Information on EC 4.2.2.2 - pectate lyase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
4.2.2.2
-
RECOMMENDED NAME
GeneOntology No.
pectate lyase
-
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pentose and glucuronate interconversions
-
-
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).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alkaline pectate lyase
-
-
alkaline pectate lyase
-
alkaline pectate lyase
Bacillus subtilis 168
-
-
alkaline pectate lyase
Bacillus subtilis TCCC11286, Bacillus subtilis WSHB04-02
-
-
-
alkaline pectate lyase
-
alkaline pectate lyase
-
-
alkaline pectate lyase
Xanthomonas campestris ACCC 10048
-
-
-
alkaline polygalacturonate lyase
-
-
alpha-1,4-D-endopolygalacturonic acid lyase
-
-
-
-
Apel
Bacillus subtilis TCCC11286
-
-
-
Bsp165PelA
-
-
Bsp165PelA
-
-
-
DKS1 pectate lyase
-
DKS1 pectate lyase
Bacillus pumilus DKS1
-
-
EC 4.2.99.3
-
-
-
-
endo-alpha-1,4-polygalacturonic acid lyase
-
-
-
-
endo-polygalacturonate trans-eliminase
-
-
endo-polygalacturonate trans-eliminase
Bacillus sp. TS 47
-
-
-
endogalacturonate transeliminase
-
-
-
-
endopectin methyltranseliminase
-
-
-
-
lyase, pectate
-
-
-
-
neutral-alkaline pectate lyase
-
-
NPLase
-
-
-
PATE
Pectobacterium carotovorum IFO3830
-
-
-
pectate lyase
-
-
pectate lyase
-
-
pectate lyase
-
pectate lyase
-
-
pectate lyase
-
pectate lyase
-
-
pectate lyase
-
-
pectate lyase
-
-
pectate lyase
-
-
pectate lyase
-
pectate lyase
-
-
pectate lyase
-
pectate lyase 10A
-
-
pectate lyase 2
-
-
pectate lyase 2
-
pectate lyase 2
-
pectate lyase 9A
Clostridium stercorarium
-
pectate lyase 9A
Clostridium stercorarium F-9
-
-
pectate lyase A
-
pectate lyase A
Aspergillus nidulans GR5
-
-
pectate lyase A
-
-
pectate lyase A
-
-
pectate lyase A
Dickeya chrysanthemi EC16
-
;
-
pectate lyase B
-
-
pectate lyase B
Dickeya chrysanthemi EC16
-
-
-
pectate lyase C
-
-
pectate lyase C
-
-
pectate lyase C
Dickeya chrysanthemi EC16
-
-
-
pectate lyase C
-
-
pectate lyase E
-
pectate lyase E
-
-
pectate lyase E
-
-
pectate lyase L
-
-
pectate lyase Pel10A
-
-
pectate lyase Pel9A
-
-
pectate lyase PL 47
-
-
pectate lyase PL 47
Bacillus sp. TS 47
-
-
-
pectate transeliminase
-
-
-
-
pectate transeliminase
-
pectate transeliminase
-
pectate transeliminase
-
-
pectate transeliminase
-
-
pectate transeliminase
Bacillus subtilis TCCC11286
-
-
-
pectic acid lyase
-
-
-
-
pectic acid transeliminase
-
-
-
-
pectic lyase
-
-
-
-
pectic lyase
-
-
Pel
Bacillus sp. P4-N, Bacillus sp. TS 47
-
-
-
Pel
Bacillus subtilis 168, Bacillus subtilis SO113, Bacillus subtilis TCCC11286
-
-
-
Pel I
Aspergillus niger MIUG 16
-
-
-
Pel II
Aspergillus niger MIUG 16
-
-
-
Pel III
Aspergillus niger MIUG 16
-
-
-
Pel SWU
-
-
Pel-15
-
-
Pel-15
Bacillus sp. P4-N, Bacillus sp. TS 47
-
-
-
Pel-22
Bacillus pumilus BS22
-
-
Pel-66
Bacillus subtilis BS66
-
-
Pel-BL11
Paenibacillus campinasensis BL11
-
-
Pel1
Penicillium occitanis CT1
-
-
-
PEL168
gene name
PEL168
Bacillus subtilis 168
gene name
-
Pel9A
Clostridium stercorarium
-
-
PelA
Aspergillus nidulans GR5
-
-
PelA
Bacillus pumilus BK2
-
-
-
PelA
-
-
PelA
Bacillus sp. P4-N, Bacillus sp. TS 47
-
-
-
PelA
Bacillus subtilis 168, Bacillus subtilis SO113
-
-
-
PelA
-
isoform
PelA
Dickeya chrysanthemi EC16
-
-
-
PelA
Paenibacillus amylolyticus 27C64
-
-
PelA
Streptomyces thermocarboxydus B1
-
-
PelB
Paenibacillus amylolyticus 27C64
-
-
PelE
-
isoform
PGA lyase
-
-
-
-
PL
Bacillus sp. TS 47
-
-
-
PL D
Xanthomonas campestris ACCC 10048
-
-
-
PL I
an endo-acting family 3 pectate lyase
PL I
Streptomyces thermocarboxydus B1
an endo-acting family 3 pectate lyase
-
PL-STR
-
gene name
Pla
-
-
-
-
PLB
-
-
-
-
PLB
Dickeya chrysanthemi EC16
-
-
-
PLC
-
-
-
-
PLC
Dickeya chrysanthemi EC16
-
-
-
PLE
Dickeya chrysanthemi EC16
-
-
-
poly(1,4-alpha-D-galacturonide) lyase
-
-
-
-
poly-galacturonic acid trans-eliminase
-
-
poly-galacturonic acid trans-eliminase
Pectobacterium carotovorum IFO3830
-
-
-
polygalacturonate lyase
-
-
-
-
polygalacturonic acid lyase
-
-
-
-
polygalacturonic transeliminase
-
-
-
-
PPase-N
-
-
-
-
additional information
the enzyme belongs to the polysaccharide family 1
additional information
Bacillus pumilus DKS1
the enzyme belongs to the polysaccharide family 1
-
CAS REGISTRY NUMBER
COMMENTARY
9015-75-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
L. Heynh. ecotype Columbia
-
-
Manually annotated by BRENDA team
strain MIUG 16
-
-
Manually annotated by BRENDA team
Aspergillus niger MIUG 16
strain MIUG 16
-
-
Manually annotated by BRENDA team
Bacillus megaterium AK2
-
-
-
Manually annotated by BRENDA team
gene pelB
UniProt
Manually annotated by BRENDA team
isolated from fermenting cocoa beans
UniProt
Manually annotated by BRENDA team
strain DKS1
-
-
Manually annotated by BRENDA team
Bacillus pumilus BK2
strain BK2
-
-
Manually annotated by BRENDA team
Bacillus pumilus BS22
isolated from fermenting cocoa beans
UniProt
Manually annotated by BRENDA team
Bacillus pumilus DKS1
gene pelB
UniProt
Manually annotated by BRENDA team
Bacillus pumilus DKS1
strain DKS1
-
-
Manually annotated by BRENDA team
an endo-pectate lyase produced by a genetically modified Bacillus sp. is used
-
-
Manually annotated by BRENDA team
BP-23
SwissProt
Manually annotated by BRENDA team
KSM-P15
Swissprot
Manually annotated by BRENDA team
strain BP-7
-
-
Manually annotated by BRENDA team
strain KSM-P15
-
-
Manually annotated by BRENDA team
strain KSM-P15
SwissProt
Manually annotated by BRENDA team
strain KSM-P15
Swissprot
Manually annotated by BRENDA team
strain KSM-P15; strain P4-N; strain TS 47
-
-
Manually annotated by BRENDA team
strain KSM-P7
-
-
Manually annotated by BRENDA team
strain N16-5
UniProt
Manually annotated by BRENDA team
strain RN1
UniProt
Manually annotated by BRENDA team
Bacillus sp. BP-23
BP-23
SwissProt
Manually annotated by BRENDA team
strain BP-7
-
-
Manually annotated by BRENDA team
KSM-P15
Swissprot
Manually annotated by BRENDA team
strain KSM-P15
SwissProt
Manually annotated by BRENDA team
strain KSM-P15
Swissprot
Manually annotated by BRENDA team
Bacillus sp. KSM-P7
strain KSM-P7
-
-
Manually annotated by BRENDA team
strain N16-5
UniProt
Manually annotated by BRENDA team
Bacillus sp. P4-N
strain P4-N
-
-
Manually annotated by BRENDA team
Bacillus sp. RK9
RK9
-
-
Manually annotated by BRENDA team
strain RN1
UniProt
Manually annotated by BRENDA team
Bacillus sp. TS 47
strain TS 47
-
-
Manually annotated by BRENDA team
Bacillus sp. TS 47
TS 47
-
-
Manually annotated by BRENDA team
gene pel168
UniProt
Manually annotated by BRENDA team
IFO 3134
-
-
Manually annotated by BRENDA team
isolated from fermenting cocoa beans
UniProt
Manually annotated by BRENDA team
isolated from soil of a saline-alkaline field in Tianjin, China, gene Bsu11286Pel
-
-
Manually annotated by BRENDA team
strain 168; strain SO113
-
-
Manually annotated by BRENDA team
strain WSHB04-02
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
gene pel168
UniProt
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
-
-
Manually annotated by BRENDA team
Bacillus subtilis BS66
isolated from fermenting cocoa beans
UniProt
Manually annotated by BRENDA team
Bacillus subtilis IFO3134
IFO3134
-
-
Manually annotated by BRENDA team
Bacillus subtilis SO113
SO113
-
-
Manually annotated by BRENDA team
Bacillus subtilis SO113
strain SO113
-
-
Manually annotated by BRENDA team
Bacillus subtilis TCCC11286
isolated from soil of a saline-alkaline field in Tianjin, China, gene Bsu11286Pel
-
-
Manually annotated by BRENDA team
Bacillus subtilis WSHB04-02
strain WSHB04-02
-
-
Manually annotated by BRENDA team
; pectate lyase precursor
SwissProt
Manually annotated by BRENDA team
Clostridium stercorarium
-
SwissProt
Manually annotated by BRENDA team
Clostridium stercorarium
strain F-9
SwissProt
Manually annotated by BRENDA team
Clostridium stercorarium F-9
strain F-9
SwissProt
Manually annotated by BRENDA team
single copy gene pecCl1
UniProt
Manually annotated by BRENDA team
3937; 5 isoenzymes: PelA, PelB, PelD, PelI and PelL
-
-
Manually annotated by BRENDA team
3937; at least 7 isoenzymes, 5 major isoenzymes, PelA, PelB, PelC, PelD, Pel E and two minor isoenzyme PelL and PelZ
-
-
Manually annotated by BRENDA team
5 isoenzymes: PelA, PelB, PelC, PelD, PelE
-
-
Manually annotated by BRENDA team
at least 4 isoenzymes
-
-
Manually annotated by BRENDA team
isoform PelB
UniProt
Manually annotated by BRENDA team
isoform PelC
UniProt
Manually annotated by BRENDA team
isoform PelD
UniProt
Manually annotated by BRENDA team
Dickeya chrysanthemi 3937
3937
-
-
Manually annotated by BRENDA team
Dickeya chrysanthemi EC16
EC16
-
-
Manually annotated by BRENDA team
gene pelN
-
-
Manually annotated by BRENDA team
nine pel genes, pelA to pelE, pelI, pelL, pelX, and pelZ
-
-
Manually annotated by BRENDA team
nine pel genes, pelA to pelE, pelI, pelL, pelX, and pelZ
-
-
Manually annotated by BRENDA team
Erwinia aroidea
-
-
-
Manually annotated by BRENDA team
cultivar Chandler
-
-
Manually annotated by BRENDA team
f. sp. lycopersici
-
-
Manually annotated by BRENDA team
f. sp. pisi
-
-
Manually annotated by BRENDA team
f. sp. pisi; Nectria haematococca mating type VI; pectate lyase B
-
-
Manually annotated by BRENDA team
f. sp. pisi; Nectria haematococca mating type VI; pectate lyase C
-
-
Manually annotated by BRENDA team
f. sp. pisi; Nectria haematococca mating type VI; pectate lyase D
-
-
Manually annotated by BRENDA team
strain NCIM 1276
-
-
Manually annotated by BRENDA team
Fusarium verticillioides NCIM 1276
strain NCIM 1276
-
-
Manually annotated by BRENDA team
gene pel-2
-
-
Manually annotated by BRENDA team
gene pel-2
UniProt
Manually annotated by BRENDA team
subsp. tabacum, gene pel-2
UniProt
Manually annotated by BRENDA team
variant acc 7235
UniProt
Manually annotated by BRENDA team
strain D32
-
-
Manually annotated by BRENDA team
Lachnospira multipara D32
strain D32
-
-
Manually annotated by BRENDA team
Lysinibacillus fusiformis, isolated from fermenting cocoa beans
UniProt
Manually annotated by BRENDA team
Alpine strain A15; Siberian strain AG25
-
-
Manually annotated by BRENDA team
strain Harichhal
-
-
Manually annotated by BRENDA team
Musa acuminata Harichhal
strain Harichhal
-
-
Manually annotated by BRENDA team
Musa acuminata Nangka
-
-
-
Manually annotated by BRENDA team
PelA; gene pelA
UniProt
Manually annotated by BRENDA team
Paenibacillus amylolyticus 27C64
gene pelB
UniProt
Manually annotated by BRENDA team
Paenibacillus amylolyticus 27C64
PelA; gene pelA
UniProt
Manually annotated by BRENDA team
Paenibacillus campinasensis BL11
-
UniProt
Manually annotated by BRENDA team
gene pelN
UniProt
Manually annotated by BRENDA team
strain BP-23
-
-
Manually annotated by BRENDA team
Paenibacillus sp. BP-23
strain BP-23
-
-
Manually annotated by BRENDA team
3 isoenzymes; subsp. atroseptica, 3 isoenzymes; subsp. carotovora
-
-
Manually annotated by BRENDA team
formerly Erwinia aroideae; pectate lyase I and pectate lyase II
-
-
Manually annotated by BRENDA team
isoenzyme PL I and PL II
-
-
Manually annotated by BRENDA team
pectate lyase B; subsp. carotovora
-
-
Manually annotated by BRENDA team
pectate lyase III
-
-
Manually annotated by BRENDA team
subsp. carotovorum
-
-
Manually annotated by BRENDA team
Pectobacterium carotovorum IFO3830
IFO3830
-
-
Manually annotated by BRENDA team
Pectobacterium carotovorum ZT0505
subsp. carotovorum
-
-
Manually annotated by BRENDA team
Penicillium occitanis CT1
-
-
-
Manually annotated by BRENDA team
gene Pcpel2
UniProt
Manually annotated by BRENDA team
pv. glycinea
-
-
Manually annotated by BRENDA team
pv. lachrymans, isoenzyme PelS
-
-
Manually annotated by BRENDA team
isolated from soil of Flaming Mountain in the Turpan Basin of Xinjiang, China, gene pl-str
-
-
Manually annotated by BRENDA team
Streptomyces thermocarboxydus B1
strain B1
UniProt
Manually annotated by BRENDA team
nov., pectate lyase a and pectate lyase b
-
-
Manually annotated by BRENDA team
DSM 3109
SwissProt
Manually annotated by BRENDA team
strain MSB8
-
-
Manually annotated by BRENDA team
ATCC 33768
SwissProt
Manually annotated by BRENDA team
gene pelB cloned from the metagenomic DNA of alkaline environment soils
UniProt
Manually annotated by BRENDA team
Xanthomonas campestris ACCC 10048
-
-
-
Manually annotated by BRENDA team
ATCC 49397, ATCC 35669 (low activity), and JB580v
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
the enzyme belongs to pectate lyase family 3
evolution
-
the enzyme belongs to family PF09492
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 mature Apel is structurally related to the enzymes in the polysaccharide lyase family 1
evolution
the enzyme belongs to the polysaccharide lyase family 1
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
-
PL-STR belongs to family PF00544
evolution
the enzyme belongs to te pectate lyase family
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
Bacillus subtilis TCCC11286
-
the mature Apel is structurally related to the enzymes in the polysaccharide lyase family 1
-
evolution
-
the enzyme belongs to the polysaccharide lyase family 1
-
evolution
Xanthomonas campestris ACCC 10048
-
the enzyme belongs to family PF09492
-
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
-
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
-
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
gene inactivation does not result in complete loss of pectate lyase activity, but the symptoms of anthracnose in the infected host plants are reduced
physiological function
PEL may play an important role in the process of normal fiber elongation in cotton
physiological function
-
pectate lyase is involved in cell wall hydrolysis and pulp softening during ripening fruits
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
-
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
-
role of secreted pectate lyase, a cell wall-degrading enzyme, in the aggressiveness of Colletotrichum coccodes, 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
-
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
Musa acuminata Nangka
-
pectate lyase is involved in cell wall hydrolysis and pulp softening during ripening fruits
-
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
-
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
-
implication of Bacillus sp. in the production of pectinolytic enzymes during cocoa fermentation
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
-
the enzyme from Xanthomonas campestris ACCC 10048 is a low-temperature-active alkaline pectate lyase
additional information
-
Pel structure modeling, 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
-
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
Bacillus subtilis TCCC11286
-
Pel structure modeling, 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
-
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
Pectobacterium carotovorum ZT0505
-
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
Xanthomonas campestris ACCC 10048
-
the enzyme from Xanthomonas campestris ACCC 10048 is a low-temperature-active alkaline pectate lyase
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
citrus pectin
?
