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Information on EC 4.2.2.2 - pectate lyase
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4.2.2.2 pectate lyaseIUBMB Comments
Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase).
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Word Map
- 4.2.2.2
- erwinia
- chrysanthemi
- lyases
- polygalacturonase
- carotovora
-
macer
- cellulase
-
pectinolytic
-
phytopathogenic
- pectinases
-
soft-rotting
-
degumming
-
beta-helix
-
softening
- polypectate
- atroseptica
-
methylesterase
- xylanase
-
wall-degrading
-
4,5-unsaturated
-
pectin-degrading
- oligogalacturonates
- digalacturonate
- pectinesterase
-
plant-parasitic
-
enterobacterium
- ramie
- viridiflava
- pectobacterium
- dickeya
- gloeosporioides
- harpins
- dadantii
- homogalacturonan
- agriculture
-
de-esterified
- food industry
- degradation
- industry
- biotechnology
- environmental protection
- molecular biology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
alkaline pectate lyase, alkaline polygalacturonate lyase, alpha-1,4-D-endopolygalacturonic acid lyase, Apel, Athe_1854, AtPLL, Bsp165PelA, BxPEL1, BxPEL2, C0W65_13990, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkaline pectate lyase
alpha-1,4-D-endopolygalacturonic acid lyase
-
-
-
-
Apel
Athe_1854
Bsp165PelA
C0W65_13990
Calkro_0863
Cthe_2179
DKS1 pectate lyase
EC 4.2.99.3
-
-
-
-
endo-alpha-1,4-polygalacturonic acid lyase
-
-
-
-
endo-polygalacturonate trans-eliminase
endogalacturonate transeliminase
-
-
-
-
endopectin methyltranseliminase
-
-
-
-
Gr-PEL2
lyase, pectate
-
-
-
-
NPLase
PATE
pectate lyase
pectate lyase 2
pectate lyase 9A
pectate lyase A
pectate lyase B
pectate lyase C
pectate lyase E
pectate lyase PL 47
pectate transeliminase
pectic acid lyase
-
-
-
-
pectic acid transeliminase
-
-
-
-
pectic lyase
Pel
Pel I
Pel II
Pel III
Pel SWU
Pel-15
Pel-15E
Pel-15H
pel-2
Pel-20
Pel-22
Pel-66
Pel-BL11
Pel1
PEL168
Pel9A
PelA
PelB
pelC
PelI
PelN
PGA lyase
-
-
-
-
PL
PL D
PL I
PL1B
Pla
-
-
-
-
PLB
PLC
PLE
poly(1,4-alpha-D-galacturonide) lyase
-
-
-
-
poly-galacturonic acid trans-eliminase
polygalacturonate lyase
-
-
-
-
polygalacturonic acid lyase
-
-
-
-
polygalacturonic transeliminase
-
-
-
-
PPase-N
-
-
-
-
additional information
pectate transeliminase
-
-
-
-
pectic lyase
-
-
-
-
PLB
-
-
-
-
PLC
-
-
-
-
additional information
the enzyme belongs to the polysaccharide family 1
additional information
the enzyme belongs to the polysaccharide family 1
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-galacturonan lyase
Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase).
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CAS REGISTRY NUMBER
COMMENTARY
9015-75-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
apple pectin
unsaturated digalacturonic acid + unsaturated trigalacturonic acid
A0A1B1LZ58
-
-
-
?
citrus pectin
unsaturated digalacturonic acid + unsaturated trigalacturonic acid
A0A1B1LZ58
-
-
-
?
de-esterified pectin
4,5-unsaturated oligogalacturonates
Q4JLV6
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
-
?
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
-
?
pentagalacturonic acid
saturated digalacturonic acid + unsaturated trigalacturonic acid + saturated trigalacturonic acid + unsaturated digalacturonic acid
polygalacturonate
unsaturated digalacturonic acid + unsaturated trigalacturonic acid
A0A1B1LZ58
-
-
-
?
polygalacturonate
unsaturated trigalacturonate + unsaturated oligogalacturonates
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
major product
-
?
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
-
-
?
reduced tetragalacturonic acid
galacturonic acid + reduced trigalacturonic acid
-
-
-
?
tetragalacturonic acid
altered trigalacturonic acid + digalacturonic acid + altered digalacturionic acid + D-galacturonic acid
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 peel pectin
unsaturated oligogalacturonides
Aspergillus luchuensis var. saitoi
-
-
-
-
?
citrus peel pectin
unsaturated oligogalacturonides
Aspergillus luchuensis var. saitoi KBN 2022
-
-
-
-
?
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
?
-
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
?
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 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
?
-
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
?
Bacillus sp. (in: Bacteria) KSM-P15
with degrees of esterification of 31%, 63% and 94% is degraded with 103%, 84% and 46% of the activity with polygalacturonic acid
-
?
pectin
?
