Any feedback?
Information on EC 4.2.2.22 - pectate trisaccharide-lyase and Organism(s) Thermotoga maritima and UniProt Accession Q9WYR4
for references in articles please use BRENDA:EC4.2.2.22Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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 .
Specify your search results
The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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
top
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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].
CAS REGISTRY NUMBER
COMMENTARY
9015-75-2
cf. EC 4.2.2.2
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
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
-
-
?
pectin
?
-
the ability of Thermotoga maritima to grow on pectin as sole carbon source coincides with the secretion of a pectate lyase A
-
-
?
pectin
unsaturated trigalacturonate
-
pectins with an increasing degree of methylation are degraded at a decreasing rate
-
-
?
polygalacturonic acid
unsaturated trigalacturonate
-
the enzyme attacks from the reducing end, since only unsaturated trigalacturonic acid is formed, followed by slight formation of unsaturated digalacturonate
-
-
?
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
pectin
?
-
the ability of Thermotoga maritima to grow on pectin as sole carbon source coincides with the secretion of a pectate lyase A
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
precursor undergoes N-terminal processing by cleavage at a putative site between alanine and serine residues
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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)
EXTERNAL LINKS (specific for EC-Number 4.2.2.22)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