show the reaction diagram
-
-
-
?
citrus pectin
?
show the reaction diagram
-
-
-
-
?
citrus pectin
?
show the reaction diagram
PelA shows 25% relative activity on citrus pectin compared to polygalacturonate
-
-
?
citrus pectin
unsaturated tetragalacturonate
show the reaction diagram
Bacillus pumilus, Bacillus pumilus BK2
-
-
-
?
citrus pectin P9311
?
show the reaction diagram
-
-
-
-
?
citrus pectin P9311
?
show the reaction diagram
Xanthomonas campestris, Xanthomonas campestris ACCC 10048
-
-
-
-
?
citrus pectin P9436
?
show the reaction diagram
-
-
-
-
?
citrus pectin P9436
?
show the reaction diagram
Xanthomonas campestris, Xanthomonas campestris ACCC 10048
-
-
-
-
?
citrus pectin P9561
?
show the reaction diagram
-
-
-
-
?
citrus pectin P9561
?
show the reaction diagram
Xanthomonas campestris, Xanthomonas campestris ACCC 10048
-
-
-
-
?
de-esterified pectin
4,5-unsaturated oligogalacturonates
show the reaction diagram
PEL can randomly catalyze the apha(1-4) linkages of de-esterified pectin by beta-elimination
-
?
digalacturonic acid
?
show the reaction diagram
Fusarium verticillioides, Fusarium verticillioides NCIM 1276
-
-
-
-
?
esterified pectin
?
show the reaction diagram
94% esterified pectin. 97% of the activity with polygalacturonic acid
-
-
?
esterified pectin
unsaturated tetragalacturonic acid
show the reaction diagram
Bacillus pumilus, Bacillus pumilus BK2
-
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
?
show the reaction diagram
-
-
-
-
?
hexagalacturonic acid
?
show the reaction diagram
-
140% of the activity with low molecular weight polygalacturonic acid
-
-
?
hexagalacturonic acid
?
show the reaction diagram
-
17.2% of the activity with polygalacturonic acid
-
-
?
lime pectin
?
show the reaction diagram
-
with 75% methyl esterification
-
-
?
oligogalacturonate
unsaturated digalacturonate
show the reaction diagram
Dickeya chrysanthemi, Dickeya chrysanthemi 3937
-
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
?
oligogalacturonic acid
?
show the reaction diagram
-
the enzyme acts on polygalacturonic acids and oligogalacturonic acids over digalacturonic acid and better on the larger galacturonic acids until at least DP8
-
-
?
pectate
?
show the reaction diagram
-
-
-
-
?
pectate
?
show the reaction diagram
-
-
-
-
?
pectate
?
show the reaction diagram
-
methylated form
-
-
?
pectate
?
show the reaction diagram
i.e. polygalacturonic acid, cleavage of the pectate alpha-1,4-glycosidic bond by Pel-BL11
-
-
?
pectate
?
show the reaction diagram
Dickeya chrysanthemi EC16
-
-
-
-
?
pectate
?
show the reaction diagram
Paenibacillus campinasensis BL11
i.e. polygalacturonic acid, cleavage of the pectate alpha-1,4-glycosidic bond by Pel-BL11
-
-
?
pectic acid
oligouronides of heterogeneous size
show the reaction diagram
Erwinia aroidea
-
-
-
?
pectic acid
oligouronides of heterogeneous size
show the reaction diagram
Bacillus sp., Bacillus sp. RK9
-
acid soluble
-
?
pectic acid amide
?
show the reaction diagram
Bacillus sp., Bacillus sp. RK9
-
about 15% of activity with acid soluble pectic acid
-
-
?
pectin
?
show the reaction diagram
-
-
-
-
?
pectin
?
show the reaction diagram
-
-
-
-
?
pectin
?
show the reaction diagram
-
-
-
-
?
pectin
?
show the reaction diagram
-
-
-
-
?
pectin
?
show the reaction diagram
-
-
-
-
?
pectin
?
show the reaction diagram
-
-
-
-
?
pectin
?
show the reaction diagram
-
-
-
-
?
pectin
?
show the reaction diagram
-
-
-
-
?
pectin
?
show the reaction diagram
-
-
-
-
?
pectin
?
show the reaction diagram
-
-
-
?
pectin
?
show the reaction diagram
-
with a low degree of methylation
-
-
?
pectin
?
show the reaction diagram
Erwinia aroidea
-
with low methoxyl content
-
-
?
pectin
?
show the reaction diagram
-
unlike other isoenzymes, pectate lyase requires partially methyl esterified pectin as substrate
-
-
?
pectin
?
show the reaction diagram
-
about 70% methylated
-
-
?
pectin
?
show the reaction diagram
-
with 4.3% methoxyl groups
-
-
?
pectin
?
show the reaction diagram
-
at about 12% of the activity with acid soluble pectic acid
-
-
?
pectin
?
show the reaction diagram
-
no activity with 93% esterified pectin
-
-
-
pectin
?
show the reaction diagram
80% of the activity with polygalacturonic acid
-
-
?
pectin
?
show the reaction diagram
-
better substrate for pectate lyase I than polygalacturonic acid
-
-
?
pectin
?
show the reaction diagram
of methyl esterification degree from 22-89%. Similar activity on polygalacturonic acid and on 89% esterified citrus pectin
-
-
?
pectin
?
show the reaction diagram
relative degradation rates of citrus pectin with methylation degrees 31%, 63% and 94% is 124%, 73% and 9% compared to polygalacturonic acid
-
-
?
pectin
?
show the reaction diagram
with degrees of esterification of 31%, 63% and 94% is degraded with 103%, 84% and 46% of the activity with polygalacturonic acid
-
-
?
pectin
?
show the reaction diagram
Clostridium stercorarium
apple or citrus pectin, activity with pectin is lower than activity with polygalacturonate
-
-
?
pectin
?
show the reaction diagram
Clostridium stercorarium
apple pectin, citrus pectin, as the percentage of methylation in pectin becomes higher, the activities become lower
-
-
?
pectin
?
show the reaction diagram
-
of methyl esterification degree from 22% to 89%, maximal activity on 22% esterified citrus pectin
-
-
?
pectin
?
show the reaction diagram
low-esterified pectin (30%) is the optimum substrate for the PelA, higher-esterified pectin is hardly cleaved
-
-
?
pectin
?
show the reaction diagram
-
pectate lyases harness anti beta-elimination chemistry to cleave the alpha-1,4 linkage in the homogalacturonan region of plant cell wall pectin
-
-
?
pectin
?
show the reaction diagram
methylated at low-degree
-
-
?
pectin
?
show the reaction diagram
Bacillus sp. TS 47
-
-
-
-
?
pectin
?
show the reaction diagram
Bacillus subtilis 168
-
-
-
-
?
pectin
?
show the reaction diagram
Dickeya chrysanthemi 3937
-
with a low degree of methylation
-
-
?
pectin
?
show the reaction diagram
-
-
-
-
?
pectin
?
show the reaction diagram
with degrees of esterification of 31%, 63% and 94% is degraded with 103%, 84% and 46% of the activity with polygalacturonic acid
-
-
?
pectin
?
show the reaction diagram
relative degradation rates of citrus pectin with methylation degrees 31%, 63% and 94% is 124%, 73% and 9% compared to polygalacturonic acid
-
-
?
pectin
?
show the reaction diagram
Bacillus sp. BP-23
of methyl esterification degree from 22-89%. Similar activity on polygalacturonic acid and on 89% esterified citrus pectin
-
-
?
pectin
?
show the reaction diagram
Clostridium stercorarium F-9
apple or citrus pectin, activity with pectin is lower than activity with polygalacturonate
-
-
?
pectin
?
show the reaction diagram
Bacillus subtilis SO113
-
-
-
-
?
pectin
?
show the reaction diagram
Fusarium verticillioides NCIM 1276
-
-
-
-
?
pectin
?
show the reaction diagram
Bacillus sp. P4-N
-
-
-
-
?
pectin
?
show the reaction diagram
Aspergillus nidulans GR5
-
low-esterified pectin (30%) is the optimum substrate for the PelA, higher-esterified pectin is hardly cleaved
-
-
?
pectin
?
show the reaction diagram
Bacillus sp. RK9
-
at about 12% of the activity with acid soluble pectic acid
-
-
?
pectin
unsaturated oligogalacturonides
show the reaction diagram
-
esterified citrus pectin
-
?
pentagalacturonic acid
saturated digalacturonic acid + unsaturated trigalacturonic acid + saturated trigalacturonic acid + unsaturated digalacturonic acid
show the reaction diagram
-
-
-
?
pentagalacturonic acid
saturated digalacturonic acid + unsaturated trigalacturonic acid + saturated trigalacturonic acid + unsaturated digalacturonic acid
show the reaction diagram
-
-
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
?
pentagalacturonic acid
saturated digalacturonic acid + unsaturated trigalacturonic acid + saturated trigalacturonic acid + unsaturated digalacturonic acid
show the reaction diagram
-
5.9% of the activity with polygalacturonic acid
-
?
pentagalacturonic acid
saturated digalacturonic acid + unsaturated trigalacturonic acid + saturated trigalacturonic acid + unsaturated digalacturonic acid
show the reaction diagram
-
215% of the activity with low molecular weight polygalacturonic acid
-
?
polygalacturonate
?
show the reaction diagram
-
-
-
-
?
polygalacturonate
?
show the reaction diagram
-
-
-
-
?
polygalacturonate
?
show the reaction diagram
-
-
-
?
polygalacturonate
?
show the reaction diagram
-
Pel I, Pel II, Pel III
-
-
?
polygalacturonate
?
show the reaction diagram
Bacillus sp. BP-23
-
-
-
?
polygalacturonate
?
show the reaction diagram
Aspergillus niger MIUG 16
-
Pel I, Pel II, Pel III
-
-
?
polygalacturonate
unsaturated galacturonic acid polymer
show the reaction diagram
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
-
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
Bacillus pumilus DKS1
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
Musa acuminata Harichhal
-
-
-
?
polygalacturonate
unsaturated oligogalacturonides
show the reaction diagram
Bacillus sp. KSM-P15, Bacillus subtilis SO113, Bacillus sp. P4-N
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
?
polygalacturonate
unsaturated tetragalacturonic acid
show the reaction diagram
Bacillus pumilus, Bacillus pumilus BK2
-
the enzyme cleaves polygalacturonic acid via a beta-elimination mechanism
-
?
polygalacturonate
unsaturated galacturonides
show the reaction diagram
Fusarium verticillioides, Fusarium verticillioides NCIM 1276
-
-
-
?
polygalacturonate
unsaturated oligo-galacturonides
show the reaction diagram
Bacillus subtilis, Bacillus subtilis WSHB04-02
-
the enzyme produces unsaturated oligo-galacturonides including unsaturated tri-galacturonic acid and unsaturated bi-galacturonic acid but not unsaturated mono-galacturonic acid
-
?
polygalacturonate
unsaturated polygalacturonic acid
show the reaction diagram
-
-
-
?
polygalacturonate
unsaturated 4,5-digalacturonate + unsaturated 4,5-trigalacturonate
show the reaction diagram
Streptomyces thermocarboxydus, Streptomyces thermocarboxydus B1
-
-
?
polygalacturonate
unsaturated 4,5-digalacturonate + unsaturated 4,5-trigalacturonate + ?
show the reaction diagram
the enzyme is specific toward alpha-1,4-galacturonic acid linkages of galactopolysaccharides
main products
?
polygalacturonate
unsaturated tetragalacturonate
show the reaction diagram
Bacillus pumilus, Bacillus pumilus BK2
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
?
polygalacturonate
unsaturated trigalacturonate + unsaturated oligogalacturonates
show the reaction diagram
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
major product
?
polygalacturonic
?
show the reaction diagram
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
?
