysis of polygalacturonic acid degradation products by electrospray ionization-mass spectrometry reveal that the degradation products are unsaturated trigalacturonic acid and unsaturated bigalacturonic acid, which confirms that the enzyme catalyzes a trans-elimination reaction
-
-
?
polygalacturonic acid
4,5-unsaturated digalacturonic acid + 4,5-unsaturated trigalacturonic acid + oligogalacturonic acid
polygalacturonic acid
DELTA4,5-unsaturated oligogalacturonides
-
-
?
polygalacturonic acid
unsaturated galacturonate
polygalacturonic acid
unsaturated oligogalacturonate
polygalacturonic acid
unsaturated oligogalacturonate + ?
polygalacturonic acid
unsaturated oligogalacturonide
polygalacturonic acid
unsaturated oligogalacturonides
reduced tetragalacturonic acid
galacturonic acid + reduced trigalacturonic acid
-
-
-
?
tetragalacturonate
?
-
-
-
?
tetragalacturonic acid
altered trigalacturonic acid + digalacturonic acid + altered digalacturionic acid + D-galacturonic acid
trigalacturonic acid
altered digalacturonic acid + galacturonic acid
additional information
?
-
apple pectin
unsaturated oligogalacturonides
Aspergillus luchuensis var. saitoi
-
-
-
-
?
apple pectin
unsaturated oligogalacturonides
Aspergillus luchuensis var. saitoi KBN 2022
-
-
-
-
?
citrus pectin
?
PelA shows 25% relative activity on citrus pectin compared to polygalacturonate
-
-
?
citrus pectin
?
PelA shows 25% relative activity on citrus pectin compared to polygalacturonate
-
-
?
citrus pectin
?
-
-
-
-
?
citrus pectin
unsaturated oligogalacturonate
-
-
-
?
citrus pectin
unsaturated oligogalacturonate
-
-
-
?
citrus pectin
unsaturated oligogalacturonides
-
-
-
?
citrus pectin
unsaturated oligogalacturonides
-
-
-
?
citrus pectin
unsaturated tetragalacturonate
-
-
-
-
?
citrus pectin
unsaturated tetragalacturonate
-
-
-
-
?
citrus pectin P9311
?
-
-
-
-
?
citrus pectin P9311
?
-
-
-
-
?
citrus pectin P9311
?
-
-
-
-
?
citrus pectin P9436
?
-
-
-
-
?
citrus pectin P9436
?
-
-
-
-
?
citrus pectin P9436
?
-
-
-
-
?
citrus pectin P9561
?
-
-
-
-
?
citrus pectin P9561
?
-
-
-
-
?
citrus pectin P9561
?
-
-
-
-
?
citrus peel pectin
unsaturated oligogalacturonides
Aspergillus luchuensis var. saitoi
-
-
-
-
?
citrus peel pectin
unsaturated oligogalacturonides
Aspergillus luchuensis var. saitoi KBN 2022
-
-
-
-
?
digalacturonic acid
?
-
-
-
-
?
digalacturonic acid
?
-
-
-
-
?
esterified pectin
unsaturated tetragalacturonic acid
-
affinity shows a maximum for intermediate esterified pectins and decreases over a value of 50% of esterification. The best substrate is 29.5% methylated pectin
-
-
?
esterified pectin
unsaturated tetragalacturonic acid
-
affinity shows a maximum for intermediate esterified pectins and decreases over a value of 50% of esterification. The best substrate is 29.5% methylated pectin
-
-
?
hexagalacturonic acid
?
-
17.2% of the activity with polygalacturonic acid
-
-
?
hexagalacturonic acid
?
-
-
-
-
?
hexagalacturonic acid
?
-
140% of the activity with low molecular weight polygalacturonic acid
-
-
?
methylated pectin
unsaturated oligogalacturonides + ?
-
-
-
?
methylated pectin
unsaturated oligogalacturonides + ?
-
-
-
?
oligogalacturonate
unsaturated digalacturonate
-
isoenzyme PelB and pelD show highest activity on hexagalacturonate and tetragalacturonate, respectively. Isoenzyme pelA, pelB and pelL are most active on the octamer
the preferential products formed are unsaturated dimer for isoenzyme PelD, unsaturated trimer for isoenzyme PelB, and unsaturated tetramer for isoenzyme PelI and PelL. For isoenzyme pelA, preferential products are dependent on the size of the oligogalacturonate
?
oligogalacturonate
unsaturated digalacturonate
-
isoenzyme PelB and pelD show highest activity on hexagalacturonate and tetragalacturonate, respectively. Isoenzyme pelA, pelB and pelL are most active on the octamer
the preferential products formed are unsaturated dimer for isoenzyme PelD, unsaturated trimer for isoenzyme PelB, and unsaturated tetramer for isoenzyme PelI and PelL. For isoenzyme pelA, preferential products are dependent on the size of the oligogalacturonate
?
pectate
?
-
-
-
?
pectate
?
-
methylated form
-
-
?
pectate
?
i.e. polygalacturonic acid, cleavage of the pectate alpha-1,4-glycosidic bond by Pel-BL11
-
-
?
pectate
?
i.e. polygalacturonic acid, cleavage of the pectate alpha-1,4-glycosidic bond by Pel-BL11
-
-
?
pectic acid
oligouronides of heterogeneous size
-
acid soluble
-
-
?
pectic acid
oligouronides of heterogeneous size
-
acid soluble
-
-
?
pectic acid
oligouronides of heterogeneous size
Erwinia aroidea
-
-
-
?
pectic acid amide
?
-
about 15% of activity with acid soluble pectic acid
-
-
?
pectic acid amide
?
-
about 15% of activity with acid soluble pectic acid
-
-
?
pectic biomass
unsaturated oligo-galacturonides + ?
-
-
-
?
pectic biomass
unsaturated oligo-galacturonides + ?
-
-
-
?
pectin
?
-
-
-
-
?
pectin
?
-
low-esterified pectin (30%) is the optimum substrate for the PelA, higher-esterified pectin is hardly cleaved
-
-
?
pectin
?
-
low-esterified pectin (30%) is the optimum substrate for the PelA, higher-esterified pectin is hardly cleaved
-
-
?
pectin
?
-
at about 12% of the activity with acid soluble pectic acid
-
-
?
pectin
?
of methyl esterification degree from 22-89%. Similar activity on polygalacturonic acid and on 89% esterified citrus pectin
-
?
pectin
?
relative degradation rates of citrus pectin with methylation degrees 31%, 63% and 94% is 124%, 73% and 9% compared to polygalacturonic acid
-
?
pectin
?
with degrees of esterification of 31%, 63% and 94% is degraded with 103%, 84% and 46% of the activity with polygalacturonic acid
-
?
pectin
?
of methyl esterification degree from 22-89%. Similar activity on polygalacturonic acid and on 89% esterified citrus pectin
-
?
pectin
?
with degrees of esterification of 31%, 63% and 94% is degraded with 103%, 84% and 46% of the activity with polygalacturonic acid
-
?
pectin
?
relative degradation rates of citrus pectin with methylation degrees 31%, 63% and 94% is 124%, 73% and 9% compared to polygalacturonic acid
-
?
pectin
?
-
at about 12% of the activity with acid soluble pectic acid
-
-
?
pectin
?
-
of methyl esterification degree from 22% to 89%, maximal activity on 22% esterified citrus pectin
-
-
?
pectin
?
pectate lyases harness anti beta-elimination chemistry to cleave the alpha-1,4 linkage in the homogalacturonan region of plant cell wall pectin
-
-
?
pectin
?
-
with a low degree of methylation
-
-
?
pectin
?
-
with a low degree of methylation
-
-
?
pectin
?
Erwinia aroidea
-
with low methoxyl content
-
-
?
pectin
?
-
about 70% methylated
-
-
?
pectin
?
-
with 4.3% methoxyl groups
-
-
?
pectin
?
-
unlike other isoenzymes, pectate lyase requires partially methyl esterified pectin as substrate
-
-
?
pectin
?
-
no activity with 93% esterified pectin
-
-
?
pectin
?
-
better substrate for pectate lyase I than polygalacturonic acid
-
?
pectin
?
apple or citrus pectin, activity with pectin is lower than activity with polygalacturonate
-
-
?
pectin
?
apple pectin, citrus pectin, as the percentage of methylation in pectin becomes higher, the activities become lower
-
-
?
pectin
?
apple or citrus pectin, activity with pectin is lower than activity with polygalacturonate
-
-
?
pectin
?
80% of the activity with polygalacturonic acid
-
?
pectin
?
methylated at low-degree
-
-
?
pectin
unsaturated oligogalacturonides
-
32% esterification, best substrate. At 54% esterification, about 70% of the activity with pectin of 32% esterification
-
-
?
pectin
unsaturated oligogalacturonides
-
32% esterification, best substrate. At 54% esterification, about 70% of the activity with pectin of 32% esterification
-
-
?
pectin
unsaturated oligogalacturonides
-
esterified citrus pectin
-
?
pentagalacturonic acid
saturated digalacturonic acid + unsaturated trigalacturonic acid + saturated trigalacturonic acid + unsaturated digalacturonic acid
-
5.9% of the activity with polygalacturonic acid
-
-
?
pentagalacturonic acid
saturated digalacturonic acid + unsaturated trigalacturonic acid + saturated trigalacturonic acid + unsaturated digalacturonic acid
-
-
-
-
?
pentagalacturonic acid
saturated digalacturonic acid + unsaturated trigalacturonic acid + saturated trigalacturonic acid + unsaturated digalacturonic acid
-
215% of the activity with low molecular weight polygalacturonic acid
-
-
?
pentagalacturonic acid
saturated digalacturonic acid + unsaturated trigalacturonic acid + saturated trigalacturonic acid + unsaturated digalacturonic acid
-
-
preferentially split into saturated digalacturonic acid + unsaturated trigalacturonic acid or into saturated trigalacturonic acid + unsaturated digalacturonic acid - at a lower rate it is also split into monogalacturonic acid and unsaturated tetragalacturonic acid
?
polygalacturonate
?
-
Pel I
-
-
?
polygalacturonate
?
-
Pel II
-
-
?
polygalacturonate
?
-
Pel III
-
-
?
polygalacturonate
?
