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EC Tree
IUBMB Comments Differs in specificity from EC 4.2.2.9, pectate disaccharide-lyase, as the predominant action is removal of a trisaccharide rather than a disaccharide from the reducing end. Disaccharides and tetrasaccharides may also be removed .
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate
Synonyms
alpha-1,4-endo-poly-GalA lyase, exopectate lyase, exopectate-lyase, pectate lyase 2A, pectate lyase A, pectate transeliminase, Pel, PelA, PL2A, Tm0433,
more
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alpha-1,4-endo-poly-GalA lyase
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exopectate lyase
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exopectate-lyase
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pectate lyase A
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pectate lyase A
is a subunit of the extracellular multienzyme complex, called the cellulosome
pectate transeliminase
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pectate transeliminase
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Pel
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PelA
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Tm0433
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eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate
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elimination
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(1->4)-alpha-D-galacturonan reducing-end-trisaccharide-lyase
Differs in specificity from EC 4.2.2.9, pectate disaccharide-lyase, as the predominant action is removal of a trisaccharide rather than a disaccharide from the reducing end. Disaccharides and tetrasaccharides may also be removed [2].
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pectin
unsaturated (1,4-alpha-D-galacturonide)3
pectin
unsaturated trigalacturonate
polygalacturonic acid
(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-(1->4)-(alpha-D-galactopyranosyluronic acid)-(1->4)-alpha-D-galactopyranuronic acid
polygalacturonic acid
4,5-unsaturated polygalacturonic acid
polygalacturonic acid
trigalacturonic acid + digalacturonic acid
polygalacturonic acid
unsaturated (1,4-alpha-D-galacturonide)3 + unsaturated (1,4-alpha-D-galacturonide)2
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?
polygalacturonic acid
unsaturated trigalacturonate
rhamnogalacturonan
?
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?
additional information
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pectin
?
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low-esterified pectin is the optimum substrate for the PelA, higher-esterified pectin is hardly cleaved
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pectin
?
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low-esterified pectin is the optimum substrate for the PelA, higher-esterified pectin is hardly cleaved
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pectin
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the ability of Thermotoga maritima to grow on pectin as sole carbon source coincides with the secretion of a pectate lyase A
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pectin
?
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the ability of Thermotoga maritima to grow on pectin as sole carbon source coincides with the secretion of a pectate lyase A
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?
pectin
unsaturated (1,4-alpha-D-galacturonide)3
the enzyme mainly degrades unesterified acidic pectin rather than esterified (90%) pectin
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?
pectin
unsaturated (1,4-alpha-D-galacturonide)3
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?
pectin
unsaturated trigalacturonate
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pectins with an increasing degree of methylation are degraded at a decreasing rate
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pectin
unsaturated trigalacturonate
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pectins with an increasing degree of methylation are degraded at a decreasing rate
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?
polygalacturonic acid
(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-(1->4)-(alpha-D-galactopyranosyluronic acid)-(1->4)-alpha-D-galactopyranuronic acid
the enzyme catalyzes selectively a x01-4,5 elimination at the third galacturonic unit from the reducing end of polygalacturonic acid by producing (4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-(1->4)-(alpha-D-galactopyranosyluronic acid)-(1->4)-alpha-D-galactopyranuronic acid with a 60% yield
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?
polygalacturonic acid
(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-(1->4)-(alpha-D-galactopyranosyluronic acid)-(1->4)-alpha-D-galactopyranuronic acid
the enzyme catalyzes selectively a x01-4,5 elimination at the third galacturonic unit from the reducing end of polygalacturonic acid by producing (4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-(1->4)-(alpha-D-galactopyranosyluronic acid)-(1->4)-alpha-D-galactopyranuronic acid with a 60% yield
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?
polygalacturonic acid
4,5-unsaturated polygalacturonic acid
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?
polygalacturonic acid
4,5-unsaturated polygalacturonic acid
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?
polygalacturonic acid
trigalacturonic acid + digalacturonic acid
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?
polygalacturonic acid
trigalacturonic acid + digalacturonic acid
pectate lyase A is a subunit of the extracellular multienzyme complex, called the cellulosome, which is involved in plant cell wall degradation
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?
polygalacturonic acid
unsaturated trigalacturonate
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main product
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?
polygalacturonic acid
unsaturated trigalacturonate
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main product
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?
polygalacturonic acid
unsaturated trigalacturonate
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the enzyme attacks from the reducing end, since only unsaturated trigalacturonic acid is formed, followed by slight formation of unsaturated digalacturonate
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?
polygalacturonic acid
unsaturated trigalacturonate
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the enzyme attacks from the reducing end, since only unsaturated trigalacturonic acid is formed, followed by slight formation of unsaturated digalacturonate
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?
additional information
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cellulose carboxymethyl sodium salt, D-xyloglucan, 1-3,1-4-beta-D-glucan, D-xylan, and D-arabinoxylan are no substrates
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?
additional information
?
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PelA shows petate lyase activity in vitro
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?
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polygalacturonic acid
trigalacturonic acid + digalacturonic acid
pectate lyase A is a subunit of the extracellular multienzyme complex, called the cellulosome, which is involved in plant cell wall degradation
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?
pectin
?
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the ability of Thermotoga maritima to grow on pectin as sole carbon source coincides with the secretion of a pectate lyase A
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?
pectin
?
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the ability of Thermotoga maritima to grow on pectin as sole carbon source coincides with the secretion of a pectate lyase A
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?