Bacillus sp. (in: Bacteria) KSM-P15
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
?
-
unlike other isoenzymes, pectate lyase requires partially methyl esterified pectin as substrate
-
-
?
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
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
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 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
EDW21517
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
Bacillus sp. (in: Bacteria) KSM-P15
-
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
-
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
-
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
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
polygalacturonate
unsaturated oligogalacturonides
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
-
?
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
?
Arg235 is an essential catalytic residue
-
-
?
polygalacturonic acid
?
Arg235 is an essential catalytic residue
-
-
?
polygalacturonic acid
?
degradation through an endo-type fashion
-
?
polygalacturonic acid
?
Bacillus sp. (in: Bacteria) KSM-P15
degradation through an endo-type fashion
-
?
polygalacturonic acid
?
the recombinant enzyme shows highest activity on polygalacturonic acid and lower activity on more highly methylated pectin
-
-
?
polygalacturonic acid
?
-
Arg initiates proton abstration during the beta elimination cleavage of 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
?
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
unsaturated galacturonate
-
-
-
?
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
Bacillus sp. (in: Bacteria) KSM-P15
-
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
-
-
-
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
-
-
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
-
endo-cleavage
-
-
?
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
-
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 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
-
-
-
?
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
-
-
?
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
?
-
A0A1B1LZ58
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
?
-
PelA does not show any activity on mannan, CMC, xylan, glucan, or soluble starch
-
-
-
additional information
?
-
Bacillus sp. (in: Bacteria) KSM-P15
-
protopectinase-like activity on cotton fibers
-
-
-
additional information
?
-
PelA does not show any activity on mannan, CMC, xylan, glucan, or soluble starch
-
-
-
additional information
?
-
-
enzyme production is repressed by glucose
-
-
-
additional information
?
-
-
digalacturonate is not cleaved at an appreciable rate
-
-
-
additional information
?
-
D8X180
substrates are 45% methylated pectin or polygalacturonate
-
-
-
additional information
?
-
-
substrates are 45% methylated pectin or polygalacturonate
-
-
-
additional information
?
-
D8X180
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
Georgenia muralis JAM 3H7-3
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
-
-
enzyme production is repressed by glucose
-
-
-
additional information
?
-
-
the enzyme plays an important role in plant-nematode interactions
-
-
-
additional information
?
-
Q33CQ4
the enzyme plays an important role in plant-nematode interactions
-
-
-
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
?
-
Q8J254
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
?
-
-
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 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
?
-
-
the Gr-PEL2 protein is capable of inducing profound changes in the plant morphology, not related to tissue maceration or soft rot
-
-
-
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
?
-
Q9WYR4
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Cu2+
Fe2+
K+
Mg2+
Mn2+
Na+
Ni2+
Sr2+
Zn2+
additional information
Ba2+
the enzyme is activated slightly in the presence of BaCl2
Ca2+
-
1 mM, 306% of initial activity. Presence of Ca2+ enhances thermoactivity and thermostability
Ca2+
strong sigmoidal CaCl2 concentration dependent relation. Optimal catalysis at 0.5-1.0 mM Ca2+
Ca2+
A0A1B1LZ58
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+
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+
Ca2+ is not required for activity on pectic substrates
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+
required, activates the recombinant enzyme from Pichia pastoris by 26%
Ca2+
-
activity of wild-type peaks at 1 mM Ca2+, and declines with the increase in Ca2+concentration
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+
presence of Ca2+ stimulates a change in tertiary structure. Binding of Ca2+ and polygalacturonic acid to the active site may occur independently
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+
-
both pectate lyase I and II require 0.2 mM Ca2+ for maximal activity
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; optimum concentration at 0.6 mM
Ca2+
-
optimum concentration at 1.0 mM, Ca2+ cannot be replaced by Ba2+, Be2+, Sr2+, Mg2+, and monovalent cations for Pel activity
Ca2+
-
enzyme from Alpine strain A15 completely loses activity in absence of 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+
activates optimally at 0-2.5 mM; activates optimally at 0-2.5 mM
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+
-
0.5 mM, 7fold activation of pectate lyase I, 4fold activation of pectate lyase II
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+
-
required, optimal concentration varies with levels of the substrate
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+
0.1 mM, 180% of initial activity. Presence of Ca2+ enhances thermal stability
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
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
additional information
D8X180
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 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