-
Pel I
-
-
?
polygalacturonate
?
-
Pel II
-
-
?
polygalacturonate
?
-
Pel III
-
-
?
polygalacturonate
?
-
-
?
polygalacturonate
?
-
-
?
polygalacturonate
?
-
-
-
-
?
polygalacturonate
?
-
-
-
?
polygalacturonate
?
-
-
-
-
?
polygalacturonate
unsaturated 4,5-digalacturonate + unsaturated 4,5-trigalacturonate
-
-
-
?
polygalacturonate
unsaturated 4,5-digalacturonate + unsaturated 4,5-trigalacturonate
-
-
-
?
polygalacturonate
unsaturated 4,5-digalacturonate + unsaturated 4,5-trigalacturonate + ?
the enzyme is specific toward alpha-1,4-galacturonic acid linkages of galactopolysaccharides
main products
-
?
polygalacturonate
unsaturated 4,5-digalacturonate + unsaturated 4,5-trigalacturonate + ?
the enzyme is specific toward alpha-1,4-galacturonic acid linkages of galactopolysaccharides
main products
-
?
polygalacturonate
unsaturated galacturonides
-
-
-
-
?
polygalacturonate
unsaturated galacturonides
-
-
-
-
?
polygalacturonate
unsaturated oligo-galacturonides
-
the enzyme produces unsaturated oligo-galacturonides including unsaturated tri-galacturonic acid and unsaturated bi-galacturonic acid but not unsaturated mono-galacturonic acid
-
-
?
polygalacturonate
unsaturated oligo-galacturonides
-
the enzyme produces unsaturated oligo-galacturonides including unsaturated tri-galacturonic acid and unsaturated bi-galacturonic acid but not unsaturated mono-galacturonic acid
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
about 75% of the activity with pectin of 32% esterification
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
about 75% of the activity with pectin of 32% esterification
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
EDW21517
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
EDW21517
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
-
-
?
polygalacturonate
unsaturated tetragalacturonate
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated tetragalacturonate
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated tetragalacturonic acid
-
the enzyme cleaves polygalacturonic acid via a beta-elimination mechanism
-
-
?
polygalacturonate
unsaturated tetragalacturonic acid
-
the enzyme cleaves polygalacturonic acid via a beta-elimination mechanism
-
-
?
polygalacturonate
unsaturated trigalacturonic acid + unsaturated tetragalacturonic acid
Aspergillus luchuensis var. saitoi
-
-
-
-
?
polygalacturonate
unsaturated trigalacturonic acid + unsaturated tetragalacturonic acid
Aspergillus luchuensis var. saitoi KBN 2022
-
-
-
-
?
polygalacturonic acid
4,5-unsaturated digalacturonic acid + 4,5-unsaturated trigalacturonic acid + oligogalacturonic acid
-
unsaturated di- and trigalacturonic acids are mainly formed as the final products of degradation by Pel SWU
-
?
polygalacturonic acid
4,5-unsaturated digalacturonic acid + 4,5-unsaturated trigalacturonic acid + oligogalacturonic acid
-
unsaturated di- and trigalacturonic acids are mainly formed as the final products of degradation by Pel SWU
-
?
polygalacturonic acid
4,5-unsaturated digalacturonic acid + 4,5-unsaturated trigalacturonic acid + oligogalacturonic acid
-
endo-type reaction
-
?
polygalacturonic acid
4,5-unsaturated digalacturonic acid + 4,5-unsaturated trigalacturonic acid + oligogalacturonic acid
-
endo-type reaction, little action on highly esterified polygalacturonic acid methylglucoside.The enzyme acts on polygalacturonic acids and oligogalacturonic acids over digalacturonic acid and better on the larger galacturonic acids until at least DP8
-
?
polygalacturonic acid
?
-
-
-
-
?
polygalacturonic acid
?
-
-
-
-
?
polygalacturonic acid
?
-
-
-
-
?
polygalacturonic acid
?
Arg235 is an essential catalytic residue
-
-
?
polygalacturonic acid
?
Arg235 is an essential catalytic residue
-
-
?
polygalacturonic acid
?
degradation through an endo-type fashion
-
?
polygalacturonic acid
?
degradation through an endo-type fashion
-
?
polygalacturonic acid
?
-
-
-
?
polygalacturonic acid
?
-
-
-
?
polygalacturonic acid
?
the recombinant enzyme shows highest activity on polygalacturonic acid and lower activity on more highly methylated pectin
-
-
?
polygalacturonic acid
?
-
-
-
-
?
polygalacturonic acid
?
-
Arg initiates proton abstration during the beta elimination cleavage of polygalacturonic acid
-
?
polygalacturonic acid
?
-
-
-
?
polygalacturonic acid
?
-
random cleavage
-
?
polygalacturonic acid
?
-
random cleavage
-
?
polygalacturonic acid
?
-
-
-
?
polygalacturonic acid
?
-
-
-
-
?
polygalacturonic acid
?
-
-
-
-
?
polygalacturonic acid
?
-
-
-
?
polygalacturonic acid
?
-
-
-
-
?
polygalacturonic acid
?
-
-
-
?
polygalacturonic acid
?
-
-
-
-
?
polygalacturonic acid
?
-
-
-
?
polygalacturonic acid
?
-
-
?
polygalacturonic acid
?
best substrate
final major end products are dimers, trimers, and tetramers of unsaturated galacturonic acid, PelB does not produce any monomeric GalpA
-
?
polygalacturonic acid
?
-
-
-
-
?
polygalacturonic acid
?
enzyme is found to be active on both polygalacturonic acid and citrus pectin as substrates, although it appears to prefer polygalacturonic acid
-
-
?
polygalacturonic acid
?
enzyme shows over ten times higher catalytic efficiency towards polygalacturonic acid than towards citrus pectin
-
-
?
polygalacturonic acid
?
-
-
-
-
?
polygalacturonic acid
?
endolytic cleavage
-
?
polygalacturonic acid
unsaturated galacturonate
-
-
-
?
polygalacturonic acid
unsaturated galacturonate
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
random attack
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
random attack
a mixture of 4,5-unsaturated oligogalacturonides, approximately molar ratios of 12:74:14 for monomer, dimer, and trimer, respectively
?
polygalacturonic acid
unsaturated oligogalacturonate
-
random attack
a mixture of 4,5-unsaturated oligogalacturonides, approximately molar ratios of 12:74:14 for monomer, dimer, and trimer, respectively
?
polygalacturonic acid
unsaturated oligogalacturonate
-
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
random attack
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
activity decreases when the methoxyl content of the substrate increases
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
-
the main product appears to be a disaccharide that contains a DELTA4,5-unsaturated galacturonic acid residue
?
polygalacturonic acid
unsaturated oligogalacturonate
-
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
-
isoenzyme PelA, PelI and PelL release oligogalacturonates of different sizes, isoenzyme PelD, pelB release mostly unsaturated dimer and unsaturated trimer, respectively
?
polygalacturonic acid
unsaturated oligogalacturonate
-
with a low degree of methylation
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
with a low degree of methylation
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
-
isoenzyme PelA, PelI and PelL release oligogalacturonates of different sizes, isoenzyme PelD, pelB release mostly unsaturated dimer and unsaturated trimer, respectively
?
polygalacturonic acid
unsaturated oligogalacturonate
-
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
endo-cleavage
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
endo-cleavage
wide range of 4,5-unsaturated oligogalacturonates, further depolymerized to unsaturated dimer and trimer
?
polygalacturonic acid
unsaturated oligogalacturonate
-
random attack
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
random attack
higher oligomers are detected in the early stage of degradation, unsaturated monogalacturonic acids and digalacturonic acids are also detected after prolonged degradation
?
polygalacturonic acid
unsaturated oligogalacturonate
-
low molecular weight. High molecular weight polygalacturonic acid is attacked at 46% of the activity with low molecular weight polygalacturonic acid
higher oligomers are detected in the early stage of degradation, unsaturated monogalacturonic acids and digalacturonic acids are also detected after prolonged degradation
?
polygalacturonic acid
unsaturated oligogalacturonate
-
-
end products at 46% saturation: unsaturated digalacturonic acids, unsaturated trigalacturonic acids, saturated monogalacturonic acid + saturated digalacturonic acid + saturated trigalacturonic acid
?
polygalacturonic acid
unsaturated oligogalacturonate + ?
specific substrate, enzyme activity decreases when the methoxyl content of the substrate increases
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate + ?
specific substrate, enzyme activity decreases when the methoxyl content of the substrate increases
-
-
?
polygalacturonic acid
unsaturated oligogalacturonide
-
-
?
polygalacturonic acid
unsaturated oligogalacturonide
-
-
?
polygalacturonic acid
unsaturated oligogalacturonides
-
-
?
polygalacturonic acid
unsaturated oligogalacturonides
-
-
?
polygalacturonic acid
unsaturated oligogalacturonides
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonides
-
i.e. pectate, endo-cleavage, the enzyme has a preference for sequences of non-esterified galacturonic acid residues
-
?
polygalacturonic acid
unsaturated oligogalacturonides
-
-
-
?
polypectate
?
-
-
-
-
?
protopectin
pectin + ?
-
-
-
?
protopectin
pectin + ?
-
-
-
?
ramie fiber
?
-
-
-
?
tetragalacturonic acid
altered trigalacturonic acid + digalacturonic acid + altered digalacturionic acid + D-galacturonic acid
-
-
only trace amounts of digalacturonic acid
?
tetragalacturonic acid
altered trigalacturonic acid + digalacturonic acid + altered digalacturionic acid + D-galacturonic acid
-
-
-
-
?
tetragalacturonic acid
altered trigalacturonic acid + digalacturonic acid + altered digalacturionic acid + D-galacturonic acid
-
141% of the activity with low molecular weight polygalacturonic acid
-
-
?
trigalacturonate
?
-
enzyme and substrate-binding structures, overview
-
-
?
trigalacturonate
?
-
enzyme and substrate-binding structures, overview
-
-
?
trigalacturonate
?
-
-
-
?
trigalacturonic acid
?
-
-
-
-
?
trigalacturonic acid
?