show the reaction diagram
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
Clostridium stercorarium
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
Clostridium stercorarium
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
best substrate
final major end products are dimers, trimers, and tetramers of unsaturated galacturonic acid, PelB does not produce any monomeric GalpA
-
?
polygalacturonic acid
?
show the reaction diagram
-
Arg initiates proton abstration during the beta elimination cleavage of polygalacturonic acid
-
-
?
polygalacturonic acid
?
show the reaction diagram
degradation through an endo-type fashion
-
-
?
polygalacturonic acid
?
show the reaction diagram
endolytic cleavage
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
random cleavage
-
-
?
polygalacturonic acid
?
show the reaction diagram
the recombinant enzyme shows highest activity on polygalacturonic acid and lower activity on more highly methylated pectin
-
-
?
polygalacturonic acid
?
show the reaction diagram
enzyme is found to be active on both polygalacturonic acid and citrus pectin as substrates, although it appears to prefer polygalacturonic acid
-
-
?
polygalacturonic acid
?
show the reaction diagram
enzyme shows over ten times higher catalytic efficiency towards polygalacturonic acid than towards citrus pectin
-
-
?
polygalacturonic acid
?
show the reaction diagram
Bacillus pumilus, Bacillus pumilus DKS1
Arg235 is an essential catalytic residue
-
-
?
polygalacturonic acid
?
show the reaction diagram
degradation through an endo-type fashion
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
random cleavage
-
-
?
polygalacturonic acid
?
show the reaction diagram
Clostridium stercorarium F-9
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
Xanthomonas campestris ACCC 10048
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
Penicillium occitanis CT1
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
Aspergillus nidulans GR5
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
Bacillus subtilis IFO3134
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
-
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
show the reaction diagram
-
-
end products at 46% saturation: unsaturated digalacturonic acids, unsaturated trigalacturonic acids, saturated monogalacturonic acid + saturated digalacturonic acid + saturated trigalacturonic acid
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
-
the main product appears to be a disaccharide that contains a DELTA4,5-unsaturated galacturonic acid residue
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
with a low degree of methylation
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
random attack
-
-
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
random attack
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
activity decreases when the methoxyl content of the substrate increases
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
endo-cleavage
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
endo-cleavage
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
-
endo-cleavage
wide range of 4,5-unsaturated oligogalacturonates, further depolymerized to unsaturated dimer and trimer
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
Bacillus sp. KSM-P7
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
Dickeya chrysanthemi 3937
-
with a low degree of methylation
-
?
polygalacturonic acid
unsaturated oligogalacturonate
show the reaction diagram
Dickeya chrysanthemi 3937
-
-
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
show the reaction diagram
-
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
show the reaction diagram
Bacillus sp. RK9
-
random attack
-
-
polygalacturonic acid
4,5-unsaturated digalacturonic acid + 4,5-unsaturated trigalacturonic acid + oligogalacturonic acid
show the reaction diagram
-
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
show the reaction diagram
-
endo-type reaction
-
?
polygalacturonic acid
4,5-unsaturated digalacturonic acid + 4,5-unsaturated trigalacturonic acid + oligogalacturonic acid
show the reaction diagram
-
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
4,5-unsaturated digalacturonic acid + 4,5-unsaturated trigalacturonic acid + oligogalacturonic acid
show the reaction diagram
-
unsaturated di- and trigalacturonic acids are mainly formed as the final products of degradation by Pel SWU
?
polygalacturonic acid
unsaturated oligogalacturonide
show the reaction diagram
-
-
?
polygalacturonic acid
unsaturated oligogalacturonides
show the reaction diagram
-
-
?
polygalacturonic acid
unsaturated oligogalacturonides
show the reaction diagram
-
i.e. pectate, endo-cleavage, the enzyme has a preference for sequences of non-esterified galacturonic acid residues
-
?
polygalacturonic acid
unsaturated oligogalacturonides
show the reaction diagram
-
-
?
polygalacturonic acid
DELTA4,5-unsaturated oligogalacturonides
show the reaction diagram
-
-
?
polygalacturonic acid
unsaturated galacturonate
show the reaction diagram
Bacillus sp., Bacillus sp. TS 47
-
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate + ?
show the reaction diagram
specific substrate, enzyme activity decreases when the methoxyl content of the substrate increases
-
?
polypectate
?
show the reaction diagram
-
-
-
-
?
polypectate
?
show the reaction diagram
-
-
-
-
?
polypectate
?
show the reaction diagram
-
-
-
-
?
protopectin
pectin + ?
show the reaction diagram
Bacillus sp., Bacillus sp. TS 47
-
-
-
?
reduced tetragalacturonic acid
galacturonic acid + reduced trigalacturonic acid
show the reaction diagram
-
-
-
?
tetragalacturonate
?
show the reaction diagram
-
-
-
-
?
tetragalacturonic acid
altered trigalacturonic acid + digalacturonic acid + altered digalacturionic acid + D-galacturonic acid
show the reaction diagram
-
-
-
?
tetragalacturonic acid
altered trigalacturonic acid + digalacturonic acid + altered digalacturionic acid + D-galacturonic acid
show the reaction diagram
-
-
only trace amounts of digalacturonic acid
?
tetragalacturonic acid
altered trigalacturonic acid + digalacturonic acid + altered digalacturionic acid + D-galacturonic acid
show the reaction diagram
-
141% of the activity with low molecular weight polygalacturonic acid
-
?
trigalacturonate
?
show the reaction diagram
-
-
-
-
?
trigalacturonate
?
show the reaction diagram
-
enzyme and substrate-binding structures, overview
-
-
?
trigalacturonic acid
?
show the reaction diagram
Fusarium verticillioides, Fusarium verticillioides NCIM 1276
-
-
-
-
?
trigalacturonic acid
altered digalacturonic acid + galacturonic acid
show the reaction diagram
-
-
-
?
trigalacturonic acid
altered digalacturonic acid + galacturonic acid
show the reaction diagram
-
-
-
?
trigalacturonic acid
altered digalacturonic acid + galacturonic acid
show the reaction diagram
-
3% of the activity with low molecular weight polygalacturonic acid
-
?
methyl esterified pectin
?
show the reaction diagram
-
citrus pectin, 7% methylation
-
-
?
additional information
?
-
-
pectate lyase E is most effective in causing maceration and inducing electrolyte loss and cell death in potato tuber tissue
-
-
-
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 activity with digalacturonic acid
-
-
-
additional information
?
-
-
no macerating activity on Gampi bark, carrot, potato, cabbage and radish
-
-
-
additional information
?
-
-
protopectinase-like activity on cotton fibers
-
-
-
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
the enzyme is involved in pathogenesis
-
-
-
additional information
?
-
Erwinia aroidea
-
pectin or pectic acid as inducer
-
-
-
additional information
?
-
-
enzyme production is repressed by glucose
-
-
-
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
?
-
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
?
-
-
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
?
-
the enzyme is involved in degradation of the pectate portion of the primary plant cell wall
-
-
?
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 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
?
-
the enzyme plays an important role in plant-nematode interactions
-
-
-
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
?
-
-
optimization of chemical and physical parameters affecting the activity of pectate lyase
-
-
-
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
?
-
-
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
?
-
PelA efficiently macerates mung bean hypocotyls and potato tuber tissues into single cells
-
-
-
additional information
?
-
-
digalacturonate is not cleaved at an appreciable rate
-
-
-
additional information
?
-
PelA does not show any activity on mannan, CMC, xylan, glucan, or soluble starch
-
-
-
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
?
-
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
?
-
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
?
-
-
PelN acts synergistically with other pectate lyases in the organism, activity comparisons, overview
-
-
-
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 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
?
-
Dickeya chrysanthemi EC16
-
pectate lyase E is most effective in causing maceration and inducing electrolyte loss and cell death in potato tuber tissue
-
-
-
additional information
?
-
Dickeya chrysanthemi EC16
-
pectate lyase A is a virulence factor for soft rot diseases in plants
-
-
?
additional information
?
-
Dickeya chrysanthemi EC16
-
pectate lyase A is a virulence factor secreted by the plant pathogenic bacterium Erwinia chrysanthemi
-
-
?
additional information
?
-
Dickeya chrysanthemi EC16
-
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
?
-
Paenibacillus amylolyticus 27C64
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelA, overview
-
-
-
additional information
?
-
Paenibacillus amylolyticus 27C64
substrates are highly methylated pectin and polygalacturonic acid, substrate specificity of PelB, overview
-
-
-
additional information
?
-
-
protopectinase-like activity on cotton fibers
-
-
-
additional information
?
-
Bacillus subtilis BS66
substrates are 45% methylated pectin or polygalacturonate
-
-
-
additional information
?
-
Bacillus pumilus BS22
substrates are 45% methylated pectin or polygalacturonate
-
-
-
additional information
?
-
Xanthomonas campestris ACCC 10048
-
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
?
-
PelA does not show any activity on mannan, CMC, xylan, glucan, or soluble starch
-
-
-
additional information
?
-
Aspergillus nidulans GR5
-
PelA efficiently macerates mung bean hypocotyls and potato tuber tissues into single cells
-
-
-
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
?
-
Bacillus sp. RK9
-
constitutive enzyme
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
polygalacturonic acid
?
show the reaction diagram
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
W8CR80
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
Penicillium occitanis CT1
-
-
-
-
?
polygalacturonic acid
?
show the reaction diagram
W8CR80
-
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
the enzyme is involved in pathogenesis
-
-
-
additional information
?
-
Erwinia aroidea
-
pectin or pectic acid as inducer
-
-
-
additional information
?
-
-
enzyme production is repressed by glucose
-
-
-
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
?
-
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
?
-
-
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
?
-
Q9WYR4
the enzyme is involved in degradation of the pectate portion of the primary plant cell wall
-
-
?
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 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
?
-
Q33CQ4
the enzyme plays an important role in plant-nematode interactions
-
-
-
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
?
-
-
optimization of chemical and physical parameters affecting the activity of pectate lyase
-
-
-
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
?
-
-
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
?
-
Dickeya chrysanthemi EC16
-
pectate lyase A is a virulence factor for soft rot diseases in plants
-
-
?
additional information
?
-
Dickeya chrysanthemi EC16
-
pectate lyase A is a virulence factor secreted by the plant pathogenic bacterium Erwinia chrysanthemi
-
-
?
additional information
?
-
Dickeya chrysanthemi EC16
-
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
?
-
Bacillus sp. RK9
-
constitutive enzyme
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ag+
1 mM, stimulates actvity up to 120%
Ba2+
-
decreases activity
Ba2+
the enzyme is activated slightly in the presence of BaCl2
Ba2+
activates 181% at 0.2 mM
Ca2+
-
required, optimal concentration varies with levels of the substrate
Ca2+
Erwinia aroidea
-
stimulates
Ca2+
-
cation required, Ca2+ is most effective
Ca2+
-
0.5 mM, 7fold activation of pectate lyase I, 4fold activation of pectate lyase II
Ca2+
-
activates; optimal concentration: 0.4 mM
Ca2+
-
required
Ca2+
-
up to 1 mM, stimulation
Ca2+
-
restores activity of the EGTA-inactivated enzyme
Ca2+
-
optimal concentration: 0.2 mM
Ca2+
-
optimal concentration: 0.2 mM; required
Ca2+
-
activates; enhances activity 5fold
Ca2+
-
activates; optimal concentration: 0.1 mM
Ca2+
-
activates; maximal activity at 0.5-1 mM CaCl2
Ca2+
-
maximal activity at 0.2 mM Ca2+; required
Ca2+
-
structurally essential
Ca2+
-
dependent on
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+
strong sigmoidal CaCl2 concentration dependent relation. Optimal catalysis at 0.5-1.0 mM Ca2+
Ca2+
-
required
Ca2+
absolute requirement
Ca2+
requires Ca2+, optimal activity with 0.25 mM
Ca2+
-
both pectate lyase I and II require 0.2 mM Ca2+ for maximal activity
Ca2+
-
maximal activity at 0.6 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+
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+
Clostridium stercorarium
