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Information on EC 4.2.2.14 - glucuronan lyase
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EC Tree
4.2.2.14 glucuronan lyaseSpecify your search results
Word Map
- 4.2.2.14
- glucuronans
- trichoderma
- polysaccharide
- meliloti
-
depolymerization
- synthesis
- unsaturated
- reesei
- oligosaccharides
-
sinorhizobium
- oligomers
-
ncimb
- chitinase
-
4,5-unsaturated
-
glucuronic
- alginate
-
deacetylated
- glycoside
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
glucuronan lyase, endopolyglucuronate lyase, gl2 glucuronan lyase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1,4)-beta-D-glucuronan lyase
(1->4)-beta-D-glucuronan lyase
-
-
-
-
endopolyglucuronate lyase
glucuronan lyase
(1,4)-beta-D-glucuronan lyase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[1,4-beta-D-Glucuronan]4n = n-1 4-deoxy-beta-D-gluc-4-enuronosyl-[1,4-beta-D-GlcA]3 + [1,4-beta-D-Glucuronan]4
[1,4-beta-D-Glucuronan]4n = n-1 4-deoxy-beta-D-gluc-4-enuronosyl-[1,4-beta-D-GlcA]3 + [1,4-beta-D-Glucuronan]4
-
-
-
-
[1,4-beta-D-Glucuronan]4n = n-1 4-deoxy-beta-D-gluc-4-enuronosyl-[1,4-beta-D-GlcA]3 + [1,4-beta-D-Glucuronan]4
complete degradation of glucuronans results in the formation of tetrasaccharides
-
[1,4-beta-D-Glucuronan]4n = n-1 4-deoxy-beta-D-gluc-4-enuronosyl-[1,4-beta-D-GlcA]3 + [1,4-beta-D-Glucuronan]4
complete degradation of glucuronans results in the formation of tetrasaccharides
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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)-beta-D-glucuronan lyase
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CAS REGISTRY NUMBER
COMMENTARY
193766-71-1
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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
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
cellouronate
?
substrate specificity of recombinant TrGL is examined using various polyuronates, including alginate, hyaluronate, pectin, polygalacturonic acid, amylouronate, and carboxymethyl cellulose. Results indicate that there is high substrate specificity of the enzyme for cellouronate
-
-
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
glucuronan
4-deoxy-beta-D-hex-4-enopyranosylglucuronate-(1-4)-O-beta-D-glucuropyranosyluronate-(1-4)-O-beta-D-glucuropyranosyluronate + ?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
-
-
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
-
-
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
-
-
-
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
-
-
-
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
-
-
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
-
-
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
-
-
-
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
-
-
-
?
deacetylated polyglucuronate
4,5-unsaturated oligoglucuronates
-
beta-(1-4)-linked, best substrate, enzyme shows specific endopolyglucuronate lyase activity
-
?
deacetylated polyglucuronate
4,5-unsaturated oligoglucuronates
-
beta-(1-4)-linked, best substrate, enzyme shows specific endopolyglucuronate lyase activity
-
?
glucuronan
4-deoxy-beta-D-hex-4-enopyranosylglucuronate-(1-4)-O-beta-D-glucuropyranosyluronate-(1-4)-O-beta-D-glucuropyranosyluronate + ?
-
-
-
-
?
glucuronan
4-deoxy-beta-D-hex-4-enopyranosylglucuronate-(1-4)-O-beta-D-glucuropyranosyluronate-(1-4)-O-beta-D-glucuropyranosyluronate + ?
-
-
-
-
?
additional information
?
-
-
no activity with polyglucuronate methyl ester alpha-(1-4)-linked, hyaluronate beta-(1-3), beta(1-4)-linked, glucogluronan beta-(1-3), beta(1-4)-linked, alpha-L-guluronate blocks alpha-(1-4)-linked, beta-D-mannuronate blocks beta(1-4)-linked, 2,3-di-O-acetylated glucuronan beta(1-4)-linked, glucuronan beta(1-4)-linked
-
?
additional information
?
-
-
no activity with polyglucuronate methyl ester alpha-(1-4)-linked, hyaluronate beta-(1-3), beta(1-4)-linked, glucogluronan beta-(1-3), beta(1-4)-linked, alpha-L-guluronate blocks alpha-(1-4)-linked, beta-D-mannuronate blocks beta(1-4)-linked, 2,3-di-O-acetylated glucuronan beta(1-4)-linked, glucuronan beta(1-4)-linked
-
?