-
-
-
-
?
trigalacturonic acid
altered digalacturonic acid + galacturonic acid
-
-
-
?
trigalacturonic acid
altered digalacturonic acid + galacturonic acid
-
-
-
-
?
trigalacturonic acid
altered digalacturonic acid + galacturonic acid
-
3% of the activity with low molecular weight polygalacturonic acid
-
-
?
additional information
?
-
-
best substrate: low-esterified pectin
-
-
?
additional information
?
-
-
best substrate: low-esterified pectin
-
-
?
additional information
?
-
-
in the completed genome of Arabidopsis, there are 26 genes that encode pectate lyase-like proteins. The stability of transcripts of PLLs varies considerably among different genes. Complex regulation of expression of PLLs and involvement of PLLs in some of the hormonal and stress responses. several PLLs are expressed highly in pollen, suggesting a role for these in pollen development and/or function
-
-
?
additional information
?
-
-
PelA efficiently macerates mung bean hypocotyls and potato tuber tissues into single cells
-
-
?
additional information
?
-
-
PelA efficiently macerates mung bean hypocotyls and potato tuber tissues into single cells
-
-
?
additional information
?
-
no substrates: carboxymethylcellulose, xylan, glucan, and locust bean gum
-
-
?
additional information
?
-
substrates are 45% methylated pectin or polygalacturonate
-
-
?
additional information
?
-
substrates are 45% methylated pectin or polygalacturonate
-
-
?
additional information
?
-
-
substrates are 45% methylated pectin or polygalacturonate
-
-
?
additional information
?
-
-
protopectinase-like activity on cotton fibers
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
PelA does not show any activity on mannan, CMC, xylan, glucan, or soluble starch
-
-
?
additional information
?
-
-
PelA does not show any activity on mannan, CMC, xylan, glucan, or soluble starch
-
-
?
additional information
?
-
-
protopectinase-like activity on cotton fibers
-
-
?
additional information
?
-
PelA does not show any activity on mannan, CMC, xylan, glucan, or soluble starch
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
enzyme production is repressed by glucose
-
-
?
additional information
?
-
digalacturonate is not cleaved at an appreciable rate
-
-
?
additional information
?
-
-
digalacturonate is not cleaved at an appreciable rate
-
-
?
additional information
?
-
substrates are 45% methylated pectin or polygalacturonate
-
-
?
additional information
?
-
substrates are 45% methylated pectin or polygalacturonate
-
-
?
additional information
?
-
-
substrates are 45% methylated pectin or polygalacturonate
-
-
?
additional information
?
-
the enzyme plays an important role in plant-nematode interactions
-
-
?
additional information
?
-
-
the enzyme plays an important role in plant-nematode interactions
-
-
?
additional information
?
-
reaction mechanism can be explained by an antiperiplanar trans-elimination reaction, in which Lys108 abstracts a proton from the C5 atom. An acidified water molecule completes the anti beta-elimination reaction by protonating the O4 atom of the substrate. Both the C5 hydrogen and C4 hydroxyl groups of the substrate must be orientated in axial configurations
-
-
?
additional information
?
-
-
reaction mechanism can be explained by an antiperiplanar trans-elimination reaction, in which Lys108 abstracts a proton from the C5 atom. An acidified water molecule completes the anti beta-elimination reaction by protonating the O4 atom of the substrate. Both the C5 hydrogen and C4 hydroxyl groups of the substrate must be orientated in axial configurations
-
-
?
additional information
?
-
reaction mechanism can be explained by an antiperiplanar trans-elimination reaction, in which Lys108 abstracts a proton from the C5 atom. An acidified water molecule completes the anti beta-elimination reaction by protonating the O4 atom of the substrate. Both the C5 hydrogen and C4 hydroxyl groups of the substrate must be orientated in axial configurations
-
-
?
additional information
?
-
-
the enzyme secreted by the bacterium into the human large intestine cooperatively digests pectic substances, producing mainly 4,5-unsaturated digalacturonic acid with the participation of the pectin methyltransferase
-
?
additional information
?
-
-
the enzyme secreted by the bacterium into the human large intestine cooperatively digests pectic substances, producing mainly 4,5-unsaturated digalacturonic acid with the participation of the pectin methyltransferase
-
?
additional information
?
-
as the external pH increases from 4.0 to 6.0, pectate lyase and other extracellular proteins are secreted and accumulate. Nitrogen assimilation also is required for enzyme secretion at pH 6.0. The ambient pH and the nitrogen source are independent regulatory factors for processes linked to secretion of pectate lyase and virulence of Colletotrichum gloeosporioides
-
?
additional information
?
-
-
as the external pH increases from 4.0 to 6.0, pectate lyase and other extracellular proteins are secreted and accumulate. Nitrogen assimilation also is required for enzyme secretion at pH 6.0. The ambient pH and the nitrogen source are independent regulatory factors for processes linked to secretion of pectate lyase and virulence of Colletotrichum gloeosporioides
-
?
additional information
?
-
-
the pathogenicity of Colletotrichum gloeosporioides is dependent on its ability to secrete pectate lyase. The host pH in pericarp regulates the secretion. Secretion is detected when the pH reaches 5.8 and the level of secretion increases up to pH 6.5
-
?
additional information
?
-
-
when the fungus is grown at pH 4.0 or 6.0 in the absence of a nitrogen source, neither pelB (encoding pectate lyase) transcription nor pectate lyase secretion is detected. pelB transcription and pectate lyase secretion are both detected when Colletotrichum gloeosporioides is grown at pH 6.0 in the presence of ammonia accumulated from different nitrogen sources. The early accumulation of ammonia induces early pelB expression and pectate lyase secretion. Nit mutants of Colletotrichum gloeosporioides, which cannot utilize KNO3 as a nitrogen source, do not secrete ammonia, alkalinize the medium, or secrete pectate lyase. If Nit mutants are grown at pH 6.0 in the presence of glutamate, then pectate lyase secretion is induced
-
-
?
additional information
?
-
-
optimization of chemical and physical parameters affecting the activity of pectate lyase
-
-
?
additional information
?
-
-
pectate lyase E is most effective in causing maceration and inducing electrolyte loss and cell death in potato tuber tissue
-
-
?
additional information
?
-
-
colonization of plant tissues by the phytopathogen Erwinia chrysanthemi E16 is aided by the activities of the pectate lyase isoenzymes, which depolymerize the polygalacturonic acid component of the plant cell walls
-
?
additional information
?
-
-
pectate lyase A is a virulence factor for soft rot diseases in plants
-
?
additional information
?
-
-
pectate lyase A is a virulence factor secreted by the plant pathogenic bacterium Erwinia chrysanthemi
-
?
additional information
?
-
-
pectate lyase E is most effective in causing maceration and inducing electrolyte loss and cell death in potato tuber tissue
-
-
?
additional information
?
-
-
pectate lyase A is a virulence factor for soft rot diseases in plants
-
?
additional information
?
-
-
pectate lyase A is a virulence factor secreted by the plant pathogenic bacterium Erwinia chrysanthemi
-
?
additional information
?
-
-
colonization of plant tissues by the phytopathogen Erwinia chrysanthemi E16 is aided by the activities of the pectate lyase isoenzymes, which depolymerize the polygalacturonic acid component of the plant cell walls
-
?
additional information
?
-
-
PelN acts synergistically with other pectate lyases in the organism, activity comparisons, overview
-
-
?
additional information
?
-
Erwinia aroidea
-
pectin or pectic acid as inducer
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
the enzyme is involved in pathogenesis
-
-
?
additional information
?
-
-
best substrates are pectates with a degree of esterification of 14%, and relative degradation rates for pectic substrates with degree of esterification between 5 and 75% are more than 60%
-
-
?
additional information
?
-
-
best substrates are pectates with a degree of esterification of 14%, and relative degradation rates for pectic substrates with degree of esterification between 5 and 75% are more than 60%
-
-
?
additional information
?
-
-
the Gr-PEL2 protein is capable of inducing profound changes in the plant morphology, not related to tissue maceration or soft rot
-
-
?
additional information
?
-
substrates are 45% methylated pectin or polygalacturonate
-
-
?
additional information
?
-
-
substrates are 45% methylated pectin or polygalacturonate
-
-
?
additional information
?
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelA, overview
-
-
?
additional information
?
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelA, overview
-
-
?
additional information
?
-
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelA, overview
-
-
?
additional information
?
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelB, overview
-
-
?
additional information
?
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelB, overview
-
-
?
additional information
?
-
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelB, overview
-
-
?
additional information
?
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelA, overview
-
-
?
additional information
?
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelA, overview
-
-
?
additional information
?
-
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelA, overview
-
-
?
additional information
?
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelB, overview
-
-
?
additional information
?
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelB, overview
-
-
?
additional information
?
-
-
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelB, overview
-
-
?
additional information
?
-
-
no activity with digalacturonic acid
-
-
?
additional information
?
-
PelN exhibits relatively high activity on methylated substrates. On pectin with relatively low degree (20-34%) of methylation, the remaining specific activity of PelN is approximately 100% of that on polygalacturonic acid. Highly methylated pectin (55-70%) results in slight inhibition of the PelN activity to 74%
-
-
?
additional information
?
-
-
the pectate lyase isoenzyme PelS appears to alter the final symptoms in infected cucumber cotyledons without contributing to pathogenicity or altering host range
-
-
?
additional information
?
-
-
macerating activity on Ganpi bark, carrot, radish and sweet potato
-
-
?
additional information
?
-
-
macerating activity on potato tissue and Ganpi bark
-
-
?
additional information
?
-
-
digalacturonic acid and trigalacturonic acid are not good substrates
-
-
?
additional information
?
-
-
no macerating activity on Gampi bark, carrot, potato, cabbage and radish
-
-
?
additional information
?
-
the enzyme is involved in degradation of the pectate portion of the primary plant cell wall
-
?
additional information
?
-
-
the enzyme is involved in degradation of the pectate portion of the primary plant cell wall
-
?
additional information
?
-
PelB is an endo-acting lyase and shows high cleavage capability on a broad range of substrates of natural methylated pectin, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme activity against polygalacturonic acid as 100%, r-PL D exhibits 91.7%, 47.3%, and 6.5% of the activity when pectin is methyl-esterified 34%, 70%, and 85%, respectively
-
-
?
additional information
?
