Information on EC 4.2.2.14 - glucuronan lyase

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

EC NUMBER
COMMENTARY
4.2.2.14
-
RECOMMENDED NAME
GeneOntology No.
glucuronan lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.
show the reaction diagram
complete degradation of glucuronans results in the formation of tetrasaccharides
-
Eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.
show the reaction diagram
-
-
-
-
Eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.
show the reaction diagram
complete degradation of glucuronans results in the formation of tetrasaccharides
Sinorhizobium meliloti M5N1CS
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
elimination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(1->4)-beta-D-glucuronan lyase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(1,4)-beta-D-glucuronan lyase
-
-
-
-
(1,4)-beta-D-glucuronan lyase
-
-
(1,4)-beta-D-glucuronan lyase
Sinorhizobium meliloti M5N1CS
-
-
-
(1,4)-beta-D-glucuronan lyase
Trichoderma sp.
-
-
(1,4)-beta-D-glucuronan lyase
Trichoderma sp. GL2
-
-
-
(1->4)-beta-D-glucuronan lyase
-
-
-
-
endo-beta-(1->4)-glucuronan lyase
B6F143
-
endo-beta-1,4-glucuronan lyase
B6F143
-
endopolyglucuronate lyase
-
-
endopolyglucuronate lyase
Sinorhizobium meliloti M5N1CS
-
-
-
GL2 glucuronan lyase
Trichoderma sp.
-
-
glucuronan lyase
B6F143
-
glucuronan lyase
Trichoderma sp.
-
-
TrGL
B6F143
-
CAS REGISTRY NUMBER
COMMENTARY
193766-71-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
M5N1CS (NCIMB 40472) mutant strain
-
-
Manually annotated by BRENDA team
strain M5N1CS, NCIMB 40472
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti M5N1CS
M5N1CS (NCIMB 40472) mutant strain
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti M5N1CS
strain M5N1CS, NCIMB 40472
-
-
Manually annotated by BRENDA team
Trichoderma sp.
-
-
-
Manually annotated by BRENDA team
Trichoderma sp.
GL2
-
-
Manually annotated by BRENDA team
Trichoderma sp.
strain GL2
-
-
Manually annotated by BRENDA team
Trichoderma sp. GL2
-
-
-
Manually annotated by BRENDA team
Trichoderma sp. GL2
GL2
-
-
Manually annotated by BRENDA team
Trichoderma sp. GL2
strain GL2
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-O-acetylated glucuronan
?
show the reaction diagram
Sinorhizobium meliloti, Sinorhizobium meliloti M5N1CS
-
beta(1-4)-linked
-
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
show the reaction diagram
-
-
-
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
show the reaction diagram
Trichoderma sp., Trichoderma sp. GL2
-
-
-
-
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
show the reaction diagram
Sinorhizobium meliloti M5N1CS
-
-
-
?
cellouronate
?
show the reaction diagram
B6F143, -
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
show the reaction diagram
-
-
-
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
show the reaction diagram
Trichoderma sp., Trichoderma sp. GL2
-
-
-
-
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
show the reaction diagram
Sinorhizobium meliloti M5N1CS
-
-
-
?
deacetylated polyglucuronate
4,5-unsaturated oligoglucuronates
show the reaction diagram
Sinorhizobium meliloti, Sinorhizobium meliloti M5N1CS
-
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 + ?
show the reaction diagram
Trichoderma sp., Trichoderma sp. GL2
-
-
-
-
?
polyglucuronic acid
?
show the reaction diagram
Trichoderma sp., Trichoderma sp. GL2
-
-
-
-
?
glucuronan
oligoglucuronan
show the reaction diagram
Trichoderma sp.
-
-
-
-
?
additional information
?
-
Sinorhizobium meliloti, Sinorhizobium meliloti M5N1CS
-
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
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
show the reaction diagram
Sinorhizobium meliloti, Sinorhizobium meliloti M5N1CS
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
Trichoderma sp.