strong activation, optimal activity at 0.05 mM CaCl2
Ca2+
Clostridium stercorarium
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+
-
71% of maximal activity in absence of Ca2+
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+
-
absolute requirement
Ca2+
BxPEL1 shows full dependency
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+
1 mM, actvity is enhanced by 1209%
Ca2+
Ca2+-dependent activity; Ca2+-dependent activity
Ca2+
Ca2+-dependent activity; Ca2+-dependent activity
Ca2+
-
activity is not changed
Ca2+
-
enhances activity
Ca2+
enzyme activity is Ca2+-dependent
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 for activity
Ca2+
Ca2+ is not required for activity on pectic substrates
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+
-
PelC is dependent on Ca2+ for activity and stability
Ca2+
-
optimum Ca2+ concentration at 0.6 mM
Ca2+
-
optimum concentration at 0.6 mM
Ca2+
-
optimum Ca2+ concentration at 2.0 mM
Ca2+
-
optimum Ca2+ concentration at 2.0-4.0 mM
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+
-
optimum Ca2+ concentration at 0.6 mM
Ca2+
-
optimum Ca2+ concentration at 0.2 mM
Ca2+
-
optimum Ca2+ concentration at 0.5 mM
Ca2+
-
optimum concentration at 1.0 mM
Ca2+
-
optimum concentration at 0.5 mM
Ca2+
-
optimum Ca2+ concentration at 0.2 mM
Ca2+
activates 208% at 0.2 mM
Ca2+
activates 263% at 0.2 mM
Ca2+
activates 208% at 0.2 mM
Ca2+
activates optimally at 0-2.5 mM; activates optimally at 0-2.5 mM
Ca2+
activates
Ca2+
activates, active site binding structure, overview
Ca2+
-
stabilizes, best activating metal ion, optimally at 2 mM
Ca2+
-
required, best at 0.05 mM
Ca2+
-
dependent on, binding structure, overview
Ca2+
-
activates, optimal at 1 mM
Ca2+
required, activates the recombinant enzyme from Pichia pastoris by 26%
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+
-
required, optimal at about 0.05 mM
Ca2+
required, activates 5.8fold at 0.5 mM
CaCl2
-
activates
Co2+
-
decreases activity
Co2+
-
1.4fold at 1 mM
Cu2+
-
decreases 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, stimulates actvity up to 592%
Fe2+
-
completely inactivates activity after incubation for 15 min
Fe2+
activates 213% at 0.2 mM; activates 231% at 0.2 mM
Fe2+
-
required for activity, optimal at 0.1 to 0.3mM
Fe3+
1 mM, stimulates actvity up to 348%
Hg2+
-
1 mM, can replace Ca2+ in activation
K+
19% activation at 0.5 mM
K+
-
9% activation at 1 mM
K+
activates slightly at 0.5-1 mM
Mg2+
-
26% of the activation with Ca2+
Mg2+
-
41% of the activation with Ca2+
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+
1 mM, stimulates actvity up to 368%
Mg2+
-
slightly increases activity
Mg2+
-
slightly enhances enzyme activity
Mg2+
the enzyme is activated 40% in the presence of MgCl2
Mg2+
activates 190% at 0.2 mM
Mg2+
25% activation at 0.5 mM
Mg2+
activates slightly at 0.5 mM
Mn2+
-
27% of the activity with Ca2+
Mn2+
-
restores activity of the EGTA-inactivated enzyme
Mn2+
-
optimal concentration: 0.1 mM
Mn2+
-
1 mM, enhances activity 6fold
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, actvity is enhanced by 1221%
Mn2+
-
decreases activity
Mn2+
-
enhances activity
Mn2+
activates 136% at 0.2 mM
Mn2+
-
1.7fold at 1 mM
Na+
-
decreases activity
Na+
-
10% activation at 1 mM
Ni2+
activates 191% at 0.2 mM
Se2+
activates 158% at 0.2 mM
Sr2+
-
restores activity of the EGTA-inactivated enzyme
Sr2+
-
21% of the activation with Ca2+
Triton X-100
activates slightly at 0.5-1 mM
Tween-20
activates slightly at 1 mM
Zn2+
activates 132% at 0.2 mM
Zn2+
16% activation at 0.5 mM
Zn2+
activates slightly at 0.5-1 mM
Mn2+
-
29% activation at 1 mM, 7.5% activation at 5 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
Fe2+ and Ni2+ do not significantly affect the activity of Pel-90
additional information
-
divalent cations are required for maximum activity
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+,
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-Butanedione
-
-
2,4,6-Trinitrobenzenesulfonate
-
1 mM, 73% inhibition
2-hydroxy-5-nitrophenyl bromide
-
-
2-mercaptoethanol
-
0.0022 mM, 50% inhibition
2-mercaptoethanol
-
29% loss of activity at 1 mM, 67% loss of activity at 5 mM
acetic acid
-
at 50 mM and above
Ag+
-
1 mM, strong
Ag+
1 mM, 47% inhibition
Ag+
25% residual activity at 1 mM
ascorbic acid
-
48% loss of activity at 0.1 mM, complete inactivation at 1.0 mM
Ba2+
Erwinia aroidea
-
-
Ba2+
-
Ba(CH3CO2)2
Ba2+
-
1 mM, strong
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% inhibtion at 0.5 mM, 97% at 1 mM
Ba2+
strong inhibition at 0.5-1 mM
Butyric acid
-
at 200 mM and above
Ca2+
-
1 mM, strong inhibition of isoenzyme pelE
Ca2+
Ca2+ does not increase but instead inhibits the activity of PelA, 41% residual activity at 1 mM
Ca2+
inhibitory above 1 mM
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
Cd2+
-
1 mM, moderate
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
Co2+
Erwinia aroidea
-
-
Co2+
-
CoCl2
Co2+
1 mM, 12% inhibition
Co2+
-
0.38 mM, 50% inhibition
Co2+
the enzyme is inhibited 30% in the presence of Co2+
Co2+
22% residual activity at 1 mM
Co2+
-
strong inhibition
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+
-
CuSO4
Cu2+
-
1 mM, moderate
Cu2+
1 mM, 91% inhibition
Cu2+
24% residual activity at 1 mM
Cu2+
93% inhibition at 5 mM
Cu2+
20% inhibtion at 0.5 mM
Cu2+
-
11% activation at 1 mM, 41% inhibition at 5 mM
Cu2+
strong inhibition at 1 mM
diethyldicarbonate
-
-
dithiothreitol
-
0.0104 mM, 50% inhibition
dithiothreitol
-
27% loss of activity at 1 mM, 67% loss of activity at 5 mM
EDTA
Erwinia aroidea
-
-
EDTA
-
1 mM, complete inhibition
EDTA
-
inhibits activity with polygalacturonate, no inhibition of the ability to cleave protopectin of Boehmeria nivea
EDTA
1 mM, in 50 mM Tris-HCl buffer, pH 7.5, 10 min at 30C, 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 30C, activity is completely abolished, fully recovered by adding 0.8 mM CaCl2
EDTA
3 mM, complete inhibition. Lyase activity can be restored by further addition of 5 mM CaCl2
EDTA
-
0.09 mM, 50% inhibition
EDTA
-
1 mM, 12% loss of activity
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
1 mM, completely represses PelA enzyme activity
EDTA
5 mM EDTA causes complete loss of enzyme activity
EDTA
PelA is sensitive to 10 mM EDTA with 39% activity retained
EDTA
-
strong inhibition
EDTA
-
complete inhibition at 2 mM
EDTA
complete inhibition at 5 mM
EDTA
complete inhibition at 0.5 mM
EDTA
-
complete inhibition
EDTA
-
inhibits completely at 1 mM
epicatechin
-
epicatechin may be involved in the resistance of unripe avocado fruits by inhibiting the pectate lyase activity of Colletotrichum gloeosporoides
ethylene glycol
-
at 50 mM and above
Fe2+
-
FeCl2
Fe2+
18% inhibtion at 0.5 mM, 43% at 1 mM
Fe2+
strong inhibition at 1 mM
Fe3+
-
-
Fe3+
41% inhibition at 5 mM
Fe3+
-
4% inhibition at 1 mM, 99% inhibition at 5 mM
ferulic acid
-
15% inhibition at 0.01 mM, 58% inhibition at 0.05 mM
Hg2+
Erwinia aroidea
-
-
Hg2+
-
HgCl2
Hg2+
-
-
Hg2+
1 mM, 23% inhibition
Hg2+
24% residual activity at 1 mM
Hg2+
complete inhibition at 5 mM
HgCl2
-
complete inactivation at 0.1 mM
Hydroxymercuribenzoate
-
-
-
iodoacetic acid
-
-
Lactic acid
-
at 50 mM and above
Li+
-
5% activation at 1 mM, 62% inhibition at 5 mM
Mg2+
1 mM, 58% inhibition
Mg2+
56% residual activity at 1 mM
Mg2+
23% inhibition at 0.2 mM
Mg2+
8.4% inhibition at 0.2 mM
Mg2+
64.5% inhibition at 5 mM
Mg2+
-
9% activation at 1 mM, 22% inhibition at 5 mM
Mg2+
strong inhibition at 1 mM
Mn2+
Erwinia aroidea
-
-
Mn2+
-
1 mM, weak
Mn2+
-
MnCl2
Mn2+
-
1 mM, moderate
Mn2+
complete inhibition at 1 mM
Mn2+
-
strong inhibition
Mn2+
weakly inhibits PelA activity at 1 mM
Mn2+
94% inhibition at 0.2 mM
Mn2+
82% inhibition at 0.2 mM
Mn2+
91.5% inhibition at 5 mM
Mn2+
25% inhibtion 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+
Erwinia aroidea
-
-
Ni2+
-
NiCl2
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
p-coumaric acid
-
33% inhibition at 0.01 mM, 61% inhibition at 0.05 mM
Pb2+
53% residual activity at 1 mM
Pb2+
-
31% inhibition at 1 mM, complete inhibition at 5 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
salicylic acid
-
33% inhibition at 0.01 mM, 61% inhibition at 0.05 mM
SDS
-
1%, strong inhibition
SDS
-
strong inhibition of enzyme from Alpine strain A15; strong inhibition of enzyme from Siberian strain AG25
SDS
PelA is sensitive to 0.1% (w/v) SDS with 43% activity retained
SDS
complete inhibition at 0.5%
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
Sodium metabisulfite
-
40% inactivation at 0.1 mM, 73% inactivation at 1 mM
Sr2+
-
1 mM, weak
Sr2+
weakly inhibits PelA activity at 1 mM
Zn2+
-
ZnCl2
Zn2+
-
-
Zn2+
-
1 mM, strong
Zn2+
1 mM, 29% inhibition
Zn2+
-
2.8 mM, 50% inhibition
Zn2+
1 mM, 40% inhibition
Zn2+
the enzyme is inhibited 30% in the presence of Zn2+
Zn2+
69% residual activity at 1 mM
Zn2+
-
strong inhibition
Zn2+
88% inhibition at 0.2 mM
Zn2+
97% inhibition at 0.2 mM
Zn2+
63.5% inhibition at 5 mM
Zn2+
-
13% activation at 1 mM, 46% inhibition at 5 mM
ZnSO4
0.1 mM, 90% decrease in activity
MnSO4
0.1 mM, 10% decrease in activity
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
Triton X-100 and Tween-20 have a negligible influence on the activity at 0.5-1.0 mM
-
additional information
-
PelN is only weakly affected by the degree of pectin methyl esterification
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cystine
-
25% activation at 1 mM, 73% activation at 5 mM
Tris-HCl buffer
enzyme activity increases with increasing concentration of the buffer (20 mM to 1 M) and has highest activity at 1 M
DMSO
24% activation at 0.5%
additional information
-
activity of pectate lyase is 9fold higher at 90C 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%
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23
pentagalacturonic acid
-
-
0.11
Polygalacturonate
-
-
0.0136
polygalacturonic acid
-
pH 9.0, 60C
0.0199
polygalacturonic acid
-
pH 7.0, 60C
0.19
tetragalacturonate
-
at pH8.5 and in the presence of 5mMCa2+
-
0.19
tetragalacturonic acid
-
-
1.2
trigalacturonate
-
at pH8.5 and in the presence of 5mMCa2+
1.5
trigalacturonic acid
-
-
0.38
hexagalacturonic acid
-
-
additional information
additional information
-
Km for acid soluble polygalacturonic acid: 0.051%
-
additional information
additional information
-
-
-
additional information
additional information
-
Km for poly-D-galacturonic acid: 0.040-0.070 mg/ml
-
additional information
additional information
-
the Km-value for pectin increases 30000fold as the percent esterification of the substrate increases from 0 to 60%
-
additional information
additional information
-
-
-
additional information
additional information
-
Km for citrus pectin: 5.0 g/l; Km for pectate: 0.5 g/l
-
additional information
additional information
-
Km for polypectate: 0.11%
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km for polygalacturonic acid: 0.862 g/l
-
additional information
additional information
-
Km for polygalacturonic acid: 16%
-
additional information
additional information
-
Km for polygalacturonic acid: 0.134 mg/ml
-
additional information
additional information
-
-
-
additional information
additional information
-
Km for polygalacturonate: 0.019 g/l
-
additional information
additional information
-
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
-
additional information
additional information
-
Km-value for polygalacturonic acid is 0.85 mg/ml
-
additional information
additional information
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
-
additional information
additional information
-
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 30C and pH 8.5
-
additional information
additional information
-
KM-value for polygalacturonate is 0.24 g/l, at pH 7.8, 50C. 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
-
additional information
additional information
-
KM-value is 0.13 mg/ml for 22% esterified pectin, the KM-value is 0.15 mg/ml for polygalacturonic acid
-
additional information
additional information
-
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
-
additional information
additional information
-
-
-
additional information
additional information
Km of 0.50 mg/ml for polygalacturonic acid
-
additional information
additional information
-
enzyme kinetics and thermodynamics at 75C and 90C in presence or absence of hydroxyapatite nanoparticles, detailed overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
265
67% esterified citrus pectin
Cellvibrio japonicus
-
37C
-
22
89% esterified citrus pectin
Cellvibrio japonicus
-
37C
-
6.6
digalacturonic acid
Fusarium verticillioides
-
-
21
Pectin
Fusarium verticillioides
-
-
110.6
Pectin
Fusarium verticillioides
-
-
750
Pectin
uncultured bacterium
S5UBI8
50-70% methylated substrate, pH 9.8, 45C, recombinant enzyme
1882
Pectin
uncultured bacterium
S5UBI8
over 80% methylated substrate, pH 9.8, 45C, recombinant enzyme
131.5
Polygalacturonate
Fusarium verticillioides
-
-
1200
Polygalacturonate
Bacillus subtilis
-
at pH8.5 and in the presence of 5mMCa2+
0.03 - 0.55
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, mutant enzyme 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
7.48
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, mutant enzyme 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
42.2
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, mutant enzyme K89A
43.2
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, mutant enzyme D84N
72.9
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, mutant enzyme D126N
101
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, mutant enzyme H66A
154
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, mutant enzyme K41A
156
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, mutant enzyme D80N
159
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, mutant enzyme Y126N
173
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, wild-type enzyme
196
polygalacturonic acid
Bacillus sp.