-
-
the enzyme activity against polygalacturonic acid as 100%, r-PL D exhibits 91.7%, 47.3%, and 6.5% of the activity when pectin is methyl-esterified 34%, 70%, and 85%, respectively
-
-
?
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Ag+
-
1 mM, stimulates activity up to 120%
Fe3+
-
1 mM, stimulates activity up to 348%
Hg2+
-
1 mM, can replace Ca2+ in activation
Se2+
activates 158% at 0.2 mM
Triton X-100
activates slightly at 0.5-1 mM
Tween-20
activates slightly at 1 mM
Ba2+
-
1 mM, 216% of initial activity
Ba2+
activates 181% at 0.2 mM
Ba2+
the enzyme is activated slightly in the presence of BaCl2
Ba2+
1 mM, 139% of initial activity
Ca2+
presence of Ca2+ increases thermostability
Ca2+
-
1 mM, 306% of initial activity. Presence of Ca2+ enhances thermoactivity and thermostability
Ca2+
Aspergillus luchuensis var. saitoi
-
activation, optimum concentration 0.3 mM
Ca2+
-
1 mM, activity is enhanced by 1209%
Ca2+
strong sigmoidal CaCl2 concentration dependent relation. Optimal catalysis at 0.5-1.0 mM Ca2+
Ca2+
-
optimum Ca2+ concentration at 0.6 mM
Ca2+
presence of Ca2+ enhances PelA stability in NaOH-glycine buffer, pH 9. About 60% activity is retained under incubation at 65°C with 0.3 mM CaCl2
Ca2+
activates 208% at 0.2 mM
Ca2+
absolute requirement
Ca2+
required for activity
Ca2+
-
restores activity of the EGTA-inactivated enzyme
Ca2+
-
optimal concentration: 0.4 mM
Ca2+
required for activity on pectic substrates, maximal activity at 0.5-0.75 mM CaCl2. Only 9% of maximal activity at 10 mM CaCl2
Ca2+
-
structurally essential
Ca2+
-
dependent on, binding structure, overview
Ca2+
Ca2+ is not required for activity on pectic substrates
Ca2+
-
optimum concentration at 0.6 mM
Ca2+
-
absolute requirement
Ca2+
-
maximal activity at 0.5-1 mM CaCl2
Ca2+
-
71% of maximal activity in absence of Ca2+
Ca2+
activity is not changed
Ca2+
-
optimum Ca2+ concentration at 2.0 mM
Ca2+
the enzyme in the absence of substrate binds a single calcium ion, two additional calcium ions bind between enzyme and substrate carboxylates occupying the +1 subsite in the Michaelis complex
Ca2+
activates 263% at 0.2 mM
Ca2+
required, activates the recombinant enzyme from Pichia pastoris by 26%
Ca2+
1 mM, 257% of initial activity
Ca2+
activity is lost at low pH because protonation of aspartates results in the loss of the two catalytic calcium-ions causing a profound failure to correctly organise the Michaelis complex
Ca2+
activity of wild-type peaks at 1 mM Ca2+, and declines with the increase in Ca2+concentration
Ca2+
presence of Ca2+ stimulates a change in tertiary structure. Binding of Ca2+ and polygalacturonic acid to the active site may occur independently
Ca2+
BxPEL1 shows full dependency
Ca2+
-
optimal activity in presence of 2.0-4.0 mM Ca2+. No activity when Ca2+ is replaced with Co2+, Cu2+, Ba2+, Mg2+, Mn2+, Ni2+, Sr2+ or Zn2+
Ca2+
-
optimum Ca2+ concentration at 2.0-4.0 mM
Ca2+
-
both pectate lyase I and II require 0.2 mM Ca2+ for maximal activity
Ca2+
-
optimal concentration: 0.2 mM
Ca2+
-
optimal concentration: 0.1 mM
Ca2+
-
the Ca2+ site consists primarily of beta-turns and beta-strands. The Ca2+ affinity for the enzyme is weak. Kd: 0.132 mM at pH 9.5, 1.09 mM at pH 11.2 and 5.84 mM at pH 4.5. Enzymatic activity at pH 4.5 is greatest at 30 mM Ca2+
Ca2+
-
the enzyme has a single high affinity calcium-binding site. A second Ca2+ binds between enzyme and substrate in the Michaelis complex
Ca2+
optimum Ca2+ concentration at 0.5 mM
Ca2+
optimum concentration at 0.6 mM
Ca2+
Erwinia aroidea
-
stimulates
Ca2+
-
optimum concentration at 1.0 mM, Ca2+ cannot be replaced by Ba2+, Be2+, Sr2+, Mg2+, and monovalent cations for Pel activity
Ca2+
-
optimum Ca2+ concentration at 0.6 mM
Ca2+
activates, active site binding structure, overview
Ca2+
enzyme activity is Ca2+-dependent
Ca2+
activates 208% at 0.2 mM
Ca2+
-
enzyme from Alpine strain A15 completely loses activity in absence of Ca2+
Ca2+
-
enzyme from Siberian strain AG25 completely loses activity in absence of Ca2+
Ca2+
-
required, can be replaced by Mn2+ or Mg2+. Optimal activity at 0.7 mM. Additive effect when any two metal ions (Mg2+, Ca2+, Mn2+) are present together
Ca2+
-
optimum Ca2+ concentration at 0.2 mM
Ca2+
activates optimally at 0-2.5 mM
Ca2+
-
enhances activity 5fold
Ca2+
required, 7.3fold activation at 0.5 mM, 4.4fold at 1 mM, Ca2+-binding residues are D151, D173, and D177 in PelN
Ca2+
residues D152, D174, and D178 form the Ca2+ ion binding sites
Ca2+
-
optimal concentration: 0.2 mM
Ca2+
-
0.5 mM, 7fold activation of pectate lyase I, 4fold activation of pectate lyase II
Ca2+
-
stabilizes, best activating metal ion, optimally at 2 mM
Ca2+
-
absolute requirement for Ca2+for pectin degradation, no other divalent cation (Mg2+, Mn2+, Ba2+, Cu2+, Zn2+ or Co2+) can substitute for Ca2+, pectate lyase activity is undetectable without Ca2+ and the maximum activity is at 0.75 mm CaCl2, while enzymatic activity decreases at higher concentrations of Ca2+
Ca2+
-
activates, optimal at 1 mM
Ca2+
-
optimum Ca2+ concentration at 0.5 mM
Ca2+
-
optimum concentration at 1.0 mM
Ca2+
-
optimum concentration at 0.5 mM
Ca2+
-
maximal activity at 0.2 mM Ca2+
Ca2+
-
optimum Ca2+ concentration at 0.2 mM
Ca2+
Ca2+-dependent activity
Ca2+
-
required, optimal concentration varies with levels of the substrate
Ca2+
-
cation required, Ca2+ is most effective
Ca2+
-
required, optimal at about 0.05 mM
Ca2+
-
maximal activity at 0.6 mM
Ca2+
absolute requirement, maximal activity of recombinantly expressed full-length enzyme at 0.05 mM, maximal activity of recombinantly expressed catalytic module CM9-1 at 0.02 mM, maximal activity of recombinantly expressed catalytic module CM9-2 at 0.1 mM
Ca2+
strong activation, optimal activity at 0.05 mM CaCl2
Ca2+
-
PelC is dependent on Ca2+ for activity and stability
Ca2+
requires Ca2+, optimal activity with 0.25 mM
Ca2+
required, activates 5.8fold at 0.5 mM
Ca2+
0.1 mM, 180% of initial activity. Presence of Ca2+ enhances thermal stability
Ca2+
-
up to 1 mM, stimulation
Ca2+
Ca2+-dependent activity
Ca2+
-
required, best at 0.05 mM
Co2+
-
1 mM, 180% of initial activity
Co2+
5 mM, 138% of initial activity
Cu2+
5 mM, 122% of initial activity
Cu2+
activates 193% at 0.2 mM
Cu2+
activates 19% at 0.2 mM
Cu2+
activates slightly at 0.5 mM
Fe2+
-
1 mM, 126% of initial activity
Fe2+
-
1 mM, stimulates activity up to 592%
Fe2+
activates 213% at 0.2 mM
Fe2+
activates 231% at 0.2 mM
Fe2+
completely inactivates activity after incubation for 15 min
Fe2+
-
required for activity, optimal at 0.1 to 0.3mM
K+
19% activation at 0.5 mM
K+
-
9% activation at 1 mM
K+
activates slightly at 0.5-1 mM
Mg2+
-
1 mM, 226% of initial activity
Mg2+
-
1 mM, stimulates activity up to 368%
Mg2+
5 mM, 133% of initial activity
Mg2+
-
slightly enhances enzyme activity
Mg2+
activates 190% at 0.2 mM
Mg2+
the enzyme is activated 40% in the presence of MgCl2
Mg2+
slightly increases activity
Mg2+
1 mM, 144% of initial activity
Mg2+
-
can substitute for Ca2+ in activation. Optimal activity at 0.7 mM. Additive effect when any two metal ions (Mg2+, Ca2+, Mn2+) are present together
Mg2+
25% activation at 0.5 mM
Mg2+
-
41% of the activation with Ca2+
Mg2+
-
26% of the activation with Ca2+
Mg2+
activates slightly at 0.5 mM
Mn2+
-
1 mM, 268% of initial activity
Mn2+
-
1 mM, activity is enhanced by 1221%
Mn2+
5 mM, 116% of initial activity
Mn2+
activates 136% at 0.2 mM
Mn2+
-
restores activity of the EGTA-inactivated enzyme
Mn2+
1 mM, 143% of initial activity
Mn2+
-
optimal concentration: 0.1 mM
Mn2+
-
11% of the activation with Ca2+
Mn2+
-
can substitute for Ca2+ in activation. Optimal activity at 0.7 mM. Additive effect when any two metal ions (Mg2+, Ca2+, Mn2+) are present together
Mn2+
-
1 mM, enhances activity 6fold
Mn2+
-
27% of the activity with Ca2+
Mn2+
-
29% activation at 1 mM, 7.5% activation at 5 mM
Na+
decreases activity
Na+
-
10% activation at 1 mM
Ni2+
5 mM, 120% of initial activity
Ni2+
activates 191% at 0.2 mM
Sr2+
-
restores activity of the EGTA-inactivated enzyme
Sr2+
-
21% of the activation with Ca2+
Zn2+
-
1 mM, 202% of initial activity
Zn2+
5 mM, 145% of initial activity
Zn2+
activates 132% at 0.2 mM
Zn2+
16% activation at 0.5 mM
Zn2+
activates slightly at 0.5-1 mM
additional information
-
enzyme does not require Ca2+
additional information
-
no requirement of Ca2+
additional information
Fe2+ and Cu2+ do not significantly affect the activity of Pel-66
additional information
no or poor effect on the recombinant enzyme from Pichia pastoris by Sr2+, K+, and Li+
additional information
-
no or poor effect on the recombinant enzyme from Pichia pastoris by Sr2+, K+, and Li+
additional information
-
no activation by Ca2+, Co2+, Cu2+, Mg2+, Mn2+, Ni2+, Zn2+, or Ba2+,
additional information
Fe2+ and Ni2+ do not significantly affect the activity of Pel-90
additional information
-
Fe2+ and Ni2+ do not significantly affect the activity of Pel-90
additional information
-
divalent cations are required for maximum activity
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2,4,6-Trinitrobenzenesulfonate
-
1 mM, 73% inhibition
2-hydroxy-5-nitrophenyl bromide
-
-
4-hydroxymercuribenzoate
-
-
acetic acid
-
at 50 mM and above
ascorbic acid
-
48% loss of activity at 0.1 mM, complete inactivation at 1.0 mM
Butyric acid
-
at 200 mM and above
caffeic acid
-
42% inhibition at 0.01 mM, 67% inhibition at 0.05 mM
