Information on EC 4.2.2.14 - glucuronan lyase

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

EC NUMBER
COMMENTARY hide
4.2.2.14
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RECOMMENDED NAME
GeneOntology No.
glucuronan lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
-
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SYSTEMATIC NAME
IUBMB Comments
(1->4)-beta-D-glucuronan lyase
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CAS REGISTRY NUMBER
COMMENTARY hide
193766-71-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-O-acetylated 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
cellouronate
?
show the reaction diagram
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
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-
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
show the reaction diagram
deacetylated polyglucuronate
4,5-unsaturated oligoglucuronates
show the reaction diagram
glucuronan
4-deoxy-beta-D-hex-4-enopyranosylglucuronate-(1-4)-O-beta-D-glucuropyranosyluronate-(1-4)-O-beta-D-glucuropyranosyluronate + ?
show the reaction diagram
glucuronan
oligoglucuronan
show the reaction diagram
-
-
-
-
?
polyglucuronic acid
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
1 mM, enhances activity 1.5fold
Li+
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1 mM, enhances activity 4.4fold
Mg2+
-
1 mM, enhances activity 2.5fold
Mn2+
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1 mM, enhances activity 2.2fold
additional information
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enzyme appears not to be really affected by ionic strength variations. The optimum is 300 mM concentration of potassium acetate buffer
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
100% reduced activity at 1 mM
Ca2+
-
21-30% reduced activity at 1 mM
Cd2+
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26-29% reduced activity at 1 mM
Fe2+
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1 mM, 19% inhibition
Hg2+
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94% reduced activity at 1 mM
Li+
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26-29% reduced activity at 1 mM
Mn2+
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21-30% reduced activity at 1 mM
NaN3
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26-29% reduced activity at 1 mM
Ni2+
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1 mM, 60% inhibition
Rb2+
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1 mM, 10% inhibition
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Zn2+
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59% reduced activity at 1 mM
additional information
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no inhibition by Mg2+
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
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isoelectric focusing
6.95
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isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
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gel filtration
27000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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 hide
LITERATURE
5 - 9
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stable over a broad when treated at 4C for 24 h
690555
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
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enzyme activity remains after incubation at 10 to 40C for 10 min, but approximately 60% of the activity is lost at 50C
35
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1 h, stable below
40
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1 h, 90% loss of activity
52
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50% of maximal activity
60
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1 h, complete inactivation
67
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complete inactivation
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
-80C, 50 mM KCl, purified enzyme, stable for several weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration and anion-exchange chromatography
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phenyl-Toyopearl column chromatography and SuperQ-Toyopearl column chromatography
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to homogeneity, 394fold
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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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