-
1 mM, enhances activity 4.56fold
Ca2+
-
activity and thermostability increases in the presence of Ca2+
Ca2+
-
a calcium ion contributes to the enzyme stability
Co2+
Trichoderma sp.
-
1 mM, enhances activity 1.5fold
Li+
Trichoderma sp.
-
1 mM, enhances activity 4.4fold
Mg2+
Trichoderma sp.
-
1 mM, enhances activity 2.5fold
Mn2+
Trichoderma sp.
-
1 mM, enhances activity 2.2fold
additional information
Trichoderma sp.
-
enzyme appears not to be really affected by ionic strength variations. The optimum is 300 mM concentration of potassium acetate buffer
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ag+
-
100% reduced activity at 1 mM
Ca2+
-
21-30% reduced activity at 1 mM
Cd2+
-
26-29% reduced activity at 1 mM
Cu2+
-
85% reduced activity at 1 mM
Cu2+
Trichoderma sp.
-
1 mM, 81% inhibition
EDTA
-
21-30% reduced activity at 1 mM
Fe2+
Trichoderma sp.
-
1 mM, 19% inhibition
-
Hg2+
-
94% reduced activity at 1 mM
Li+
-
26-29% reduced activity at 1 mM
NaN3
-
26-29% reduced activity at 1 mM
Ni2+
Trichoderma sp.
-
1 mM, 60% inhibition
Rb2+
Trichoderma sp.
-
1 mM, 10% inhibition
-
Zn2+
-
59% reduced activity at 1 mM
Mn2+
-
21-30% reduced activity at 1 mM
additional information
-
no inhibition by Mg2+
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
162
-
Trichoderma sp.
-
-
additional information
-
Trichoderma sp.
-
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
Trichoderma sp.
-
-
5.5
-
Trichoderma sp.
-
assay at
6.5
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
assay at
55
-
Trichoderma sp.
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
-
isoelectric focusing
6.95
-
Trichoderma sp.
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Trichoderma sp.
-
-
-
Manually annotated by BRENDA team
Trichoderma sp. GL2
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20000
-
-
gel filtration
27000
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Trichoderma sp.
-
x * 27000, SDS-PAGE
?
Trichoderma sp. GL2
-
x * 27000, SDS-PAGE
-
monomer
-
1 * 20000, SDS-PAGE
monomer
Sinorhizobium meliloti M5N1CS
-
1 * 20000, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method, using 20% (w/v) PEG3350 and 0.2 M ammonium citrate buffer (pH 5.0)
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
8
Trichoderma sp.
-
30 min, stable
4
8
Trichoderma sp.
-
-
5
9
-
stable over a broad when treated at 4C for 24 h
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
40
-
enzyme activity remains after incubation at 10 to 40C for 10 min, but approximately 60% of the activity is lost at 50C
35
-
Trichoderma sp.
-
1 h, stable below
40
-
Trichoderma sp.
-
1 h, 90% loss of activity
52
-
-
50% of maximal activity
60
-
Trichoderma sp.
-
1 h, complete inactivation
67
-
-
complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
Trichoderma sp.
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, 50 mM KCl, purified enzyme, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
phenyl-Toyopearl column chromatography and SuperQ-Toyopearl column chromatography
-
to homogeneity, 394fold
-
-
Trichoderma sp.
-
gel filtration and anion-exchange chromatography
Trichoderma sp.
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Pichia pastoris
B6F143
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
Trichoderma sp.
-
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
Trichoderma sp.
-
production of oligoglucuronans by enzymatic depolymerization of nascent glucuronan
synthesis
Trichoderma sp.
-
production of glucuronan oligosaccharides
synthesis
Trichoderma sp.
-
large-scale production of oligocellouronic acids
synthesis
Trichoderma sp.
-
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
Trichoderma sp. GL2
-
large-scale production of oligocellouronic acids; 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; production of oligoglucuronans by enzymatic depolymerization of nascent glucuronan
-