calcium-alginate
-
calcium-alginate concentration levels higher or lower 38.5 units/ml result in reduced enzyme activity
-
catechol
-
24% inhibition at 0.01 mM, 52% inhibition at 0.05 mM
chlorogenic acid
-
27% inhibition at 0.01 mM, 68% inhibition at 0.05 mM
Cinnamic acid
-
40% inhibition at 0.01 mM, 67% inhibition at 0.05 mM
ethylene glycol
-
at 50 mM and above
ferulic acid
-
15% inhibition at 0.01 mM, 58% inhibition at 0.05 mM
HgCl2
-
complete inactivation at 0.1 mM
Lactic acid
-
at 50 mM and above
Li+
-
5% activation at 1 mM, 62% inhibition at 5 mM
MnSO4
0.1 mM, 10% decrease in activity
p-coumaric acid
-
33% inhibition at 0.01 mM, 61% inhibition at 0.05 mM
PCMB
-
49% loss of activity at 0.01 mM, complete inactivation at 0.1 mM
polygalacturonic acid
-
at concentrations exceeding the Km-value
propionic acid
-
at 50 mM and above
Sodium metabisulfite
-
40% inactivation at 0.1 mM, 73% inactivation at 1 mM
ZnSO4
0.1 mM, 90% decrease in activity
2-mercaptoethanol
-
29% loss of activity at 1 mM, 67% loss of activity at 5 mM
2-mercaptoethanol
-
0.0022 mM, 50% inhibition
Ag+
-
1 mM, strong
Ag+
25% residual activity at 1 mM
Ba2+
-
strong inhibition
Ba2+
1 mM, 91% inhibition
Ba2+
38% inhibition at 0.2 mM
Ba2+
21% inhibition at 0.2 mM
Ba2+
causes a severe loss of activity, 88% inhibition at 0.5 mM, 97% at 1 mM
Ba2+
strong inhibition at 0.5-1 mM
Ca2+
Ca2+ does not increase but instead inhibits the activity of PelA, 41% residual activity at 1 mM
Ca2+
-
1 mM, strong inhibition of isoenzyme pelE
Ca2+
inhibitory above 1 mM
Cd2+
-
1 mM, no residual activity
Co2+
-
0.38 mM, 50% inhibition
Co2+
1 mM, 12% inhibition
Co2+
the enzyme is inhibited 30% in the presence of Co2+
Co2+
22% residual activity at 1 mM
Co2+
53% inhibition at 5 mM
Co2+
-
8% activation at 1 mM, 78.5% inhibition at 5 mM
Cr3+
-
inhibits completely at 1 mM
Cu2+
-
1 mM, 51% of initial activity
Cu2+
Aspergillus luchuensis var. saitoi
-
5.0 mM, 30-35% inhibition
Cu2+
-
1 mM, 91% inhibition
Cu2+
24% residual activity at 1 mM
Cu2+
93% inhibition at 5 mM
Cu2+
1 mM, 77% of initial activity
Cu2+
20% inhibition at 0.5 mM
Cu2+
-
11% activation at 1 mM, 41% inhibition at 5 mM
Cu2+
strong inhibition at 1 mM
dithiothreitol
-
27% loss of activity at 1 mM, 67% loss of activity at 5 mM
dithiothreitol
-
0.0104 mM, 50% inhibition
EDTA
-
complete inhibition
EDTA
-
1 mM, completely represses PelA enzyme activity
EDTA
5 mM, no residual activity
EDTA
-
0.09 mM, 50% inhibition
EDTA
-
1 mM, complete inhibition
EDTA
1 mM, in 50 mM Tris-HCl buffer, pH 7.5, 10 min at 30°C, complete inhibition, activity recovered by addition of 0.1 mM CaCl2
EDTA
-
activity is recovered by addition of Ca2+
EDTA
1 mM, pH 7.5, 10 min at 30°C, activity is completely abolished, fully recovered by adding 0.8 mM CaCl2
EDTA
5 mM EDTA causes complete loss of enzyme activity
EDTA
PelA is sensitive to 10 mM EDTA with 39% activity retained
EDTA
-
1 mM, 12% loss of activity
EDTA
complete inhibition at 5 mM
EDTA
1 mM, 17% of initial activity
EDTA
-
complete inhibition
EDTA
-
1 mM, enzyme from Alpine strain A15 loses 67% of initial activity, complete inactivation at 10 mM; 1 mM, enzyme from Siberian strain AG25 loses 85% of initial activity, complete inactivation at 10 mM
EDTA
complete inhibition at 0.5 mM
EDTA
-
complete inhibition at 2 mM
EDTA
-
inhibits activity with polygalacturonate, no inhibition of the ability to cleave protopectin of Boehmeria nivea
EDTA
-
inhibits completely at 1 mM
EDTA
3 mM, complete inhibition. Lyase activity can be restored by further addition of 5 mM CaCl2
EDTA
1 mM, 2% of initial activity
epicatechin
-
epicatechin may be involved in the resistance of unripe avocado fruits by inhibiting the pectate lyase activity of Colletotrichum gloeosporoides
Fe2+
5 mM, 46% of initial activity
Fe2+
18% inhibition at 0.5 mM, 43% at 1 mM
Fe2+
strong inhibition at 1 mM
Fe3+
Aspergillus luchuensis var. saitoi
-
5.0 mM, 30-35% inhibition
Fe3+
5 mM, 36% of initial activity
Fe3+
41% inhibition at 5 mM
Fe3+
-
4% inhibition at 1 mM, 99% inhibition at 5 mM
Hg2+
-
1 mM, no residual activity
Hg2+
5 mM, 40% of initial activity
Hg2+
1 mM, 23% inhibition
Hg2+
24% residual activity at 1 mM
Hg2+
complete inhibition at 5 mM
Mg2+
1 mM, 58% inhibition
Mg2+
56% residual activity at 1 mM
Mg2+
23% inhibition at 0.2 mM
Mg2+
64.5% inhibition at 5 mM
Mg2+
8.4% inhibition at 0.2 mM
Mg2+
-
9% activation at 1 mM, 22% inhibition at 5 mM
Mg2+
strong inhibition at 1 mM
Mn2+
-
strong inhibition
Mn2+
complete inhibition at 1 mM
Mn2+
94% inhibition at 0.2 mM
Mn2+
91.5% inhibition at 5 mM
Mn2+
weakly inhibits PelA activity at 1 mM
Mn2+
82% inhibition at 0.2 mM
Mn2+
25% inhibition at 0.5 mM, 43% at 1 mM
Mn2+
strong inhibition at 0.5-1 mM
N-bromosuccinimide
-
-
N-bromosuccinimide
-
0.1 mM, 32% inhibition
Ni2+
-
-
Ni2+
1 mM, 75% inhibition
Ni2+
the enzyme is inhibited 30% in the presence of Ni2+
Ni2+
67% residual activity at 1 mM
Ni2+
31% inhibition at 0.2 mM
Ni2+
18% inhibition at 5 mM
Ni2+
-
4% inhibition at 1 mM, 93% inhibition at 5 mM
Pb2+
53% residual activity at 1 mM
Pb2+
-
31% inhibition at 1 mM, complete inhibition at 5 mM
salicylic acid
-
-
salicylic acid
-
33% inhibition at 0.01 mM, 61% inhibition at 0.05 mM
SDS
0.1%, 3% of initial activity
SDS
PelA is sensitive to 0.1% (w/v) SDS with 43% activity retained
SDS
-
1%, strong inhibition
SDS
complete inhibition at 0.5%
SDS
-
strong inhibition of enzyme from Alpine strain A15; strong inhibition of enzyme from Siberian strain AG25
SDS
1 mM, 57% of initial activity
Se2+
18% inhibition at 0.2 mM
Se2+
10% inhibition at 0.2 mM
Sn2+
1 mM, 64% inhibition
Sn2+
75% residual activity at 1 mM
Sr2+
-
1 mM, weak
Sr2+
weakly inhibits PelA activity at 1 mM
Zn2+
Aspergillus luchuensis var. saitoi
-
5.0 mM, 30-35% inhibition
Zn2+
-
1 mM, 40% inhibition
Zn2+
-
2.8 mM, 50% inhibition
Zn2+
1 mM, 29% inhibition
Zn2+
the enzyme is inhibited 30% in the presence of Zn2+
Zn2+
69% residual activity at 1 mM
Zn2+
88% inhibition at 0.2 mM
Zn2+
63.5% inhibition at 5 mM
Zn2+
97% inhibition at 0.2 mM
Zn2+
-
13% activation at 1 mM, 46% inhibition at 5 mM
additional information
Aspergillus luchuensis var. saitoi
-
not inhibitory: 0.5% SDS, 5% Tween-20, 10% Triton X-100, 5% acetone, 20% ethanol, 10% isopropanol, and 10% methanol
-
additional information
no effect on activity is detected with KCl or NaCl
-
additional information
-
no effect on activity is detected with KCl or NaCl
-
additional information
-
Mg2+ and Zn2+ have no effect on Pel-15 activity
-
additional information
no or poor effect by Tween-80, methanol, ethanol, isopropyl alcohol at 0.5%
-
additional information
-
no or poor effect by Tween-80, methanol, ethanol, isopropyl alcohol at 0.5%
-
additional information
-
PelN is only weakly affected by the degree of pectin methyl esterification
-
additional information
-
not significantly inhibitory: 5 mM dithiothreitol, 2-mercaptoethanol, N-ethylmaleimide, monoiodo acetate, EDTA, and EGTA and 0.1 mM p-chloromercuribenzoate
-
additional information
Triton X-100 and Tween-20 have a negligible influence on the activity at 0.5-1.0 mM
-
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evolution
pectate lyase 2 sequence analysis and evolutionary analysis, overview
evolution
pectate lyase 2 sequence analysis and evolutionary analysis, overview
evolution
-
pectate lyase 2 sequence analysis and evolutionary analysis, overview
evolution
pectate lyase 2 sequence analysis and evolutionary analysis, overview
evolution
-
Dickeya dadantii pectate lyases belong to different families, namely, PL1, PL2, PL3, and PL9, PelN belongs to the PL9 family. The PelN orthologue is encoded by all of the sequenced genomes of the Dickeya and Pectobacterium species. The PelN structural model, constructed on the basis of the PelL structure, suggests that the PelL global topology and its catalytic amino acids are conserved in PelN. Notable differences concern the presence of additional loops at the PelN surface, and the replacement of PelL charged residues, involved in substrate binding, by aromatic residues in PelN
evolution
-
parallel beta-helix, active site residues, and substrate binding cleft are similar to those in the other pectate lyases from polysaccharide lyase family 1, PL1
evolution
-
PL-STR belongs to family PF00544
evolution
-
the enzyme belongs to family PF09492
evolution
the enzyme belongs to pectate lyase family 3
evolution
the enzyme belongs to te pectate lyase family
evolution
the enzyme belongs to the polysaccharide lyase family 1
evolution
-
the mature Apel is structurally related to the enzymes in the polysaccharide lyase family 1
evolution
-
parallel beta-helix, active site residues, and substrate binding cleft are similar to those in the other pectate lyases from polysaccharide lyase family 1, PL1
-
evolution
-
the enzyme belongs to family PF09492
-
evolution
-
the mature Apel is structurally related to the enzymes in the polysaccharide lyase family 1
-
malfunction
-
construction of CcpelA gene-disrupted mutants, the mutants show reduced aggressiveness towards tomato fruits and impaired pectate lyase secretion and extracellular activity, while overexpression of CcpelA in the Si-60 isolate increases its aggressiveness and PL secretion, overview
malfunction
-
