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Information on EC 4.2.2.22 - pectate trisaccharide-lyase
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4.2.2.22 pectate trisaccharide-lyaseIUBMB 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 .
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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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
exopectate lyase
exopectate-lyase
pectate lyase A
pectate transeliminase
Pel
PelA
Tm0433
pectate lyase A
is a subunit of the extracellular multienzyme complex, called the cellulosome
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
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SYSTEMATIC NAME
IUBMB Comments
(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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CAS REGISTRY NUMBER
COMMENTARY
9015-75-2
cf. EC 4.2.2.2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
unsaturated (1,4-alpha-D-galacturonide)3 + unsaturated (1,4-alpha-D-galacturonide)2
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-
-
-
?
pectin
?
-
low-esterified pectin is the optimum substrate for the PelA, higher-esterified pectin is hardly cleaved
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-
?
pectin
?
-
low-esterified pectin is the optimum substrate for the PelA, higher-esterified pectin is hardly cleaved
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-
?
pectin
?
-
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
?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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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 trigalacturonate
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pectins with an increasing degree of methylation are degraded at a decreasing rate
-
-
?
pectin
unsaturated trigalacturonate
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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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
-
-
?
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
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
-
?
polygalacturonic acid
unsaturated trigalacturonate
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main product
-
?
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
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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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
?
-
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
?
-
-
PelA shows petate lyase activity in vitro
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
pectin
?
-
the ability of Thermotoga maritima to grow on pectin as sole carbon source coincides with the secretion of a pectate lyase A
-
-
?
pectin
?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
-
utilizes a metal atom other than calcium for catalysis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Ki-value for polygalacturonic acid is 1.08 g/l
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
more than 50% of maximal activity at 40°C and at 60°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
PelA knockout mutants do not show significant differences in virulence compared to the wild-type strains during infection of Triticum aestivum plants
Show AA Sequence and Transmembrane Helices (122 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
precursor undergoes N-terminal processing by cleavage at a putative site between alanine and serine residues
proteolytic modification
-
precursor undergoes N-terminal processing by cleavage at a putative site between alanine and serine residues
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, in 30% polyethylene glycol 1500 and 0.1 M sodium citrate, pH 5.0
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the recombinant protein using Ni2+-nitrilotriacetateagarose column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag
overexpression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
industry
synthesis
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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)
-
brenda
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
-
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)
brenda
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Release 2023.1 (January 2023)
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