Q9RHW0
pH 10.5, 30C, mutant enzyme W78F
259.5
polygalacturonic acid
Cellvibrio japonicus
-
37C
260
polygalacturonic acid
Cellvibrio japonicus
-
37C
2295
polygalacturonic acid
uncultured bacterium
S5UBI8
20-34% methylated substrate, pH 9.8, 45C, recombinant enzyme
6092
polygalacturonic acid
uncultured bacterium
S5UBI8
unmethylated substrate, pH 9.8, 45C, recombinant enzyme
1000
tetragalacturonate
Bacillus subtilis
-
at pH8.5 and in the presence of 5mMCa2+
-
340
trigalacturonate
Bacillus subtilis
-
at pH8.5 and in the presence of 5mMCa2+
65.95
trigalacturonic acid
Fusarium verticillioides
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0022
2-mercaptoethanol
-
-
0.0104
dithiothreitol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.065
culture filtrate, in 20 mM Tris-HCl pH 8.0, at 60C
3.03
purified recombinant enzyme
12
after 185fold purification, in 20 mM Tris-HCl pH 8.0, at 60C
177
purified native enzyme
194.3
-
purified enzyme, pH 9.0, 60C
200 - 220
-
444.6
-
purified recombinant enzyme, pH 9.0, 50C
614.7
purified recombinant His-tagged enzyme, 50-70% methylated pectin, pH 9.8, 45C
668.2
purified recombinant His-tagged enzyme, over 80% methylated pectin, pH 9.8, 45C
750
purified recombinant PCPEL2 expressed from pLysS, pH not specified in the publication, temperature not specified in the publication
852
-
purified native enzyme, pH 8.5, 55C
860
purified recombinant PCPEL2 expressed from pMAL, pH not specified in the publication, temperature not specified in the publication
1000
after 25.3fold purification
1320
purified recombinant enzyme from Pichia pastoris, pH 9.5, 50C
1623
purified recombinant His-tagged Pel-BL11, pH 10.0, 50C
1984
purified recombinant His-tagged enzyme, unmethylated polygalacturonic acid, pH 9.8, 45C
2060
purified recombinant enzyme, pH 9.8, 65C
2096
purified recombinant His-tagged enzyme, 20-34% methylated polygalacturonic acid, pH 9.8, 45C
2893
purified recombinant wild-type enzyme, pH 8.5, 60C
additional information
Erwinia aroidea
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
pectate lyase activity as high as 100 U/ml is attained in the fermentation broth of Pichia pastoris GS 115, which is about 10 times higher than when the gene is expressed in Escherichia coli
additional information
93 U/ml and weight of the ramie fibre of 1 g, pH 8.5, 37C
additional information
-
PelN acts synergistically with other pectine lyases in the organism, activity comparisons, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
-
Pel III
4.6
-
Pel II
7
Clostridium stercorarium
-
8
-
pectate lyase a
8
-
isoenzyme pelE
8
-
incubation carried out at
8.1
optimum 1, about 70% of maximal activity
8.5
-
isoenzyme PelA
8.5
-
wild-type enzyme, mutant enzyme R236K and mutant enzyme D154E, lime pectin as substrate
8.5
-
enzyme from Siberian strain AG25
8.5
-
assay at
8.5
-
assay at
8.8
-
isoenzyme isoenzyme pelD
9
-
pectate lyase B
9
-
enzyme from Alpine strain A15
9
-
recombinant His-tagged enzyme
9 - 9.2
Erwinia aroidea
-
-
9.2
-
isoenzyme PelC
9.3
-
isoenzyme PelB
9.4
-
assay at
9.4 - 10
-
-
9.5
-
pectate lyase B
9.5
-
above, mutant enzyme D154N, lime pectin as substrate
9.8
optimum 2, maximal activity
10
-
pectate lyase I and pectate lyase II
10
-
polygalacturonic acid and esterified citrus pectin
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10.5
activity range
3 - 10.5
activity range
3 - 10.5
activity range
3 - 12
-
over 45% of maximal activity within this range
4 - 12
activity range
6 - 10
-
pH 6.0: about 40% of maximal activity, pH 10.0: about 50% of maximal activity, pectate lyase a
6.3 - 7.3
-
assay range
7 - 10
-
pH 7.0: about 35% of maximal activity, pH 10.0: 50% of maximal activity, pectate lyase b
7 - 10
-
pH 7.0: about 40% of maximal activity, pH 10.0: about 60% of maximal activity
7 - 11
activity range
7 - 11
-
activity range
7 - 8
-
pH 7.0: about 35% of maximal activity, pH 8.0: optimum, pH 9.0: no activity
7 - 9
-
pH 7: less than 10% of maximal activity, pH 8.5-9: optimum
7 - 9
-
pH 7.0: about 70% of maximal activity, pH 9.0: about 65% of maximal activity
7.5 - 10
pH 7.5: about 50% of maximal activity, pH 10: about 50% of maximal activity
7.5 - 9.5
-
pH 7.5: enzyme from Alpine strain A15 shows about 40% of maximal activity, pH 9.5: enzyme from Alpine strain A15 shows about 60% of maximal activity; pH 7.5: enzyme from Siberian strain AG25 shows about 40% of maximal activity, pH 9.0: enzyme from Siberian strain AG25 shows about 75% of maximal activity, pH 9.5: enzyme from Siberian strain AG25 shows about 25% of maximal activity
7.6 - 10.4
activity range, recombinant enzyme
8 - 10
-
pH 8: about 35% of maximal activity, pH 10: about 25% of maximal activity
8 - 10
pH 8.0: about 50% of maximal activity, pH 10.0: about 40% of maximal activity
8.3 - 10.3
-
pH 8.3: about 45% of maximal activity, pH 10.3: about 40% of maximal activity
8.5 - 10
-
pH 8.5: about 55% of maximal activity, pH 10.0: about 40% of maximal activity
8.5 - 11.5
pH 8.5: about 35% of maximal activity, pH 11.5: 75% of maximal activity
9 - 11
-
pH 9: about 40% of maximal activity, pH 11: about 50% of maximal activity
9.5 - 11
-
pH 9.5: about 25% of maximal activity, pH 11.0: about 35% of maximal activity with polygalacturonic acid as substrate
9.5 - 11.5
-
about 30% of maximal activity at pH 9.5 and at pH 11.5
9.5 - 12
pH 9.5: about 50% of maximal activity, pH 12.0: about 60% of maximal activity
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 30
-
at pH 9.5
30
-
enzyme from Alpine strain A15; enzyme from Siberian strain AG25
30
-
recombinant His-tagged enzyme
35
Erwinia aroidea
-
-
35
-
pectate lyase C
35
-
Pel III
37
-
assay at
40
-
pectate lyase b
43 - 48
-
without CaCl2
45
-
at pH 8.5
50
-
pectate lyase I
50
-
in a 2 min reaction at pH 9.5
50
-
isoenzyme PelD and pelE
50
-
Pel I; Pel II
50
-
incubation carried out at
50
; isoform PelD; isoform PelE
50 - 55
-
-
55
-
isoenzyme, isoenzyme A
55
-
assay at
60
-
pectate lyase II
60
-
isoenzyme PelB pelC
60
-
at pH 6.0
60
isoform PelB; isoform PelC
60 - 65
-
-
63 - 67
-
0.1 mM CaCl2
65
Clostridium stercorarium
-
75
-
pectate lyase a
75
-
assay at
80
-
pectate lyase b
90
at pH 8.0
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 30
-
a low-temperature-active alkaline pectate lyase, 35% of maximal activity at 0C, maximal activity at 30C
15 - 40
-
15C: about 40% of maximal activity, enzyme from Alpine strain A15, 35C: enzyme from Alpine strain shows about 80% of maximal activity, 40C: enzyme from Alpine strain shows about 55% of maximal activity; 15C: enzyme from Siberian strain AG25 shows about 40% of maximal activity, 35C: enzyme from Siberian strain AG25 shows about 45% of maximal activity, 40C: enzyme from Siberian strain AG25 shows about 10% of maximal activity
22 - 32
-
assay range
30 - 100
activity range
30 - 55
-
about 45% of maximal activity at 30C and at 55C
30 - 60
-
30C: 30% of maximal activity, 40C: 50% of maximal activity, 60C: optimum
30 - 60
-
30C: about 25% of maximal activity, 60C: about 40% of maximal activity
30 - 65
-
30C: about 45% of maximal activity, 65C: about 40% of maximal activity, pectate lyase I
30 - 70
30C: about 35% of maximal activity, 70C: about 20% of maximal activity
30 - 70
about 50% of maximal activity at 30C and at 70C
30 - 70
activity range
30 - 70
activity range
30 - 70
activity range
30 - 70
-
activity range
35 - 70
activity range
35 - 75
activity range, recombinant enzyme, 14.8% of maximal activity at 35C, 18% at 75C
37 - 50
37C: about 85% of maximal activity, 50C: about 75% of maximal activity
37 - 50
-
37C: optimum, 45C: 70% of maximal activity, 50C: 55% of maximal activity
40 - 50
40C: about 50% of maximal activity, 60C: about 25% of maximal activity
40 - 60
more than 50% of maximal activity at 40C and at 60C
40 - 65
-
40C: about 40% of maximal activity, 65C: about 65% of maximal activity
40 - 65
more than 60% of the maximum activity is detectable between 40 and 65C
40 - 70
-
40C: about 40% of maximal activity, 70C: about 30% of maximal activity
40 - 70
-
40C: about 60% of maximal activity, 70C: about 10% of maximal activity
40 - 70
-
40C: about 30% of maximal activity, 45C: about 55% of maximal activity, 70C: about 35% of maximal activity
40 - 70
activity range
45
-
assay at
50 - 70
Clostridium stercorarium
about 30% of maximal activity at 50C and at 70C
50 - 80
-
50C: about 60% of maximal activity, 80C: about 60% of maximal activity
60 - 75
-
50C: about 20% of maximal activity, 60C: about 45% of maximal activity, 75C: about 75% of maximal activity, 80C: about 10% of maximal activity
60 - 85
-
60C: about 55% of maximal activity, 80C: about 90% of maximal activity, 85C: about 20% of maximal activity, pectate lyase a
60 - 90
-
60C: about 45% of maximal activity, 90C: about 30% of maximal activity, pectate lyase b
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
below, Pel I, chromatofocusing on Mono P HR 5/20
4.1
-
pectate lyase II
4.2
-
pectate lyase I
4.2
-
isoelectric focusing
4.4
calculation from nucleotide sequence
4.4
-
Pel II, chromatofocusing on Mono P HR 5/20
4.6
isoelectric focusing; isoform PelA, isoelectric focusing
4.6 - 4.7
isoelectric focusing, pH-gradient: 3.5-9.5
4.7 - 4.8
-
-
5.02
-
Pel III, chromatofocussing on Mono P HR 5/20
5.3
-
isoelectric focusing
6
pI-value around pH 6.0, isoelectric focusing
6.2
-
isoelectric focusing
6.5
-
Pel1, isoelectric focusing
6.7
-
minor pI, isoelectric focusing
6.83
-
sequence calculation
7.1
calculated from amino acid sequence
7.9
isoform PelB, isoelectric focusing
8
-
isoelectric focusing, pH range 3-10
8.2
isoform PelC, isoelectric focusing
8.5
-
2D PAGE, pH-range 3-10
8.5
-
isoelectric focusing
8.6
-
isoelectric focusing
9.1
calculated from amino acid sequence
9.1
-
isoelectric focusing
9.2
isoelectric focusing, pH range: 3-10
9.2
Hspel2, calculated from sequence
9.23
sequence calculation
9.3
Hspel1, calculated from sequence
9.6
-
isoelectric focusing
9.7
-
isoelectric focusing
9.8
isoform PelD, isoelectric focusing
10
-
major pI, isoelectric focusing
10
-
isoelectric focusing
10.3
isoform PelE, isoelectric focusing
10.5
-
isoelectric focusing
additional information
pI of 9.0 or higher
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Erwinia aroidea
-
-
Manually annotated by BRENDA team
-
highest enzyme production in medium supplemented with pectin
Manually annotated by BRENDA team
-
enzyme is detected in the late logarithmic growth phase, enzyme production is highest in the early stationary growth phase. The Alpine strain A15 produces high amounts of enzyme only at a cultivation temperature of 1-10C, with a maximum of enzyme production at 5C. Enzyme production by the Siberian strain AG25 is approximately twice as high than production by the Alpine strain A15; enzyme is detected in the late logarithmic growth phase, enzyme production is highest in the early stationary growth phase. The Siberian strain AG25 produces the enzyme over the growth temperature range of 1-20C, with a maximum of enzyme production at 1C. Enzyme production by the Siberian strain AG25 is approximately twice as high than production by the Alpine strain A15
Manually annotated by BRENDA team
-
54% of the extracellular pectate lyase protein is present in the active state at pH 8
Manually annotated by BRENDA team
-
highest enzyme production in medium supplemented with pectin
-
Manually annotated by BRENDA team
Bacillus sp. KSM-P15, Bacillus subtilis IFO3134
-
-
-
Manually annotated by BRENDA team
Fusarium verticillioides NCIM 1276
-
54% of the extracellular pectate lyase protein is present in the active state at pH 8
-
Manually annotated by BRENDA team
Paenibacillus sp. BP-23
-
highest enzyme production in medium supplemented with pectin
-
Manually annotated by BRENDA team
-
activity peak is observed on the 4th and 10th day of treatment with ethylene and 2,4-dichlorophenoxy acetic acid, respectively, compared to the 16th day in fruits not treated with phytohormone
Manually annotated by BRENDA team
-
transcript is detectable in fruit during ripening. MdPL1 exhibits higher expression before commercial maturity
Manually annotated by BRENDA team
-
the expression pattern of pectate lyase in Fragaria chiloensis reveal a gradual increment in the transcript level between stages 2 and 4, with a higher increment between stages 2 and 3 in Fragaria ananassa than in Fragaria chiloensis (stages 1 and 2 correspond to small, unripe and hard fruit, while stages 3 and 4 correspond to color-breaker and ripening fruit)
Manually annotated by BRENDA team
Musa acuminata Harichhal
-
activity peak is observed on the 4th and 10th day of treatment with ethylene and 2,4-dichlorophenoxy acetic acid, respectively, compared to the 16th day in fruits not treated with phytohormone
-
Manually annotated by BRENDA team
Musa acuminata Nangka
-
ripening
-
Manually annotated by BRENDA team
PEL transcripts are much lower in ovule compared to fibres
Manually annotated by BRENDA team
-
several PLLs are expressed highly in pollen, suggesting a role for these in pollen development and/or function
Manually annotated by BRENDA team
PEL transcripts are much lower in roots compared to fibres
Manually annotated by BRENDA team
-
analysis of expression of all PLL genes in seedlings treated with hormones, abiotic stresses and elicitors of defense responses reveals significant changes in the expression of some PLLs without affecting the other PLLs
Manually annotated by BRENDA team
PEL transcripts are much lower in stem compared to fibres
Manually annotated by BRENDA team
PEL transcripts are much lower in leaf compared to fibres
Manually annotated by BRENDA team
additional information
-
in infected host tissue 0.84%-13.4% of the pectate lyase protein is present in active state
Manually annotated by BRENDA team
additional information
-
analysis of the expression pattern of all AtPLLs in different organs, at different stages of seedling development and in response to various hormones and stresses. The expression of PLLs varies considerably in different organs, with no expression of some PLLs in vegetative organs
Manually annotated by BRENDA team
additional information
transcripts of pectate lyase in the latex of rubber tree at various times after the first tapping is quantified by real-time PCR. Most transcripts are detected on the first day after tapping and then decreased with time
Manually annotated by BRENDA team
additional information
cell wall-modifying and aquaporin gene expression profiles follow similar trends in exocarp and mesocarp tissues throughout berry development, with the exception of the up-regulation of pectin methylesterase, pectate lyase, two aquaporin genes (AQ1 and AQ2), and two expansin genes (EXP3 and EXPL) during stage II, which is delayed in the exocarp tissue compared with mesocarp tissue
Manually annotated by BRENDA team
additional information
-
pectate lyase production in Bacilli studied is modulated by the growth phase and by the carbon source present in the medium, low level expressionin Bacillus cereus
Manually annotated by BRENDA team
additional information
-
pectate lyase production in Bacilli studied is modulated by the growth phase and by the carbon source present in the medium, high level expression in Bacillus pumilus