type II secretion system-deficient mutant of Dickeya dadantii 3937, A1919, DELTA ouC, loses the capability to promote the multiplication of EDL933, whereas Ech159, DELTApoS, a stress-responsive sigma-factor RpoS-deficient mutant, increases EDL933 proliferation on lettuce leaves 2fold mor than the wild-type strain. Mutant A1919 is completely deficient in the secretion of pectate lyases, which play a major role in plant tissue maceration
malfunction
gene inactivation does not result in complete loss of pectate lyase activity, but the symptoms of anthracnose in the infected host plants are reduced
malfunction
-
no significant difference is detected after infection of potato tubers, but a weak decrease in the degree of maceration of chicory leaves is caused by the pelN mutant compared to the wild-type strain
malfunction
-
type II secretion system-deficient mutant of Dickeya dadantii 3937, A1919, DELTA ouC, loses the capability to promote the multiplication of EDL933, whereas Ech159, DELTApoS, a stress-responsive sigma-factor RpoS-deficient mutant, increases EDL933 proliferation on lettuce leaves 2fold mor than the wild-type strain. Mutant A1919 is completely deficient in the secretion of pectate lyases, which play a major role in plant tissue maceration
-
physiological function
PEL may play an important role in the process of normal fiber elongation in cotton
physiological function
pectate lyase 2 degrades the unesterified polygalacturonate pectate of the host cell wall
physiological function
pectate lyase 2 degrades the unesterified polygalacturonate pectate of the host cell wall
physiological function
-
pectate lyase 2 degrades the unesterified polygalacturonate pectate of the host cell wall
physiological function
pectate lyase 2 degrades the unesterified polygalacturonate pectate of the host cell wall
physiological function
-
pectate lyase is involved in cell wall hydrolysis and pulp softening during ripening fruits
physiological function
-
role of secreted pectate lyase, a cell wall-degrading enzyme, in the aggressiveness of Colletotrichum coccodes, overview
physiological function
-
the influence of the virulence mechanisms of Dickeya dadantii strain 3937, a broad-host-range phytopathogen, on the proliferation of the human pathogen Escherichia coli O157:H7 EDL933 on postharvest lettuce, strain 3937 promotes the multiplication of EDL933, overview
physiological function
the organism causes anthracnose in infected bean plants, pectate lyase encoded by the pecCl1 gene is an important determinant for the aggressiveness of Colletotrichum lindemuthianum
physiological function
activity is lost at low pH because protonation of aspartates results in the loss of the two catalytic calcium-ions causing a profound failure to correctly organise the Michaelis complex
physiological function
-
analysis of 30 pectate lyase-like genes in Populus trichocarpa. Most of the PL1 genes from subgroups Ia and Ib are highly expressed in xylem. Isoform PL1-18 from subgroup Ia is preferentially expressed in developing primary xylem and in xylem cells that are developing secondary walls. Overexpression of PL1-18 in poplar reduces plant growth and xylem development. Reduced secondary cell wall thickening and irregular xylem cells are observed in the transgenic trees, probably due to their lower pectin content
physiological function
-
downregulation of pectate lyase by antisense transformation leads to transgenicplants with fruits firmer than the control. The average molecular masses of transgenic pectins are higher than that of the control. The mean length values for chelated chains increases from 84 nm in the control to 95.5 nm in antisense samples. Sodium carbonate-soluble polyuronides are longer in transgenic fruits. Transgenic pectins show a more complex structure, with a higher percentage of branched chains than the control
physiological function
purified Pel1 triggers defense responses and confers resistance to Botrytis cinerea and Verticillium dahliae in tobacco and cotton plants. A mutant proterin lacking the enzymatic activity lacks functions to induce both cell death and plant resistance. Enzyme deletion strains severely compromise the virulence of Verticillium dahliae
physiological function
-
activity is lost at low pH because protonation of aspartates results in the loss of the two catalytic calcium-ions causing a profound failure to correctly organise the Michaelis complex
-
physiological function
-
pectate lyase is involved in cell wall hydrolysis and pulp softening during ripening fruits
-
physiological function
-
purified Pel1 triggers defense responses and confers resistance to Botrytis cinerea and Verticillium dahliae in tobacco and cotton plants. A mutant proterin lacking the enzymatic activity lacks functions to induce both cell death and plant resistance. Enzyme deletion strains severely compromise the virulence of Verticillium dahliae
-
physiological function
-
the influence of the virulence mechanisms of Dickeya dadantii strain 3937, a broad-host-range phytopathogen, on the proliferation of the human pathogen Escherichia coli O157:H7 EDL933 on postharvest lettuce, strain 3937 promotes the multiplication of EDL933, overview
-
additional information
-
implication of Bacillus sp. in the production of pectinolytic enzymes during cocoa fermentation
additional information
-
implication of Bacillus sp. in the production of pectinolytic enzymes during cocoa fermentation
additional information
-
implication of Bacillus sp. in the production of pectinolytic enzymes during cocoa fermentation
additional information
-
implication of Bacillus sp. in the production of pectinolytic enzymes during cocoa fermentation
additional information
-
implication of Bacillus sp. in the production of pectinolytic enzymes during cocoa fermentation
additional information
-
implication of Bacillus sp. in the production of pectinolytic enzymes during cocoa fermentation
additional information
-
RpoS, the general stress response sigma-factor involved in cell survival in suboptimal conditions, plays a role in EDL933 proliferation by controlling the production of pectate lyases in Dickeya dadantii 3937, e.g. via negative regulation of pelD promoter activity
additional information
-
the organism is the soft rot pathogen of calla lily growing around Kunming, soft rot is a major disease of calla lily, Zantedeschia spp., and other important crops worldwide. The pectate lyase contributes to the disease by tuber maceration cleaving structural pectic polymers, overview
additional information
invariant amino acids involved in catalytic function mainly comprised the catalytic residues R275, K244, and R280, and the Ca2+-binding residues D151, D173, and D177 in PelN
additional information
-
Pel structure modeling, overview
additional information
-
the enzyme from Xanthomonas campestris ACCC 10048 is a low-temperature-active alkaline pectate lyase
additional information
-
the PelN structural model, constructed on the basis of the PelL structure, suggests that the PelL global topology and its catalytic amino acids are conserved in PelN. Notable differences concern the presence of additional loops at the PelN surface, and the replacement of PelL charged residues, involved in substrate binding, by aromatic residues in PelN
additional information
-
the enzyme from Xanthomonas campestris ACCC 10048 is a low-temperature-active alkaline pectate lyase
-
additional information
-
Pel structure modeling, overview
-
additional information
-
the organism is the soft rot pathogen of calla lily growing around Kunming, soft rot is a major disease of calla lily, Zantedeschia spp., and other important crops worldwide. The pectate lyase contributes to the disease by tuber maceration cleaving structural pectic polymers, overview
-
additional information
-
RpoS, the general stress response sigma-factor involved in cell survival in suboptimal conditions, plays a role in EDL933 proliferation by controlling the production of pectate lyases in Dickeya dadantii 3937, e.g. via negative regulation of pelD promoter activity
-
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I140V
Aspergillus luchuensis var. saitoi
-
about 25% decrease in catalytic efficiency
V197D
Aspergillus luchuensis var. saitoi
-
about 25% decrease in catalytic efficiency
I140V
Aspergillus luchuensis var. saitoi KBN 2022
-
about 25% decrease in catalytic efficiency
-
V197D
Aspergillus luchuensis var. saitoi KBN 2022
-
about 25% decrease in catalytic efficiency
-
R227W
EDW21517
increase in expression and specific activity, no increase in thermostability
R227W/S145C/T206A
EDW21517
increase in specific activity and thermostability
R227W/S145C/T50T
EDW21517
increase in specific activity and thermostability
R227W/T206A/T222T
EDW21517
increase in specific activity and thermostability
R235A
site-directed mutagenesis, inactive catalytic residue mutant
R227W
-
increase in expression and specific activity, no increase in thermostability
-
R227W/S145C/T206A
-
increase in specific activity and thermostability
-
R227W/S145C/T50T
-
increase in specific activity and thermostability
-
R227W/T206A/T222T
-
increase in specific activity and thermostability
-
R235A
-
site-directed mutagenesis, inactive catalytic residue mutant
-
D106N
mutant enzyme without pectate lyase activity
D126N
the ratio of turnover number to Km-value is 57.5% of the wild-type value
D63N
mutant enzyme without pectate lyase activity