48% loss of activity at 0.1 mM, complete inactivation at 1.0 mM
calcium-alginate
-
calcium-alginate concentration levels higher or lower 38.5 units/ml result in reduced enzyme activity
-
2-mercaptoethanol
-
29% loss of activity at 1 mM, 67% loss of activity at 5 mM
Ba2+
causes a severe loss of activity, 88% inhibtion at 0.5 mM, 97% at 1 mM
Ca2+
Ca2+ does not increase but instead inhibits the activity of PelA, 41% residual activity at 1 mM
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
1 mM, pH 7.5, 10 min at 30°C, activity is completely abolished, fully recovered by adding 0.8 mM CaCl2
EDTA
PelA is sensitive to 10 mM EDTA with 39% activity retained
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
-
inhibits activity with polygalacturonate, no inhibition of the ability to cleave protopectin of Boehmeria nivea
EDTA
3 mM, complete inhibition. Lyase activity can be restored by further addition of 5 mM CaCl2
epicatechin
-
epicatechin may be involved in the resistance of unripe avocado fruits by inhibiting the pectate lyase activity of Colletotrichum gloeosporoides
Mn2+
weakly inhibits PelA activity at 1 mM
SDS
PelA is sensitive to 0.1% (w/v) SDS with 43% activity retained
SDS
-
strong inhibition of enzyme from Alpine strain A15; strong inhibition of enzyme from Siberian strain AG25
Sr2+
weakly inhibits PelA activity at 1 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
-
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
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tris-HCl buffer
enzyme activity increases with increasing concentration of the buffer (20 mM to 1 M) and has highest activity at 1 M
additional information
-
activity of pectate lyase is 9fold higher at 90°C in the presence of hydroxyapatite nanoparticles than in the presence of 1 mM CaCl2
-
additional information
no or poor effect by Tween-80, methanol, ethanol, isopropyl alcohol at 0.5%
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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apple pectin
Aspergillus luchuensis var. saitoi
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Km value of wild-type, 1.12 mg/ml, of mutant I140V 0.97 mg/ml, of mutant V197D 1.00 mg/ml, respectively, pH 8.0, 30°C
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apple pectin
A0A1B1LZ58
Km value 0.42 mg/ml, pH 10.5, 70°C
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citrus pectin
A0A1B1LZ58
Km value 0.45 mg/ml, pH 10.5, 70°C
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citrus peel pectin
Aspergillus luchuensis var. saitoi
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Km value of wild-type, 0.97 mg/ml, of mutant I140V 0.93 mg/ml, of mutant V197D 0.91 mg/ml, respectively, pH 8.0, 30°C
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Km for acid soluble polygalacturonic acid: 0.051%
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Km for poly-D-galacturonic acid: 0.040-0.070 mg/ml
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the Km-value for pectin increases 30000fold as the percent esterification of the substrate increases from 0 to 60%
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Km for citrus pectin: 5.0 g/l; Km for pectate: 0.5 g/l
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Km for polypectate: 0.11%
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Km for polygalacturonic acid: 0.862 g/l
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Km for polygalacturonic acid: 16%
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Km for polygalacturonic acid: 0.134 mg/ml
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Km for polygalacturonate: 0.019 g/l
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Km-values: 0.104 mg/ml for polygalacturonic acid, 0.131 mg/ml for esterified citrus pectin, 1.837 mg/ml for 67% esterified citrus pectin, 1.837 mg/ml for 89% esterified citrus pectin
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Km-value for polygalacturonic acid is 0.85 mg/ml
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KM-values for wild-type and mutant enzymes for polygalacturonic acid: 1.87 g/l for wild-type enzyme, 1.55 g/l for mutant enzyme K41A, 1.9 g/l for mutant enzyme H66A, 2.07 g/l for mutant enzyme W78F, 1.78 g/l for mutant enzyme D80N, 1.6 g/l for mutant enzyme D84N, 1.42 g/l for mutant enzyme K89A, 1.34 g/l for mutant enzyme D126N, 1.86 g/l for mutant enzyme Y174A, 1.55 g/l for the 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
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Km-value for lime pectin with 75% methyl esterification: 6.3 mg/ml for wild-type enzyme, 7.8 mg/ml for mutant enzyme D154E, 14.8 mg/ml for mutant enzyme D154N, at 30°C and pH 8.5
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KM-value for polygalacturonate is 0.24 g/l, at pH 7.8, 50°C. KM-value is 0.24 g/l for not esterified pectin, 0.36 g/l for pectin with 5.3% esterification, 0.35 g/l for pectin with 29.5% esterification, 1.34 g/l for pectin with 51.4% esterification
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KM-value is 0.13 mg/ml for 22% esterified pectin, the KM-value is 0.15 mg/ml for polygalacturonic acid
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KM-value for polygalacturonate is 0.4 g/l in presence of 0.7 mM Ca2+, KM-value for polygalacturonate is 0.32 g/l in presence of 0.7 mM Mg2+, KM-value for polygalacturonate is 0.45 g/l in presence of 0.7 mM Ca2+ + 0.7 mM Mg2+, KM-value for citrus pectin (7.2% methylation) is 0.77 g/l
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Km of 0.50 mg/ml for polygalacturonic acid
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values of Km (polygalacturonic acid) is 0.44 mg/ml
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enzyme kinetics and thermodynamics at 75°C and 90°C in presence or absence of hydroxyapatite nanoparticles, detailed overview
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