Manually annotated by BRENDA team
additional information
-
pectate lyase production in Bacilli studied is modulated by the growth phase and by the carbon source present in the medium, high level expression in Bacillus subtilis
Manually annotated by BRENDA team
additional information
-
pectate lyase production in Bacilli studied is modulated by the growth phase and by the carbon source present in the medium. low level expressioni n Bacillus thuringiensis
Manually annotated by BRENDA team
additional information
-
pectate lyase production in Bacilli studied is modulated by the growth phase and by the carbon source present in the medium, high level expression in Bacillus fusiformis
Manually annotated by BRENDA team
additional information
-
pectate lyase production in Bacilli studied is modulated by the growth phase and by the carbon source present in the medium, low level expressionin Bacillus sphaericus
Manually annotated by BRENDA team
additional information
-
highest enzyme expression at 28C culture temperature
Manually annotated by BRENDA team
additional information
-
highest level of Pel1 activity, 434 U/ml, is obtained in a medium supplemented with apple pectin
Manually annotated by BRENDA team
additional information
analysis of the differential expression of pecCl1 during different stages of infectionby the phytopathgen shows a significant increase in pecCl1 expression five days after infection, at the onset of the necrotrophic phase
Manually annotated by BRENDA team
additional information
high cell-density cultivation in 7-L bioreactor, expression profile over time, overview
Manually annotated by BRENDA team
additional information
Fusarium verticillioides NCIM 1276
-
in infected host tissue 0.84%-13.4% of the pectate lyase protein is present in active state
-
Manually annotated by BRENDA team
additional information
Pectobacterium carotovorum ZT0505
-
highest enzyme expression at 28C culture temperature
-
Manually annotated by BRENDA team
additional information
Penicillium occitanis CT1
-
highest level of Pel1 activity, 434 U/ml, is obtained in a medium supplemented with apple pectin
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
over 70% of the activity in cell bound fraction
-
Manually annotated by BRENDA team
Musa acuminata Nangka
-
fruit
-
Manually annotated by BRENDA team
Erwinia aroidea
-
-
-
Manually annotated by BRENDA team
-
secreted during the exponential death phase of growth, just before sporulation
-
Manually annotated by BRENDA team
-
the bacterium secretes four pectate lyases: PLa, PLb, PLc and PLe
-
Manually annotated by BRENDA team
-
54% of the pectate lyase protein is present in the active state at pH 8
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted and injected into the host plant
-
Manually annotated by BRENDA team
the enzyme is secreted and injected into the host plant
-
Manually annotated by BRENDA team
the enzyme is secreted and injected into the host plant
-
Manually annotated by BRENDA team
the enzyme is secreted and injected into the host plant
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted by the Out system
-
Manually annotated by BRENDA team
Bacillus pumilus BK2, Bacillus sp. KSM-P15, Bacillus sp. RK9, Bacillus sp. TS 47
-
-
-
-
Manually annotated by BRENDA team
Bacillus subtilis SO113
-
secreted during the exponential death phase of growth, just before sporulation
-
-
Manually annotated by BRENDA team
Dickeya chrysanthemi 3937
-
isoenzyme PelZ
-
-
Manually annotated by BRENDA team
Dickeya chrysanthemi EC16
-
the bacterium secretes four pectate lyases: PLa, PLb, PLc and PLe
-
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
Fusarium verticillioides NCIM 1276
-
54% of the pectate lyase protein is present in the active state at pH 8
-
-
Manually annotated by BRENDA team
Nocardiopsis sp. TOA-1, Penicillium occitanis CT1
-
-
-
-
Manually annotated by BRENDA team
-
more than 86% of the pectate lyase protein is present in the active state at pH 8
Manually annotated by BRENDA team
Fusarium verticillioides NCIM 1276
-
more than 86% of the pectate lyase protein is present in the active state at pH 8
-
Manually annotated by BRENDA team
-
associated with membranes under certain conditions
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
Dickeya dadantii (strain 3937)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10600
-
ultracentrifugation
706911
11000
-
gel filtration
706911
12100
-
SDS-PAGE
706911
20300
-
analytical ultracentrifugation
37395
23000
-
SDS-PAGE
706911
23900
mature enzyme, electrospray ionization mass spectrometry
702772
23960
mature enzyme, calculated from amino acid sequence
702772
28000
recombinant His-tagged enzyme, SDS-PAGE
702772
30000
-
Pel II, gel filtration
680985
31000
-
SDS-PAGE
706911
32000
-
gel filtration
37393
33000
SDS-PAGE
702760
33400
-
SDS-PAGE
706911
33450
calculated from amino acid sequence
702760
35000
-
SDS-PAGE
691354
35000
-
SDS-PAGE
706911
35200
mature protein, predicted from cDNA
690572
35500
-
Pel III, gel filtration
680985
35940
calculated from amino acid sequence
705099
36000 - 38000
Erwinia aroidea
-
gel filtration
37368
37300
-
SDS-PAGE
706911
37700
mature protein, predicted from cDNA
690572
39000
-
gel filtration
37369
39000
-
gel filtration
37396
40000
gel filtration
682998
42000
SDS-PAGE
705099
42500
isoform PelA, SDS-PAGE
706911
42600
-
Pel I, gel filtration
680985
43000
-
recombinant enzyme, SDS-PAGE
706768
43640
-
deduced from cDNA
690786
43900
predicted from cDNA
694751
44000
-
gel filtration
666570
44000
SDS-PAGE
706911
44300
mature protein, predicted from cDNA
690572
44400
-
SDS-PAGE
706911
45000
-
non-denaturing PAGE
37388
45000
gel filtration
705099
45000
calculated from amino acid sequence
706260
46000
-
-
677646
49900
mature protein, predicted from cDNA
690572
50000
-
SDS-PAGE
706911
54000
-
-
651602
56000
-
SDS-PAGE
706911
64000
gel filtration
650605
68500
-
SDS-PAGE
706911
148000
-
pectate lyase a, non-denaturing PAGE
37383
10000000
-
matrix-assisted laser desorption ionization mass spectrometry
37401
additional information
-
pectate lyase b shows two bands in non-denaturing PAGE: 200000 Da and 252000 Da
37383
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 41000, SDS-PAGE
?
-
x * 74000, SDS-PAGE
?
-
x * 55000, SDS-PAGE
?
-
x * 38000, calculation from DNA sequence of the processed protein; x * 44000, SDS-PAGE
?
-
x * 33355, calculation from nucleotide sequence
?
-
x * 40000, isoenzyme PelZ, SDS-PAGE
?
-
x * 39500, SDS-PAGE
?
-
x * 39500, isoenzymes PelB and PelC, SDS-PAGE; x * 42000, isoenzyme PelD, SDS-PAGE; x * 42500, isoenzymes PelA and PelE, SDS-PAGE
?
-
x * 42000, recombinant enzyme, SDS-PAGE
?
-
x * 43000, SDS-PAGE
?
-
x * 42000, SDS-PAGE
?
-
x * 26000, SDS-PAGE
?
-
x * 40000, isoenzyme PelZ, SDS-PAGE
?
-
x * 23000, pectate lyase D, SDS-PAGE
?
-
x * 39000, isoenzyme PL I and PL II, SDS-PAGE
?
-
x * 37482, pectate lyase B, calculation from nucleotide sequence
?
-
x * 38000, N-terminally His-tagged Pel10Acm, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
x * 33000, SDS-PAGE
?
-
x * 48000, SDS-PAGE
?
-
x * 28000, SDS-PAGE
?
Clostridium stercorarium
x * 135171, calculated from sequence
?
Clostridium stercorarium
x * 133297, recombinant full-length enzyme, SDS-PAGE; x * 58513, recombinantly expressed catalytic module CM9-1, SDS-PAGE; x * 76383, recombinantly expressed catalytic module CM9-2, SDS-PAGE
?
-
x * 37300, SDS-PAGE
?
-
x * 38500, SDS-PAGE
?
-
x * 37500, enzyme from Alpine strain A15, SDS-PAGE; x * 38000, Siberian strain AG25, SDS-PAGE
?
x * 24700, Hspel2, calculated from sequence; x * 26020, Hspel1, calculated from sequence
?
x * 34500-38200, recombinant His-tagged enzyme, SDS-PAGE
?
x * 37556, sequence calculation
?
-
x * 39000, Pel1, SDS-PAGE
?
-
x * 38000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 45498, sequence calculation, x * 38600, mature recombinant enzyme, SDS-PAGE
?
x * 48600-51400, recombinant enzyme from Pichia pastoris, SDS-PAGE, x * 46000, recombinant enzyme from Escherichia coli, SDS-PAGE
?
-
x * 33500, about, sequence calculation, x * 35000, recombinant enzyme, SDS-PAGE
?
Bacillus pumilus BK2
-
x * 37300, SDS-PAGE
-
?
Bacillus pumilus DKS1
-
x * 37556, sequence calculation
-
?
-
x * 26000, SDS-PAGE; x * 33000, SDS-PAGE
-
?
Bacillus sp. KSM-P7
-
x * 33355, calculation from nucleotide sequence
-
?
Bacillus sp. TS 47
-
x * 50000, SDS-PAGE
-
?
Bacillus subtilis 168
-
x * 48600-51400, recombinant enzyme from Pichia pastoris, SDS-PAGE, x * 46000, recombinant enzyme from Escherichia coli, SDS-PAGE
-
?
Bacillus subtilis SO113
-
x * 42000, SDS-PAGE
-
?
Bacillus subtilis TCCC11286
-
x * 45498, sequence calculation, x * 38600, mature recombinant enzyme, SDS-PAGE
-
?
Clostridium stercorarium F-9
-
x * 135171, calculated from sequence
-
?
Dickeya chrysanthemi 3937
-
x * 40000, isoenzyme PelZ, SDS-PAGE
-
?
Paenibacillus campinasensis BL11
-
x * 34500-38200, recombinant His-tagged enzyme, SDS-PAGE
-
?
Penicillium occitanis CT1
-
x * 39000, Pel1, SDS-PAGE
-
?
Xanthomonas campestris ACCC 10048
-
x * 38000, recombinant His-tagged enzyme, SDS-PAGE
-
dimer
-
1 * 93000 + 1 * 158000, pectate lyase b, SDS-PAGE
monomer
-
1 * 135000, pectate lyase a, SDS-PAGE
monomer
-
1 * 35000, SDS-PAGE
monomer
-
1 * 31000, SDS-PAGE
monomer
1 * 70000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 30200, Pel II, SDS-PAGE; 1 * 36300, Pel III, SDS-PAGE; 1 * 41700, Pel I, SDS-PAGE
monomer
1 * 40000, SDS-PAGE
monomer
Aspergillus nidulans GR5
-
1 * 40000, SDS-PAGE
-
monomer
Aspergillus niger MIUG 16
-
1 * 30200, Pel II, SDS-PAGE; 1 * 36300, Pel III, SDS-PAGE; 1 * 41700, Pel I, SDS-PAGE
-
monomer
-
1 * 70000, SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
purification of the recombinant enzyme results in identification of two enzyme forms of which one appears to be N-glycosylated and the other appears to be free of N-glycosylation. The two enzyme forms show identical specific activies
glycoprotein
the enzyme has five putative N-glycosylation sites (Asn-X-Thr/Ser), three near to the N-terminus (N-48, N-127, N-184), and the other two near the C-terminus (N-345, N-351)
glycoprotein
Bacillus subtilis 168
-
the enzyme has five putative N-glycosylation sites (Asn-X-Thr/Ser), three near to the N-terminus (N-48, N-127, N-184), and the other two near the C-terminus (N-345, N-351)
-
glycoprotein
-
-
side-chain modification
-
one putative N-glycosylation site
side-chain modification
-
glycoprotein
side-chain modification
-
neutral sugar content : 2.5% for pectate lyase I and 4.8% for pectate lyase II
glycoprotein
-
Pel1 is 7.7% glycosylated
glycoprotein
Penicillium occitanis CT1
-
Pel1 is 7.7% glycosylated
-
no modification
-
contains no carbohydrate
side-chain modification
-
contains 0.195 mg of glucose equivalents per mg of protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure determined at 1.5 A resolution by the multiple isomorphous replacement method
-
hanging-drop vapour-diffusion method at 4C. Two different crystal forms are obtained. Both forms belong to the orthorhombic space group P2(1)2(1)2(1) and contain one molecule per asymmetric unit. The unit-cell parameters of form I are a = 43.2 A, b * 60.2 A, c = 82.2 A and that of form II are a = 42.9 A, b = 43.4 A and c = 105.9 A
-
hanging-drop vapour-diffusion method using 2-propanol and polyethylene glycol 4000 as precipitant. The crystals belong to the trigonal space group P3(1)21 with unit-cell parameters a = b = 58.8 A, c = 229.7 A, gamma = 120
-
purified enzyme, alone or complexed with trigalacturonate, sitting drop method, 0.002 ml of 12.5 mg/ml protein in 25 mM Tris-HCl, 150 mM NaCl, pH 8.0, are mixed with 0.002 ml of 0.18 M Li2SO4, 0.085 M Tris-HCl, pH 8.5, 24% PEG 4000, and 15% v/v glycerol anhydrous, and equilibrated against 0.5 ml of well solution, three days, X-ray diffraction structure determination and analysis at 1.5-1.9 A resolution
-
R279A mutant, streak seeding pre-equilibrated protein drops, using 0.1 M sodium acetate (pH 4.6), 0.2 M ammonium acetate, and 18% (w/v) PEG 4000, supplemented with 20 mM trigalacturonate, 7 mM calcium chloride, and 15% glycerol as a cryoprotectant
-
purified recombinant N-terminally His6-tagged enzyme, sitting drop vapor diffusion method, mixing of 0.0002 ml of protein containing 15 mg/ml protein, 20 mM acetic acid, pH 5, 100 mM NaCl and 5 mM CaCl2, with 0.0002 ml of well solution, containing 0.2 M ammonium phosphate monobasic, 0.1 M Tris, pH 8.5, and 50% v/v 2-methyl-2,4-pentanediol, 20C, X-ray diffraction structure determination and analysis at 1.5 A resolution, molecular replacement method, modeling
vapour-diffusion using hanging-drop method. The precipitant is 20% w/v monomethyl polyethyleneglycol 2000. Crystals belong to the space group P2(1), with unit-cell parameters a = 47.7 A, b = 106.1 A, c = 55.4 A, beta = 92, and have two molecules in the asymmetric unit. The crystals diffract beyond 12.5 A using synchrotron radiation
-
1.6 A resolution crystal structure
-
crystal structure of PelI is solved to 1.45 A resolution. It consists of an N-terminal domain harboring a fibronectin type III fold linked to a catalytic domain displaying a parallel beta-helix topology. The N-terminal domain is located away from the active site and is not involved in the catalytic process. The structure of PelI in complex with its substrate, a tetragalacturonate, is solved to 2.3 A resolution. The sugar binds from subsites -2 to +2 in one monomer of the asymmetric unit, although it lies on subsites -1 to +3 in the other. These two Michaelis complexes are consistent with the dual mode of bond cleavage in this substrate. The bound sugar adopts a mixed 21 and 31 helical conformation similar to that reported in inactive mutants from families PL-1 and PL-10
crystallographic analysis of 11 enzyme-Ca2+ complexes formed at pH 4.5, 9.5 and 11.2 under varying Ca2+ concentrations, solved and refined at a resolution of 2.2 A
-
hanging-drop vapor-diffusion method, crystal structure of the PelA T1.5 mutant solved to 1.6 and 2.9 A resolution. Four residues in the T1.5 loop region of PelA are mutated (N215S, T217S, S219G and A220S) to match the structurally analogous T1.5 loop of PelE
-
hanging-drop vapour-diffusion method, unit-cell parameters a = 61.6 A, b = 70.7 A, c = 73.4 A, beta = 112.8. Crystals diffract to 1.45 A using synchrotron radiation
-
oligosaccharide substrate alpha-D-GalpA-((1-4)-alpha-D-GalpA)3-(1-4)-D-GalpA trapped in crystals by using the inactive R218K mutant. 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
-
sitting-drop vapour-diffusion method, two crystal forms: monoclinic C2 to 1.8 A and rhombohedral R3 to 21 A
-
vapour-diffusion techniques in presence of polyethylene glycol, recombinant enzyme expressed in Escherichia coli
-
hanging-drop vapour-diffusion method at 4C. The crystals are hexagonal, with unit-cell parameters a = b = 85.55 A, c * 230.13 A, gamma = 120 and belong to space group P6(5)22 or P6(1)22, having one molecule per asymmetric unit
-
vapour-diffusion method, three-dimensional structure is determined at 2.65 A resolution. Crystals are hexagonal, belonging to space group P6(5)22, with unit cell parameters a = b = 85.37 A, c = 231.32 A.