D80N
the ratio of turnover number to Km-value is 93% of the wild-type value
D84N
the ratio of turnover number to Km-value is 28.6% of the wild-type value
E38Q
mutant enzyme without pectate lyase activity
E47Q
mutant enzyme retains almost full activity relative to wild-type enzyme
E83Q
mutant enzyme without pectate lyase activity
H66A
the ratio of turnover number to Km-value is 70.4% of the wild-type value
K107A
mutant enzyme without pectate lyase activity
K107H
mutant enzyme without pectate lyase activity
K107R
mutant enzyme without pectate lyase activity
K129A
mutant enzyme without pectate lyase activity
K129H
mutant enzyme without pectate lyase activity
K129R
mutant enzyme is not produced extracellularly
K182A
mutant enzyme retains almost full activity relative to wild-type enzyme
K185A
mutant enzyme retains almost full activity relative to wild-type enzyme
K20A
mutant enzyme retains almost full activity relative to wild-type enzyme
K41A
the ratio of turnover number to Km-value is 105% of the wild-type value
K89A
the ratio of turnover number to Km-value is 31.5% of the wild-type value
R132A
mutant enzyme without pectate lyase activity
R132H
mutant enzyme without pectate lyase activity
R132K
mutant enzyme without pectate lyase activity
R152A
mutant enzyme retains almost full activity relative to wild-type enzyme
W78F
the ratio of turnover number to Km-value is identical to wild-type value
W78Y
mutant enzyme with slightly increased activity relative to wild-type enzyme
Y174A
the ratio of turnover number to Km-value is 90.7% of the wild-type value
D80N
-
the ratio of turnover number to Km-value is 93% of the wild-type value
-
D84N
-
the ratio of turnover number to Km-value is 28.6% of the wild-type value
-
K41A
-
the ratio of turnover number to Km-value is 105% of the wild-type value
-
K89A
-
the ratio of turnover number to Km-value is 31.5% of the wild-type value
-
E124I
mutant displays increased thermostability
E124I/T178A/N186D/I211V/A254T/S271G/N289H
140fold increase in the t50 value at 50°C, accompanied by an 84.3% decrease in activity
K313R
mutation does not improve thermostability
N186D/I211V/A254T/S271G/N289H
24fold increase in the t50 value at 50°C, with a 23.3% increase in activity
R72S
mutation does not improve thermostability
S233C
mutation does not improve thermostability
S271G
mutant displays increased thermostability
S308L
mutation does not improve thermostability
T178A
mutant displays increased thermostability
D173A
the mutation results in approximately 40% of wild type activity
D173A/N180A/K247A
the mutation results in approximately 0.2% of wild type activity
D173A/N180N
the mutation results in approximately 5% of wild type activity
K47D/V132F
2.2fold improvement in specific activity compared to wild-type
K47D/V132F/R272W
specific activity is significantly improved by about 400% in the presence of 1 mM Ca2+. Half-life at 50°C is extended to 330 min. Mutant can significantly improve the wettability and softness of fabrics
K47E
displays 1.8fold increase in activity, and half-life increased by 2.0fold at 50°C
K47E/V132F
3.9fold improvement in specific activity compared to wild-type
N180A
the mutation results in approximately 30% of wild type activity
V132F
mutant shows 1.7fold increase in activity with wider pH stability
K47D/V132F
-
2.2fold improvement in specific activity compared to wild-type
-
K47D/V132F/R272W
-
specific activity is significantly improved by about 400% in the presence of 1 mM Ca2+. Half-life at 50°C is extended to 330 min. Mutant can significantly improve the wettability and softness of fabrics
-
K47E
-
displays 1.8fold increase in activity, and half-life increased by 2.0fold at 50°C
-
K47E/V132F
-
3.9fold improvement in specific activity compared to wild-type
-
V132F
-
mutant shows 1.7fold increase in activity with wider pH stability
-
D107N
complete loss of activity, crystallization data
E84A
complete loss of activity
K108A
complete loss of activity, crystallization data
K108A/D107N
crystallization data
K108A/E39Q
crystallization data
K108A/Q111A
crystallization data
K108A/Q111N
crystallization data
K108A/R133A
crystallization data
D107N
-
complete loss of activity, crystallization data
-
E84A
-
complete loss of activity
-
K108A
-
complete loss of activity, crystallization data
-
K108A/E39Q
-
crystallization data
-
K108A/Q111A
-
crystallization data
-
D154E
-
mutant enzyme with 44% of the activity of the wild-type enzyme, the Km-value for the substrate lime pectin (with 75% methyl esterification) is 1.2fold higher than the Km-value of the wild-type enzyme
D154N
-
mutant enzyme with 44% of the activity of the wild-type enzyme, the Km-value for the substrate lime pectin (with 75% methyl esterification) is 2.3fold higher than the Km-value of the wild-type enzyme. The pH-optimum is higher than that of the wild-type enzyme
K224R
mutant is completely defective in lyase activity
K249R
mutant shows 40-60% of wild-type activity. At a higher Ca2+ concentration in the substrate medium, enzymatic activities of K249R and R252K mutants are less affected
K273A
-
inactive but correctly folded enzyme
N215S/T217S/S219G/A220S
-
the four residues in the T1.5 loop region of PelA are mutated to match the structurally analogous T1.5 loop of PelE. Mutant enzyme shows a conformational change in the T1.5 loop from PelA conformation to that observed in pelE. The pH-optimum of the mutant enzyme is identical to that of PelA, but the T1.5 mutant has an increased specific activity that is comparable to that of PelE
R218K
-
inactive mutant enzyme R218K. Crystals of mutant enzyme R218K are isomorphous with wild-type PelC crystals and belong to space group P2(1)2(1)2(1) with unit cell parameters of a = 72.14 A, b = 78.32 A and c = 94.43 A
R236K
-
mutant enzyme with 0.2% of the activity of the wild-type enzyme
R236Q
-
inactive mutant enzyme
R252K
mutant shows 6-9% of wild-type activity. At a higher Ca2+ concentration in the substrate medium, enzymatic activities of K249R and R252K mutants are less affected
N215S/T217S/S219G/A220S
-
the four residues in the T1.5 loop region of PelA are mutated to match the structurally analogous T1.5 loop of PelE. Mutant enzyme shows a conformational change in the T1.5 loop from PelA conformation to that observed in pelE. The pH-optimum of the mutant enzyme is identical to that of PelA, but the T1.5 mutant has an increased specific activity that is comparable to that of PelE
-
D174A
mutation in Ca2+ binding site, complete loss of activity
K93I
1.75fold increase in specific activity, folding free energy decreases by 1.03 kcal/ml
C132I/C156N/C194L
mutations increase expression level
D125
loss of catalytic activity
D147
loss of catalytic activity
D125
-
loss of catalytic activity
-
D147
-
loss of catalytic activity
-
N198A
95% of wild-type activity
N198D
77% of wild-type activity
N198Q
72% of wild-type activity
N95A
38% of wild-type activity
N95D
51% of wild-type activity
N95Q
54% of wild-type activity
N95S
81% of wild-type activity
additional information
chimeric enzyme composed of Ala1 to Tyr105 of Pel-15 in the N-terminal regions, Asp133 to Arg 159 of pectate lyase B from Fusarium solani in the internal regions, and Gln133 to Tyr197 of Pel-15 in the C-terminal regions: the ratio of turnover number to Km-value is 5.1% of the wild-type value
additional information
-
chimeric enzyme composed of Ala1 to Tyr105 of Pel-15 in the N-terminal regions, Asp133 to Arg 159 of pectate lyase B from Fusarium solani in the internal regions, and Gln133 to Tyr197 of Pel-15 in the C-terminal regions: the ratio of turnover number to Km-value is 5.1% of the wild-type value
-
additional information
-
construction of CcpelA gene-disrupted mutants, the mutants show reduced aggressiveness towards tomato fruits and impaired pectate lyase secretion and extracellular activity
additional information
-
regulation of pectate lyase secretion by knocking out PAC1, which encodes the PacC transcription factor that regulates gene products with pH-sensitive activities is studied. Loss-of-function PAC1 mutants show 85% reduction of PELB transcript expression, delayed pectate lyase secretion and dramatically reduced virulence, as detected in infection assays with avocado fruits. PELB is up-regulated in the presence of carbon sources. When glucose is used as a carbon source in the medium for the WT strain and the knock out pac1 mutant PELB transcript expression and PL secretion are activated
additional information
genetic inactivation, function of the pecCl1 gene is assessed using the genetic inactivation strategy known as split-marker, protoplast transformation, molecular phenotype, overview
additional information
-
genetic inactivation, function of the pecCl1 gene is assessed using the genetic inactivation strategy known as split-marker, protoplast transformation, molecular phenotype, overview
additional information
-
in a gacA deletion mutant the production of pectate lyase, protease, and cellulase is diminished in mutant cells compared with the wild-type cells
additional information
-
construction of mutants, type II secretion system-deficient mutant of Dickeya dadantii 3937, A1919, DELTA ouC, loses the capability to promote the multiplication of EDL933, whereas Ech159, DELTApoS, a stress-responsive sigma-factor RpoS-deficient mutant, increases EDL933 proliferation on lettuce leaves 2fold mor than the wild-type strain. Mutant A1919 is completely deficient in the secretion of pectate lyases, which play a major role in plant tissue maceration