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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
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
-
-
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
-
enzyme appears not to be really affected by ionic strength variations. The optimum is 300 mM concentration of potassium acetate buffer
Ca2+
activity and thermostability increases in the presence of Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
immobilized glucuronan lyase activity is calculated for deacetylated glucuronan. The activity is 1300times less than the theoretical immobilized activity. Activity decreases 4times and 14times for native and highly acetylated glucuronans, respectively
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PL_STRMK
Stenotrophomonas maltophilia (strain K279a)
331
0
36696
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 20% (w/v) PEG3350 and 0.2 M ammonium citrate buffer (pH 5.0)
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
enzyme activity remains after incubation at 10 to 40°C for 10 min, but approximately 60% of the activity is lost at 50°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after 4 h of immobilization on activated epoxy-Sepharose, no decrease of activity is measured in the buffer containing epoxy activated Sepharose, immobilizations on CNBr and NHS activated matrices show a rapid decrease of the glucuronan lyase activity in coupling buffers
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
phenyl-Toyopearl column chromatography and SuperQ-Toyopearl column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
a glucuronan lyase is immobilized on a monolithic Convective Interaction Media disk. Degradations of three glucuronans with various O-acetylation degrees is investigated and compared with degradations using free enzyme. The immobilized glucuronan lyase is inhibited by the O-acetylation degree like the free enzyme. 1H NMR analyses are used to study the O-acetylation degree of oligoglucuronans and demonstrate that the average degrees of polymerization are inclusive between 4 and 13 after 24 h of degradation. This first immobilization of a glucuronan lyase constitutes a tool to produce oligoglucuronans
synthesis
synthesis
-
production of oligoglucuronans by enzymatic depolymerization of nascent glucuronan
synthesis
-
production of highly O-acetylated oligoglucuronan in order to envisage new therapeutic applications fields such as the realization of biological tests among animals and vegetals
synthesis
-
production of oligoglucuronans by enzymatic depolymerization of nascent glucuronan
-
synthesis
-
production of highly O-acetylated oligoglucuronan in order to envisage new therapeutic applications fields such as the realization of biological tests among animals and vegetals
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Michaud, P.; Pheulpin, P.; Petit, E.; Seguin, J.P.; Barboutin, J.N.; Heyraud, A.; Courtois, B.; Courtois, J.
Identification of glucuronan lyase from a mutant strain of Rhizobium meliloti
Int. J. Biol. Macromol.
21
3-9
1997
Sinorhizobium meliloti, Sinorhizobium meliloti M5N1 CS
brenda
Da Costa, A.; Michaud, P.; Petit, E.; Heyraud, A.; Colin-Morel, P.; Courtois, B.; Courtois, J.
Purification and properties of a glucuronan lyase from Sinorhizobium meliloti M5N1CS (NCIMB 40472)
Appl. Environ. Microbiol.
67
5197-5203
2001
Sinorhizobium meliloti, Sinorhizobium meliloti M5N1 CS
brenda
Delattre, C.; Michaud, P.; Keller, C.; Elboutachfaiti, R.; Beven, L.; Courtois, B.; Courtois, J.
Purification and characterization of a novel glucuronan lyase from Trichoderma sp. GL2
Appl. Microbiol. Biotechnol.
70
437-443
2006
Trichoderma sp., Trichoderma sp. GL2
brenda
Delattre, C.; Michaud, P.; Keller, C.; Courtois, B.; Courtois, J.
Production of oligoglucuronans by enzymatic depolymerization of nascent glucuronan
Biotechnol. Prog.
21
1775-1781
2005
Trichoderma sp., Trichoderma sp. GL2
brenda
Delattre, C.; Michaud, P.; Lion, J.M.; Courtois, B.; Courtois, J.
Production of glucuronan oligosaccharides using a new glucuronan lyase activity from a Trichoderma sp. strain
J. Biotechnol.
118
448-457
2005
Trichoderma sp.
brenda
Delattre, C.; Michaud, P.; Elboutachfaiti, R.; Courtois, B.; Courtois, J.
Production of oligocellouronates by biodegradation of oxidized cellulose
Cellulose
13
63-71
2006
Trichoderma sp., Trichoderma sp. GL2
-
brenda
Delattre, C.; Michaud, P.; Courtois, J.; Courtois, B.
Production of O-acetylated oligouronides by depolymerization of a natural highly acetylated anionic bacterial polysaccharide
Enzyme Microb. Technol.
41
250-257
2007
Trichoderma sp., Trichoderma sp. GL2
-
brenda
Konno, N.; Igarashi, K.; Habu, N.; Samejima, M.; Isogai, A.
Cloning of the Trichoderma reesei cDNA encoding a glucuronan lyase belonging to a novel polysaccharide lyase family
Appl. Environ. Microbiol.
75
101-107
2009
Trichoderma reesei (B6F143), Trichoderma reesei
brenda
Tavernier, M.L.; Petit, E.; Delattre, C.; Courtois, B.; Courtois, J.; Strancar, A.; Michaud, P.
Production of oligoglucuronans using a monolithic enzymatic microreactor
Carbohydr. Res.
343
2687-2691
2008
Trichoderma sp.
brenda
Redouan, E.; Cedric, D.; Emmanuel, P.; Mohamed, e.l..G.; Bernard, C.; Philippe, M.; Cherkaoui, e.l..M.; Josiane, C.
Improved isolation of glucuronan from algae and the production of glucuronic acid oligosaccharides using a glucuronan lyase
Carbohydr. Res.
344
1670-1675
2009
Trichoderma sp.
brenda
Tavernier, M.; Michaud, P.; Wadouachi, A.; Petit, E.
Continuous production of oligoglucuronans by immobilized glucuronan lyase
Enzyme Microb. Technol.
45
48-52
2009
Trichoderma sp., Trichoderma sp. GL2
-
brenda
Konno, N.; Ishida, T.; Igarashi, K.; Fushinobu, S.; Habu, N.; Samejima, M.; Isogai, A.
Crystal structure of polysaccharide lyase family 20 endo-beta-1,4-glucuronan lyase from the filamentous fungus Trichoderma reesei
FEBS Lett.
583
1323-1326
2009
Trichoderma reesei (B6F143), Trichoderma reesei
brenda
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