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CaCl2
optimal activity at 0.05-0.5 mM
NaCl
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highest activity at 200 mM
additional information
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utilizes a metal atom other than calcium for catalysis
Ca2+
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stimulating
Ca2+
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best at 0.5 mM CaCl2
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CaCl2
1 mM reduces activity to less than that without addition of CaCl2
polygalacturonic acid
recombinant fusion protein containing a C-terminal His-tag is inhibited by excess substrate
EDTA
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EDTA
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PL2A activity is ablated upon the addition of EDTA
EGTA
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1 mM, complete inhibition
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0.06
polygalacturonic acid
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additional information
additional information
Km-value for polygalacturonic acid is 0.56 g/l, recombinant fusion protein containing a C-terminal His-tag
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additional information
additional information
Ki-value for polygalacturonic acid is 1.08 g/l
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57.3
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polygalacturonic acid
6.37
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90% esterified pectin
6.38
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60% esterified pectin
63.7
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30% esterified pectin
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8.5
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7 - 8
pH 7.0: less than 30% of maximal activity, pH 8.0: optimum
8.5 - 10
pH 8.5: about 70% of maximal activity, pH 10.0: about 50% of maximal activity. Below pH 7 or above pH 11, no appreciable activity can be detected
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65
recombinant fusion protein containing a C-terminal His-tag
50
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40 - 60
more than 50% of maximal activity at 40°C and at 60°C
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GR5
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SwissProt
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SwissProt
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ATCC 35296
SwissProt
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SwissProt
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subspecies Yersinia enterocolitica 8081
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fragment, formerly Aspergillus nidulans
UniProt
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GR5
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SwissProt
brenda
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brenda
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brenda
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malfunction
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PelA knockout mutants do not show significant differences in virulence compared to the wild-type strains during infection of Triticum aestivum plants
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33451
x * 33451, calculated from sequence
36000
x * 36000, SDS-PAGE
42000
x * 42000, SDS-PAGE
40000
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SDS-PAGE, Sephadex G-100 chromatography
40000
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4 * 40000, SDS-PAGE
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?
x * 36000, SDS-PAGE
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x * 33451, calculated from sequence
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x * 36000, SDS-PAGE
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x * 33451, calculated from sequence
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?
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x * 42000, SDS-PAGE
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tetramer
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4 * 40000, SDS-PAGE
tetramer
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4 * 40000, SDS-PAGE
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proteolytic modification
precursor undergoes N-terminal processing by cleavage at a putative site between alanine and serine residues
proteolytic modification
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precursor undergoes N-terminal processing by cleavage at a putative site between alanine and serine residues
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hanging drop vapour diffusion method, in 30% polyethylene glycol 1500 and 0.1 M sodium citrate, pH 5.0
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additional information
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construction of PelA knockout mutants
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103
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apparent melting temperature
100
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2 min, 50% loss of activity
100
the enzyme loses 50% of its initial activity within 30 min
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the recombinant protein using Ni2+-nitrilotriacetateagarose column chromatography
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expressed in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag
overexpressed in Escherichia coli
overexpression in Escherichia coli
overexpression in Escherichia coli
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overexpression in Escherichia coli
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industry
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food and textile industry
industry
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food and textile industry
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synthesis
the highly thermostable enzyme constitutes a useful catalyst for a simplified synthesis of (4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-(1->4)-(alpha-D-galactopyranosyluronic acid)-(1->4)-alpha-D-galactopyranuronic acid which is extremely difficult to obtain via chemical synthesis
synthesis
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the highly thermostable enzyme constitutes a useful catalyst for a simplified synthesis of (4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-(1->4)-(alpha-D-galactopyranosyluronic acid)-(1->4)-alpha-D-galactopyranuronic acid which is extremely difficult to obtain via chemical synthesis
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Kluskens, L.D.; van Alebeek, G.J.; Voragen, A.G.; de Vos, W.M.; van der Oost, J.
Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima
Biochem. J.
370
651-659
2003
Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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Tamaru, Y.; Doi, R.H.
Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome
Proc. Natl. Acad. Sci. USA
27
4125-4129
2001
Clostridium cellulovorans (Q9AQF3)
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Berensmeier, S.; Singh, S.A.; Meens, J.; Buchholz, K.
Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase
Appl. Microbiol. Biotechnol.
64
560-567
2004
Bacillus licheniformis (Q8GCB2), Bacillus licheniformis 14A (Q8GCB2)
brenda
Abbott, D.W.; Boraston, A.B.
A family 2 pectate lyase displays a rare fold and transition metal-assisted beta-elimination
J. Biol. Chem.
282
35328-35336
2007
Yersinia enterocolitica
brenda
Zhao, Q.; Yuan, S.; Zhang, Y.; Zhu, H.; Dai, C.; Yang, F.; Han, F.
Expression, purification and characterization of pectate lyase A from Aspergillus nidulans in Escherichia coli
World J. Microbiol. Biotechnol.
23
1057-1064
2007
Aspergillus nidulans, Aspergillus nidulans GR5
brenda
Zhao, Q.; Yuan, S.; Wang, X.; Zhang, Y.; Zhu, H.; Lu, C.
Restoration of mature etiolated cucumber hypocotyl cell wall susceptibility to expansin by pretreatment with fungal pectinases and EGTA in vitro
Plant Physiol.
147
1874-1885
2008
Aspergillus nidulans (A4L7I1)
brenda
Yao, S.; Jia, L.; Zhang, X.; Zhang, D.; Xu, L.
Biological function analysis of a pectate lyase PelA in Fusarium graminearum
Plant Physiol. J.
50
243-252
2014
Fusarium graminearum
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brenda
Parisot, J.; Ghochikyan, A.; Langlois, V.; Sakanyan, V.; Rabiller, C.
Exopolygalacturonate lyase from Thermotoga maritima Cloning, characterization and organic synthesis application
Carbohydr. Res.
337
1427-1433
2002
Thermotoga maritima (Q9WYR4), Thermotoga maritima DSM 3109 (Q9WYR4)
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