additional information
-
construction of mutants, type II secretion system-deficient mutant of Dickeya dadantii 3937, A1919, DELTA ouC, loses the capability to promote the multiplication of EDL933, whereas Ech159, DELTApoS, a stress-responsive sigma-factor RpoS-deficient mutant, increases EDL933 proliferation on lettuce leaves 2fold mor than the wild-type strain. Mutant A1919 is completely deficient in the secretion of pectate lyases, which play a major role in plant tissue maceration
-
additional information
-
transgenic lines exhibiting a greater than 90% reduction in pectate lyase transcript abundance are generated. Wall extracts from transgenic fruits show a reduction in pectin solubility and decreased depolymerization of more tightly bound polyuronides. Additional patterns of differential extraction of other wall-associated pectin subclasses are apparent, particularly in the sodium carbonate and chelator-soluble polymers. Microscopic studies reveal that the typical ripening-associated loss of cell-cell adhesion is substantially reduced in the transgenic fruits
additional information
-
improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
additional information
-
improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
-
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30 - 40
inactivation of recombinant PL I occurs above 30°C whereas the activity of native PL I is stable up to 40°C
30 - 60
PelA is stable during 30°C to 40°C and not very stable at 50°C (in 50 mM glycine-NaOH buffer, pH 10.0), about 60% activity is retained after 30 min incubation at 50°C and it almost completely loses activity when it is incubated at 60°C
35 - 45
-
optimal stability
37 - 50
-
purified recombinant His-tagged enzyme, 45 min, without substrate, pH 9.0-12.0, over 80% activity remaining
39
-
transition midpoint of pectate lyase C is 38.9°C
40 - 70
the enzyme loses 60% of its activity when incubated at 40°C for 1 h after treatment with EDTA, thermostability increases to approximately 80% of initial activity at 50 and 70°C in the presence of Ca2+ alone and both Ca2+ and polygalacturonic acid, respectively
44
-
transition midpoint of pectate lyase C is 44.3°C
45 - 50
purified recombinant PelN displays a half-life of around 9 h and 42 h at 50°C and 45°C, respectively
47.9
melting temperature, mutant N198Q
48.7
melting temperature, mutant N198D
48.9
melting temperature, mutant N198A
50.7
melting temperature, mutant N95S
55 - 70
more than 80% of the original enzyme activity is retained in Tris-HCl buffers with pH 7 and 8, after incubation for 30 min
57
-
20 min, complete inactivation
60 - 95
-
the enzyme keeps stable, possesses a high level of activity at 60°C and a half-life of almost 2 h at 95°C
86
melting temperature, presence of 0.6 mM Ca2+
2
-
48 h, enzyme from Alpine strain A15 loses 21% of initial activity
2
-
48 h, enzyme from Siberian strain AG25 loses 5% of initial activity
30
-
half-life: more than 75 h
30
-
purified recombinant enzyme, pH 9.0, 2 h, over 90% activity remaining
30
Erwinia aroidea
-
pH 7.0-8.5, stable
30
-
pH 9.0, 15 min, enzyme from Alpine strain A15 loses 40% of initial activity
30
-
pH 9.0, 15 min, enzyme from Siberian strain AG25 loses 35% of initial activity
30
-
room temperature, activity is lost within 2 days
30
-
pH 6.0-9.0, 3 h, stable
37
-
pH 6.5-9.6, 2 h, stable
37
-
purified recombinant His-tagged enzyme, 1 h, without substrate, pH 12.0, over 58% activity remaining
37
-
purified recombinant His-tagged enzyme, 1 h, without substrate, pH 7.0-10.0, over 80% activity remaining
40
pH 10.0, 4 h, retains more than 50% of the initial activity
40
-
purified recombinant enzyme, pH 9.0, 2 h, over 80% activity remaining
40
-
pH 9.0, 15 min, enzyme from Alpine strain A15 loses 10% of initial activity
40
-
pH 9.0, 15 min, enzyme from Siberian strain AG25 loses 95% of initial activity
40
-
5 min, 5-10% loss of activity
40
purified recombinant His-tagged enzyme, half-life is 288 min at pH 10.0
40
-
3 h, 93% loss of activity without CaCl2, 14% loss of activity in presence of 0.1 mM CaCl2
40
-
pH 7.0, 10 min, stable below
40
1h, more than 60% residual activity
40 - 50
-
pH 6.0, 30 min, stable
40 - 50
2 h, 90% residual activity
45
-
pH 9.4: stable for 300 h. pH 10.0: about 40% loss of activity after 300 h
45
-
10 min, about 10% loss of activity
45
purified recombinant enzyme, 2 h, 64.9% activity remaining, half-life is 360 min
47
-
20 min, stable
47
-
transition midpoint of pectate lyase C is 46.9°C
50
-
half-life: 1 h
50
EDW21517
half-live of inactivation is 2.7 min for wild-type, 3.1 min for mutant R227W, 6.9 min for mutant R227W/S145C/T50T, 190.5 min for mutant R227W/T206A/T222T, 800.3 min for mutant R227W/S145C/T206A
50
-
30 min, stable up to
50
pH 10.0, 4 h, retains only 1% of the initial activity
50
time at which the enzyme loses 50% of its initial activity, i.e. t50 value, is 10 min for wild-type, 240 min for mutant N186D/I211V/A254T/S271G/N289H, 1400 min for mutant E124I/T178A/N186D/I211V/A254T/S271G/N289H, respectively
50
-
purified recombinant enzyme, 2 h, 90% activity remaining
50
half-life 55 min, recombinant protein
50
-
half life: 11 min for isoenzyme PelA, 4 min for isoenzyme PelD, 2 min for isoenzyme PelE
50
-
recombinant enzyme, 90 min, 50% activity remaining
50
Erwinia aroidea
-
10 min, 50% loss of activity
50
-
10 min, about 35% of maximal activity
50
purified recombinant His-tagged enzyme, stable up to for 3 h, half-lives at pH 7.0-11.0 are 327-103 min, half-life of 147 min at pH 10.0, overview
50
-
10 min, stable in absence of Ca2+
50
-
1 h, loss of activity
50
-
10 min, pH 7.0, 35% loss of activity
50
-
purified recombinant His-tagged enzyme, 45 min, without substrate, pH 10.0, over 80% activity remaining
50
purified recombinant enzyme, half-life is 88 min
52
-
20 min, 38% loss of activity
52
melting temperature, wild-type
55
-
stable up to, in absence of CaCl2
55
enzyme is stable to incubation up to 55°C when incubated at various temperatures for 20 min in glycine-NaOH buffer (pH 9.4)
55
-
10 min, about 80% of maximal activity
55
-
10 min, stable in presence of Ca2+
60
Aspergillus luchuensis var. saitoi
-
1 h, 71% residual activity
60
-
readily inactivated above
60
-
Ca2+ slightly enhances thermostability up to 60°C
60
pH 7.5, stable in presence of Ca2+
60
-
pH 9.0, 15 min, about 20% loss of activity
60
purified enzyme, 20 min, recombinant enzyme from Pichia pastoris retaines 26% activity, recombinant enzyme from Escherichia coli is inactivated
60
-
purified recombinant enzyme, pH 9.0, half-life is 20 min, inactivation after 80 min
60
-
half-life: 20-30 min for isoenzyme PelB and PelC, isoenzymes PelA, PelD and PelE loses more than 80% of activity after 2 min
60
-
10 min, 50% loss of activity in absence of cations, 10% loss of activity in presence of Mn2+, Ca2+ or polygalacturonic acid
60
-
30 min, more than 30% of the activity remains
60
purified recombinant His-tagged enzyme, half-life is 207 min at pH 10.0
60
-
purified native Pel1, half-life is 14.2 min at pH 7.0, 16.4 min at pH 9.0, the half-life is increased by Ca2+
60
-
purified recombinant His-tagged enzyme, 45 min, without substrate, pH 10.0, 30% activity remaining
65
-
half-life: 13 h
65
-
10 min, 50% loss of activity
70
-
half-life 18 h
70
Aspergillus luchuensis var. saitoi
-
1 h, 61% residual activity
70
-
beyond 70°C, enzyme activity is severely inhibited. The half-life is 6.93 min at 70°C as compared to 31 min at 40°C
70
-
pH 9.0, 15 min, 50% loss of activity
70
-
purified recombinant enzyme, pH 9.0, half-life is about 12 min, inactivation after 60 min
70
purified recombinant His-tagged enzyme, half-life is 120 min at pH 10.0
70
-
2 h, about 10% loss of activity
70
pH 7, 10 min, absence of substrate, stable
75
-
10 min, thermal denaturation is reversible
75
-
15 min, 60% residual activity
80
-
half-life 12 h
80
Aspergillus luchuensis var. saitoi
-
1 h, 46% residual activity
80
-
half-life at pH 8.0 and 7.0 is 1.2 min, half-life at pH 9.0 is 0.8 min
80
-
5 min, complete inactivation
80
-
half-life: about 60 min
90
-
half-life 7 h
90
-
half-life of pectate lyase is 60fold higher in the presence of hydroxyapatite nanoparticles than in the presence of 1 mM CaCl2. Thermodynamic analysis of the nanoparticle-induced stability reveals an enhanced entropy-enthalpy compensation by hydroxyapatite nanoparticles since a reciprocal linearity of the enthalpy-entropy change to 90°C is observed
90
-
complete loss of activity after 5 min
additional information
-
Ca2+ slightly enhances thermal stability
additional information
Ca2+ increases thermal stability of the enzyme slightly
additional information
-
Ca2+ increases thermal stability of the enzyme slightly
additional information
-
thermal denaturation is not reversible. The enzyme has its maximal thermal stability at pH 5, CD-monitored thermal denaturation
additional information
-
improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
additional information
-
Ca2+ and sodium polygalacturonate improve thermal stability
additional information
-
Ca2+ slightly enhances thermal stability
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