-
purified recombinant PCPEL2, hanging-drop vapour-diffusion method, 16C, 0.001 ml of protein solution containing 5 mg/ml protein in 10 mM Tris-HCl, pH 7.5, 150 mM NaCl and 1 mM DTT, is mixed with 0.001 ml of reservoir solution containing 0.1 M HEPES, pH 7.5, 10% w/v PEG 6000, 5% v/v 2-methy-2,4-pentanediol, equilibration versus 0.2 ml of reservoir solution, 5 days, X-ray diffraction structure determination and analysis
crystallization of mutant enzyme C132I/C156N/C194L, hanging-drop vapour-diffusion method
hanging drop vapor diffusion method at 18C, apo form (1.5 A resolution), a metal-bound form of YePL2A (2.0 A resolution) and a trigalacturonic acid-bound substrate complex (2.1 A resolution)
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
-
37C, 16 h, stable
37393
3 - 10
Clostridium stercorarium
4C, 12 h, stable in the range
664374
3 - 10
Clostridium stercorarium
4C, 12 h, stable
664386
3 - 10
pH ranging from 3.0 to 10.0 does not significantly influence the stability of the enzyme, but the enzyme seems to be more stable at its optimum pH
713825
3 - 10
pH ranging from 3.0 to 10.0 does not significantly influence the stability of the enzyme, but the enzyme seems to be more stable at its optimum pH
713825
3 - 10
pH ranging from 3.0 to 10.0 does not significantly influence the stability of the enzyme, but the enzyme seems to be more stable at its optimum pH
713825
4 - 10
at 4C
702760
4 - 10.4
purified recombinant enzyme, about 50% activity within this range
730852
4 - 11
-
2C, 48 h, stable
37371
4 - 12
-
5C, 24 h, stable
37384
4 - 12
enzymes are stable for 24 h at pH 4-12; enzymes are stable for 24 h at pH 4-12
690572
4 - 12
enzymes are stable for 24 h at pH 4-12; enzymes are stable for 24 h at pH 4-12
690572
5
-
30% loss of activity after 3 h, 90% loss of activity after 24 h
666570
5 - 10
-
2C, 72 h, stable
37369
5 - 11
-
30C, 1 h, with or without CaCl2, stable
37395
6 - 8
-
optimal stability in the range
37401
6 - 8
40C, 1 h, stable
682998
6 - 9
-
stable at 2C for 72 h or at 30C for 3 h
37367
6 - 9.5
-
stable
37382
6.5 - 9.5
-
37C, 2 h
37388
7 - 10
-
purified recombinant His-tagged enzyme, 1 h, 60C, without substrate, 30% activity remaining, at 37-50C over 80% activity remain
730134
7 - 11.5
-
purified recombinant enzyme, 2 h, stable up to pH 9.0, inactivation at pH 11.5
729460
7 - 8.5
Erwinia aroidea
-
30C, stable
37368
7 - 8.5
-
stable
666570
8.2 - 9.8
-
-
706768
8.5 - 11
-
recombinant enzyme shows a wider pH and thermal stability spectrum than the purified pectate lyase from Bacillus subtilis WSHB04-02
690786
9 - 10
-
1 h, 35-40% loss of activity, enzyme from Alpine strain A15 and Siberian strain AG25; 1 h, 35-40% loss of activity, enzyme from Siberian strain AG25
666207
9 - 12
PelA is stable at pH 9.0 and 10.0 and maintains more than 85% activity after incubation at 40C for 1 h, about 50% activity is retained when it is incubated at pH 11.0 and it almost completely loses activity when it is incubated at pH 12.0
705099
9 - 12
-
purified recombinant His-tagged enzyme, 1 h, 60C, without substrate, 30% activity remaining, at 37-50C over 80% activity remain
730134
9.4
-
45C, stable for 300 h
678886
9.5
-
optimal stability, at 65C
37372
9.7
-
45C, about 30% loss of activity after 300 h
678886
10
-
37C, 1 h, 6% loss of activity
37372
10 - 10.5
-
optimal stability, at 45C-55C
37372
10.5
-
45C, about 40% loss of activity after 300 h; 45C, about 55% loss of activity after 300 h
678886
11
-
37C, 1 h, stable
37372
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2
-
48 h, enzyme from Alpine strain A15 loses 21% of initial activity; 48 h, enzyme from Siberian strain AG25 loses 5% of initial activity
666207
30
-
pH 6.0-9.0, 3 h, stable
37367
30
Erwinia aroidea
-
pH 7.0-8.5, stable
37368
30
-
half-life: more than 75 h
665787
30
-
pH 9.0, 15 min, enzyme from Alpine strain A15 loses 40% of initial activity; pH 9.0, 15 min, enzyme from Siberian strain AG25 loses 35% of initial activity
666207
30
-
room temperature, activity is lost within 2 days
666570
30
-
purified recombinant enzyme, pH 9.0, 2 h, over 90% activity remaining
729460
30 - 40
inactivation of recombinant PL I occurs above 30C whereas the activity of native PL I is stable up to 40C
702772
30 - 60
PelA is stable during 30C to 40C and not very stable at 50C (in 50 mM glycine-NaOH buffer, pH 10.0), about 60% activity is retained after 30 min incubation at 50C and it almost completely loses activity when it is incubated at 60C
705099
35 - 45
-
optimal stability
37394
37
-
pH 6.5-9.6, 2 h, stable
37388
37
-
purified recombinant His-tagged enzyme, 1 h, without substrate, pH 12.0, over 58% activity remaining; purified recombinant His-tagged enzyme, 1 h, without substrate, pH 7.0-10.0, over 80% activity remaining
730134
37 - 50
-
purified recombinant His-tagged enzyme, 45 min, without substrate, pH 9.0-12.0, over 80% activity remaining
730134
39
-
transition midpoint of pectate lyase C is 38.9C
649435
40
-
pH 7.0, 10 min, stable below
37371
40
-
10 min, stable
649635
40
pH 10.0, 4 h, retains more than 50% of the initial activity
653150
40
-
pH 9.0, 15 min, enzyme from Alpine strain A15 loses 10% of initial activity; pH 9.0, 15 min, enzyme from Siberian strain AG25 loses 95% of initial activity
666207
40
-
5 min, 5-10% loss of activity
666570
40
-
3 h, 93% loss of activity without CaCl2, 14% loss of activity in presence of 0.1 mM CaCl2
677646
40
purified recombinant His-tagged enzyme, half-life is 288 min at pH 10.0
713765
40
-
purified recombinant enzyme, pH 9.0, 2 h, over 80% activity remaining
729460
40 - 50
-
pH 6.0, 30 min, stable
37393
40 - 70
the enzyme loses 60% of its activity when incubated at 40C for 1 h after treatment with EDTA, thermostability increases to approximately 80% of initial activity at 50 and 70C in the presence of Ca2+ alone and both Ca2+ and polygalacturonic acid, respectively
702760
44
-
transition midpoint of pectate lyase C is 44.3C
649435
45
-
10 min, about 10% loss of activity
649635
45
-
pH 9.4: stable for 300 h. pH 10.0: about 40% loss of activity after 300 h
678886
45
purified recombinant enzyme, 2 h, 64.9% activity remaining, half-life is 360 min
730852
45 - 50
purified recombinant PelN displays a half-life of around 9 h and 42 h at 50C and 45C, respectively
729497
47
-
transition midpoint of pectate lyase C is 46.9C
649435
47
-
20 min, stable
649703
50
Erwinia aroidea
-
10 min, 50% loss of activity
37368
50
-
10 min, pH 7.0, 35% loss of activity
37371
50
-
10 min, stable in absence of Ca2+
37388
50
-
half life: 11 min for isoenzyme PelA, 4 min for isoenzyme PelD, 2 min for isoenzyme PelE
37390
50
-
30 min, stable up to
37395
50
-
1 h, loss of activity
37401
50
-
10 min, about 35% of maximal activity
649635
50
-
stable up to
651603
50
-
stable up to
651604
50
pH 10.0, 4 h, retains only 1% of the initial activity
653150
50
-
stable for 30 min
678886
50
half-life: 1 h
682998
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
713765
50
-
purified recombinant enzyme, 2 h, 90% activity remaining
729460
50
-
recombinant enzyme, 90 min, 50% activity remaining
729926
50
-
purified recombinant His-tagged enzyme, 45 min, without substrate, pH 10.0, over 80% activity remaining
730134
50
purified recombinant enzyme, half-life is 88 min
730852
52
-
20 min, 38% loss of activity
649703
55
-
stable up to, in absence of CaCl2
37384
55
-
10 min, stable in presence of Ca2+
37388
55
-
10 min, about 80% of maximal activity
649635
55
-
enzyme is stable to incubation up to 55C when incubated at various temperatures for 20 min in glycine-NaOH buffer (pH 9.4)
690786
57
-
20 min, complete inactivation
649703
60
-
Ca2+ slightly enhances thermostability up to 60C
37384
60
-
10 min, 50% loss of activity in absence of cations, 10% loss of activity in presence of Mn2+, Ca2+ or polygalacturonic acid
37385
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
37390
60
-
30 min, more than 30% of the activity remains
37398
60
pH 7.5, stable in presence of Ca2+
651060
60
-
pH 9.0, 15 min, about 20% loss of activity
666207
60
readily inactivated above
682998
60
purified recombinant His-tagged enzyme, half-life is 207 min at pH 10.0
713765
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+
716809
60
-
purified recombinant enzyme, pH 9.0, half-life is 20 min, inactivation after 80 min
729460
60
purified enzyme, 20 min, recombinant enzyme from Pichia pastoris retaines 26% activity, recombinant enzyme from Escherichia coli is inactivated
729493
60
-
purified recombinant His-tagged enzyme, 45 min, without substrate, pH 10.0, 30% activity remaining
730134
60 - 95
-
the enzyme keeps stable, possesses a high level of activity at 60C and a half-life of almost 2 h at 95C
706768
65
-
10 min, 50% loss of activity
37394
65
-
half-life: 13 h
650616
70
-
2 h, about 10% loss of activity
37383
70
-
half-life: 1 h
650616
70
Clostridium stercorarium
10 min, stable up to
664374
70
Clostridium stercorarium
pH 7, 10 min, absence of substrate, stable
664386
70
-
pH 9.0, 15 min, 50% loss of activity
666207
70
-
beyond 70C, enzyme activity is severely inhibited. The half-life is 6.93 min at 70C as compared to 31 min at 40C
691354
70
purified recombinant His-tagged enzyme, half-life is 120 min at pH 10.0
713765
70
-
purified recombinant enzyme, pH 9.0, half-life is about 12 min, inactivation after 60 min
729460
75
-
10 min, thermal denaturation is reversible
649635
80
-
half-life: about 60 min
37383
80
-
half-life at pH 8.0 and 7.0 is 1.2 min, half-life at pH 9.0 is 0.8 min
665787
80
-
5 min, complete inactivation
666570
90
-
complete loss of activity after 5 min
37383
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 90C is observed
729417
additional information
-
Ca2+ slightly enhances thermal stability
37377
additional information
-
Ca2+ slightly enhances thermal stability
37395
additional information
-
Ca2+ and sodium polygalacturonate improve thermal stability
37401
additional information
-
thermal denaturation is not reversible. The enzyme has its maximal thermal stability at pH 5, CD-monitored thermal denaturation
649948
additional information
Ca2+ increases thermal stability of the enzyme slightly
651060
additional information
-
improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
729417
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+, Mn2+ or polygalacturonate increase thermostability
-
complete unfolding in 6 M guanidine-HCl
-
pectate lyase B, C and E are denatured by guanidine hydrochloride with transition midpoint concentrations of 1.3 mM, 1.1 mM and 1.8 mM
-
PelN stability is not at all, or only weakly, increased by the addition of Fe2+ or polygalacturonate
-
the enzyme is reversibly unfolded by urea and guanidine-HCl at its optimal pH of 8.5
-
UV-C light blanching (13.8Wm-2UV-C light for 5 min at 4C) allows to non-thermally increase the enzymatic stability of the surface of fresh-cut fruit and vegetables.
-
enzyme from Alpine strain A15 is stable up to fourfold freezing and thawing
-
enzyme from Siberian strain AG25 is stable up to fourfold freezing and thawing
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
bubbling O2 through the enzyme preparation increases activity 63%
-
37377
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 26% loss of activity after 10 days
-
4C, 29% loss of activity after 10 days
-
2-5C, pH 7.0, 0.02 M sodium phosphate buffer, stable for at least 15 days
-
10C, 100 mM ammonium chloride buffer, pH 9.0, stable for 1 month, 70% loss of activity in 20 mM ammonium chloride buffer, pH 9.0, after 24 h
-
-20C, stable for a few weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Pel I; Pel II; Pel III
-
purification of the recombinant enzyme results in identification of two enzyme forms of which one appears to be N-glycosylated and the other appears to be free of N-glycosylation
Ni-NTA column chromatography
-
native enzyme 18.6fold from strain AK2 culture supernatant by cation exchange chromatography and gel filtration
-
an extracellular pectate lyase is purified from the culture filtrate of a newly isolated Bacillus pumilus DKS1 grown in pectin containing medium using ion-exchange and gel filtration chromatography
-
native Pel-22 from supernatant by ammonium sulfate fractionation and cation exchange chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3) plysS 6.64fold by single step cation exchange chromatography to homogeneity
CM-Toyopearl 650M column chromatography, Mono S column chromatography, Resource PHE column chromatography, and ammonium sulfate precipitation, recombinant enzyme is purified by amylase resin column chromatography
DEAE-Sepharose column chromatography
ion exchange chromatography and gel filtration
-
native Pel-66 from supernatant by ammonium sulfate fractionation and cation exchange chromatography
recombinant
-
recombinant enzyme
-
recombinant enzyme 17.3fold from strain WB600 culture supernatant by ammonium sulfate fractionation, cation exchange chromatography, and gel filtration
-
single-step
-
using butyl-Toyopearl 650 column
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, gel filtration, and ultrafiltration
38000 Da N-terminally His-tagged Pel10Acm
-
pectate lyase I and II
-
recombinant
Clostridium stercorarium
5 isoenzymes: PelA, PelB, PelC, PelD, PelE
-
recombinant enzyme
-
wild-type and mutant enzymes
-
-
Erwinia aroidea
-
pectate lyase B; recombinant enzyme
-
pectate lyase C; recombinant enzyme
-
pectate lyase D; recombinant enzyme
-
affinity column chromatography and gel filtration
-
Ni-NTA-agarose column chromatography
native Pel-90 from supernatant by ammonium sulfate fractionation and cation exchange chromatography
recombinant His-tagged Pel-BL11 from Escherichia coli by nickel affinity and anion exchange chromatography
recombinant enzyme PelN 3fold from Escherichia coli strain BL21(DE3)
isoenzyme PL I and PL II
-
pectate lyase I and pectate lyase II
-
pectate lyase III
-
recombinant enzyme
-
native extracellular Pel1 71fold by anion exchange chromatography
-
recombinant His-tagged PCPEL2 from Escherichia coli strain BL21(DE3), 34.1fold from the pLysS system and 53.8fold from the pMal system, by nickel affinity chromatography and gel filtration chromatography, recombinant MBP-PCPEL2 by amylose affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatgraphy
-
Ni-NTA column chromatography, gel filtration
pectate lyase a and pectate lyase b
-
6*His-tagged recombinant enzyme
recombinant His-tagged enzyme 2.47fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chrmatography to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpressed using a promoter fusion with the Aspergillus niger pyruvate kinase promoter
expressed in Escherichia coli
-
DNA and amino acid sequence determnination and analysis
gene pelB, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) plysS
expressed in Escherichia coli BL21(DE3) and DH5alpha cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
DNA and amino acid sequence determnination and analysis
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
gene Bsu11286Pel, DNA and amino acid sequence determination and analysis, recombinant expression in Bacillus subtilis strain WB600
-
gene encoding pectate lyase is amplified by PCR, fused with a periplasmic secretion signal peptide sequence, pelB, from pET22b(+), cloned and expressed in Escherichia coli cells using a temperature control vector, pHsh
-
gene pel168, enzyme expression in Pichia pastoris strain and in Escherichia coli, the latter shows less glycosylation and thermostability
pectate lyase gene fused to the pelB gene encoding the periplasmic secretion signal and the fusion gene is expressed under the control of the T7 promoter in a culture of Escherichia coli BL21DE3
-
recombinantly expressed in Pichia pastoris
-
recombinantly expressed in Pichia pastoris. The ratio of methanol to cell concentration has a significant influence on PGL production. An advanced glycerol exponential feeding strategy is developed for biomass accumulation in cell growth phase, by which cell concentration reaches 140 g/L after 19 h glycerol feeding. In subsequent production phase, a methanol feeding profile is proposed according to the optimal ratio of methanol to cell concentration at a range of 0.163-0.171 g/g, and PGL activity and productivity reaches 430 U/ml and 4.34 U/ml/h, respectively
-
pectate lyase BxPEL1; pectate lyase BxPEL2
recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
expression in Escherichia coli
-
-
Clostridium stercorarium
full-length enzyme and catalytic modules CM9-1 and CM9-2 are separately expressed in Escherichia coli
Clostridium stercorarium
gene pelA from isolate US-41, DNA and amino acid sequence determinationand analysis, expression and promoter analysis, overexpression of CcpelA in Si-60 under the regulation of the promoter Pgpd. The CcpelA promoter of US-41, but not Si-60, contains a putative AreA-binding motif, GATA box. Point mutation in the Si-60 GATA box might prevent positive regulation of CcpelA by the AreA transcription factor, leading to slower gene expression and delayed CcPelA secretion
-
gene pecCl1, DNA amino acid sequence determination and analysis, phylogenetic analysis, possible cis-regulatory elements and transcription factor binding sites that may be involved in the regulation of genetic expression were detected in the promoter region of the gene
expressed in Escherichia coli
overproduced in Escherichia coli
-
pectate lyase A, pectate lyase B, pectate lyase C and pectate lyase E, expression in Escherichia coli
-
gene pelN, overexpression in Escherichia coli strain BL21(DE3) in the periplasmic space from pNA13
-
expressed in the transgenic strawberry lines Pel 1 and Pel 3
-
pectate lyase B, expression in Pichia pastoris
-
pectate lyase C, expression in Pichia pastoris; pectate lyase D, expression in Pichia pastoris
-
gene pel-2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
-
gene pel-2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
gene pel-2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
transient expression of Gr-Pel2 in leaves of Nicotiana benthamiana results in severe malformations of the infiltrated tissues, not relating to maceration and soft rot symptom
-
gene pel-2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
expressed in Escherichia coli
Hspel1 full-length cDNA sequence; Hspel2 full-length cDNA sequence
expressed in Escherichia coli
DNA and amino acid sequence determnination and analysis
expressed in Escherichia coli
-
expressed in Escherichia coli
-
DNA and amino acid sequence determination and analysis, expression of His-tagged Pel-BL11 in Escherichia coli pET25b
gene pelN, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in recombinant Escherichia coli strain BL21(DE3)
expression in Escherichia coli
-
pectate lyase B
-
gene Pcpel2, DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli BL21(DE3) using the pMAL or pLysS system, expression of maltose binding fusion protein, MBP-PCPEL2
none of the 10 Pseudomonas syringae pv. glycinea strains examined exhibits pectolytic activity. The pectate lyase gene is detected in four out of four strains examined. The pel gene contains a single-base insertion, a double-base insertion, and an 18-bp deletion, which can lead to the synthesis of an inactive pectate lyase protein. The function of the protein can be restored by removing the unwanted base insertion and by filling in the 18-bp deletions by site-directed mutagenesis and expression in Escherichia coli
-
gene pl-str, DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3), subcloning in Escherichia coli strain JM109
-
expressed in Escherichia coli Origami cells
expressed in Escherichia coli JM109 cells
-
expression in Bacillus licheniformis
expression in Escherichia coli
gene pelB, DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli strain DH5alpha, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
-
enzyme from strain ATCC49397 overproduced in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the production of enzyme increases significantly with increasing calcium-alginate concentration and reaches a maximum enzyme yield of 38.5 units/ml at 18 g/l
-
the production of enzyme increases significantly with increasing calcium-alginate concentration and reaches a maximum enzyme yield of 38.5 units/ml at 18 g/l
Bacillus pumilus DKS1
-
-
analysis of the differential expression of pecCl1 during different stages of infection shows a significant increase in pecCl1 expression five days after infection, at the onset of the necrotrophic phase
RpoS downregulates pelD expression of in planta, RpoS negatively regulates pelD promoter activity
-
the pelN expression is comtrolled by the repressors KdgR and PecS and is affected by different environmental conditions, such as pH, osmolarity, and temperature
-
the enzyme expression is controlled and activated by activator GacA
-
RpoS downregulates pelD expression of in planta, RpoS negatively regulates pelD promoter activity
-
-
the PEL gene is preferentially expressed in fibers at 10 days-post anthesis
isolate Phytophthora capsici SD33 shows an approximately 8fold increase of pectate lyase activity grown on pepper extract plus pectin compared with those on pectin alone as carbon source
-
polygalacturonic acid and CaCl2 induce the expression of the pelA1 gene, cAMP receptor protein-like protein and RpfF (an enoyl-CoA hydratase homologue that is required for the synthesis of cis-11-methyl-2-dodecenoic acid) positively regulate pelA1 transcription
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R235A
site-directed mutagenesis, inactive catalytic residue mutant
R235A
Bacillus pumilus DKS1
-
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
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
-
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
N180A
-
the mutation results in approximately 30% of wild type activity
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
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inactive but correctly folded enzyme
N215S/T217S/S219G/A220S
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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
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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
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mutant enzyme with 0.2% of the activity of the wild-type enzyme
R236Q
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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
C132I/C156N/C194L
mutations increase expression level
additional information
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improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
additional information
Bacillus megaterium AK2
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improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
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K89A
the ratio of turnover number to Km-value is 31.5% 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
K89A
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the ratio of turnover number to Km-value is 31.5% of the wild-type value
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additional information
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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
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R279A
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inactive
additional information
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construction of CcpelA gene-disrupted mutants, the mutants show reduced aggressiveness towards tomato fruits and impaired pectate lyase secretion and extracellular activity
additional information
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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
N215S/T217S/S219G/A220S
Dickeya chrysanthemi EC16
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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
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additional information
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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
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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
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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
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additional information
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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
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
after complete unfolding in 6 M guanidine-HCl and removal of the denaturant by dialysis, the enzymatic activity of pelC is regained and is identical to that of freshly purified enzyme. Thermal denaturation is not reversible
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thermal denaturation at 75C for 10 min is reversible. The enzyme is reversibly unfolded by urea and guanidine-HCl at its optimal pH of 8.5
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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the enzyme can be used for bioscouring of cotton
biotechnology
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a combined (enzymatic and chemical) process using a Bacillus pumilus strain (DKS1), isolated from the soil, is used to degum ramie bast fibres. Results indicate the process provides an economical and eco-friendly method for the small scale as well as large-scale degumming of decorticated ramie fibre. Results are of importance for the textile as well as paper industry
industry
the thermoactive pectate lyase from strain DKS1 of Bacillus pumilus has a potential use for degumming ramie fiber, the purified pectate lyase causes a weight loss of the ramie fibre of 25%. Arg235 is an essential catalytic residue to degumming ramie fibre
biotechnology
Bacillus pumilus BK2
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the enzyme can be used for bioscouring of cotton
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industry
Bacillus pumilus DKS1
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the thermoactive pectate lyase from strain DKS1 of Bacillus pumilus has a potential use for degumming ramie fiber, the purified pectate lyase causes a weight loss of the ramie fibre of 25%. Arg235 is an essential catalytic residue to degumming ramie fibre
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biotechnology
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application of a commercial pectinase for a range of concentrations and treatment times creates pectin-free textiles with low wax content. Assessment of physicochemical properties such as, wettability, whiteness index, polymerization degree, crystallinity index, color depth, as well as low-stress mechanical properties, proves that bioscouring can be as much efficient as the conventional alkaline treatment
degradation
useful for degradation of pectin networks at high temperatures
industry
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pectate lyase (Bsp165PelA) from Bacillus sp. N16-5 has a great potential in industrial applications because it shows high specific activity under extremely alkaline conditions
industry
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pectate lyase (Bsp165PelA) from Bacillus sp. N16-5 has a great potential in industrial applications because it shows high specific activity under extremely alkaline conditions
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degradation
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useful for degradation of pectin networks at high temperatures
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biotechnology
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enhancing PGL production by controlling the optimal ratio provides an alternative approach to enhance heterologous protein production with Pichia pastoris
environmental protection
the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption
industry
the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption
environmental protection
Bacillus subtilis 168
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the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption
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industry
Bacillus subtilis 168
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the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption
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molecular biology
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pH-regulated response is only part of a multi-factor regulation of PELB. Sugars are also needed to promote the transition from quiescent to active necrotrophic development by the pathogen
biotechnology
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parameters for maximum production of PGL by yeast strain Debaryomyces nepalensis in bioreactor are determined: optimal levels of pH, aeration and agitation rate is found to be 7.0, 300 rpm and 1 vvm, respectively. Combined feeding of inducer (lemon peel) and carbon source (galactose) at 12 h is the best strategy for enhanced production of PGL. The production is increased by 1.8fold and productivity 1.4fold for PGL when compared to batch culture
molecular biology
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virulence factors, including pectate lyase (Pel),exoprotease, tabtoxin, and syringomycin production, are found to be regulated by GacS/GacA homologues in phytopathogens
molecular biology
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the increase in expression of both pectate lyase correlates well with the decrease in firmness observed in the fruit
food industry
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inhibition of the pectate lyase gene improves postharvest behavior of strawberries
food industry
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effects of pectate lyase-silencing in tissue integrity increases the content of large particles in juice, its viscoelastic properties being modified and its viscosity increased
food industry
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firmness of full ripen strawberry fruits from Pel lines is significantly higher than control fruits, while color and soluble solids are not affected. The increase of firmness in Pel lines is maintained when ripe fruits are stored for 3 days at 25C
molecular biology
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pectate lyase plays an important degradative role in the primary wall and middle lamella in ripening strawberry fruit, and should be included in synergistic models of cell wall disassembly
agriculture
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during infection controlling of pectate lyase and pectin lyase activities by host sap pH or oligogalacturonides would be the best mechanism to control Fusarium colonization or infection
agriculture
Fusarium verticillioides NCIM 1276
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during infection controlling of pectate lyase and pectin lyase activities by host sap pH or oligogalacturonides would be the best mechanism to control Fusarium colonization or infection
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industry
enzyme treatment in fibre degumming validated by weight loss in gampi and paper mulberry fibres
industry
Paenibacillus campinasensis BL11
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enzyme treatment in fibre degumming validated by weight loss in gampi and paper mulberry fibres
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biotechnology
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the pectinase preparation from Bacillus macerans can compete with the commercial preparations for the process of cotton fabric boil off
environmental protection
biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process
industry
biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process
environmental protection
-
biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process
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industry
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biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process
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biotechnology
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optimization of fermentation conditions
biotechnology
Pectobacterium carotovorum IFO3830
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optimization of fermentation conditions
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environmental protection
alkaline pectate lyases play an important role in mild and eco-friendly bioscouring pretreatment processes in the textile industry. So far, only a few pectate lyases can be applied in industrial-scale production, and many of them exhibit high production cost, low activity, and/or do not meet the treatment requirements. Recombinant PelB has with promising properties for use in bioscouring in the textile pretreatment process and is a potential enzyme for industrial applications