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Information on EC 4.2.2.14 - glucuronan lyase
for references in articles please use BRENDA:EC4.2.2.14
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 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
Reaction Schemes
showSynonyms
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
glucuronan specific lyase
PL20A
PL20B
PL38A
(1,4)-beta-D-glucuronan lyase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
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.
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.
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.
-
-
-
-
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.
complete degradation of glucuronans results in the formation of tetrasaccharides
-
-
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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
LITERATURE
COMMENTARY
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
?
Substrates: 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
Products: -
Products: -
?
cellouronate
oligomers and dimers
-
Substrates: the enzyme shows high substrate specificity for cellouronate, i.e. (1,4)-beta-polyglucuronate
Products: -
Products: -
?
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 + ?
[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
-
Substrates: -
Products: -
Products: -
?
3-O-acetylated glucuronan
?
-
Substrates: beta(1-4)-linked
Products: -
Products: -
?
3-O-acetylated glucuronan
?
-
Substrates: beta(1-4)-linked
Products: -
Products: -
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
Substrates: -
Products: -
Products: -
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
Substrates: -
Products: -
Products: -
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
Substrates: -
Products: -
Products: -
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
Substrates: -
Products: -
Products: -
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
Substrates: -
Products: -
Products: -
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
Substrates: -
Products: -
Products: -
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
Substrates: -
Products: -
Products: -
?
deacetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
Substrates: -
Products: -
Products: -
?
deacetylated polyglucuronate
4,5-unsaturated oligoglucuronates
-
Substrates: beta-(1-4)-linked, best substrate, enzyme shows specific endopolyglucuronate lyase activity
Products: -
Products: -
?
deacetylated polyglucuronate
4,5-unsaturated oligoglucuronates
-
Substrates: beta-(1-4)-linked, best substrate, enzyme shows specific endopolyglucuronate lyase activity
Products: -
Products: -
?
glucuronan
4-deoxy-beta-D-hex-4-enopyranosylglucuronate-(1-4)-O-beta-D-glucuropyranosyluronate-(1-4)-O-beta-D-glucuropyranosyluronate + ?
-
Substrates: -
Products: -
Products: -
?
glucuronan
4-deoxy-beta-D-hex-4-enopyranosylglucuronate-(1-4)-O-beta-D-glucuropyranosyluronate-(1-4)-O-beta-D-glucuropyranosyluronate + ?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme's mode of action is endo-type
Products: -
Products: -
-
additional information
?
-
-
Substrates: no activity with amylouronate, curdluronate, alginate, pectate, carboxymethyl cellulose, xylan, and barley glucan
Products: -
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: isoform PL38A shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
-
Substrates: isoform PL38A shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
Substrates: isoform PL20A shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
-
Substrates: isoform PL20A shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
Substrates: isoform PL20B shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
-
Substrates: isoform PL20B shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
Trichoderma parareesei CBS125925
Substrates: isoform PL20A shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
Trichoderma parareesei CBS125925
-
Substrates: isoform PL20A shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
Trichoderma parareesei CBS125925
Substrates: isoform PL38A shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
Trichoderma parareesei CBS125925
-
Substrates: isoform PL38A shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
Trichoderma parareesei CBS125925
Substrates: isoform PL20B shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
additional information
?
-
Trichoderma parareesei CBS125925
-
Substrates: isoform PL20B shows no activity on alginate, chondroitin or hyaluronan
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
[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
-
Substrates: -
Products: -
Products: -
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
Substrates: -
Products: -
Products: -
?
acetylated (1->4)-beta-D-glucuronan
4-deoxy-beta-D-gluc-4-enuronosyl (1->4)-beta-D-glucuronan
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
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
Mg2+
isoform PL20A shows complete inhibition at 2 mM; isoform PL20B shows complete inhibition at 2 mM
Mn2+
isoform PL20A shows complete inhibition at 2 mM; isoform PL20B shows complete inhibition at 2 mM; isoform PL38A shows 94% residual activity at 2 mM Mn2+
Ni2+
isoform PL20A shows complete inhibition at 2 mM; isoform PL20B shows complete inhibition at 2 mM; isoform PL38A shows 70% residual activity at 2 mM Ni2+
Zn2+
isoform PL20A shows complete inhibition at 2 mM; isoform PL20B shows complete inhibition at 2 mM; isoform PL38A shows 51% residual activity at 2 mM Zn2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
deacetylated glucuronan
-
wild-type, Km value 0.096 g/l, pH 5.5, 25°C
-
additional information
deacetylated glucuronan
-
fusion construct without linker, Km value 0.092 g/l, pH 5.5, 25°C
-
additional information
deacetylated glucuronan
-
fusion construct with linker 1, Km value 0.076 g/l,pH 5.5, 25°C
-
additional information
deacetylated glucuronan
-
fusion construct with linker 2, Km value 0.088 g/l, pH 5.5, 25°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0074
deacetylated glucuronan
-
fusion construct with linker 1, pH 5.5, 25°C
-
0.00822
deacetylated glucuronan
-
fusion construct with linker 2, pH 5.5, 25°C
-
0.00838
deacetylated glucuronan
-
fusion construct without linker, pH 5.5, 25°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
deacetylated glucuronan
-
wild-type, kcat/Km value 3105 g/L/min, pH 5.5, 25°C
-
additional information
deacetylated glucuronan
-
fusion construct without linker, kcat/Km value 5423 g/L/min, pH 5.5, 25°C
-
additional information
deacetylated glucuronan
-
fusion construct with linker 1, kcat/Km value 5847 g/L/min, pH 5.5, 25°C
-
additional information
deacetylated glucuronan
-
fusion construct with linker 2, kcat/Km value 5570 g/L/min, pH 5.5, 25°C
-
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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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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
isoform PL20B has more than 40% increased activity between 25 and 50°C
40 - 50
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Trichoderma parareesei CBS125925
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
?
-
x * 30000, wild-type, x * 75000, SDS-PAGE of glucuronan lyase-chitinase fusion protein, SDS-PAGE
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
construction of chimeric proteins by the fusion of glucuronan lyase (EC 4.2.2.14) and chitinase without or with linker. The chimeric enzymes display a decreased stability to temperature and pH variations, compared to parental ones. The specific actvities of chitinase are similar or slightly decreased compared to wild-type, while the specific activities of glucuronan lyase increase by 28-91%
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
5 - 8
-
the wild type and chimeric enzymes are stable for pH ranging from 5.0 to 8.0
7 - 9
-
the enzyme is relatively stable at pH 6.0-9.0, but loses 60% or less of its activity at pH values lower than 5.0. The enzyme remains stable in Tris-HCl pH 7.0-9.0 for 24 h
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 30
-
the enzyme retains approximately 70% of its activity after incubation for 10 min at 10-30°C
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
50
-
the wild type enzyme maintains about 35% activity after 30 min at 50°C, while chimeric enzymes are inactive under the same conditions
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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
-
bifunctional enzymes created by the fusion of a glucuronan lyase and a chitinase from Trichoderma sp. induce a slight decrease of the thermostability of glucuronan lyase, without modifying its catalytic activity regarding pH variations ranging from 5.0 to 8.0. The chimeric enzymes display a decreased stability to temperature and pH variations, compared to parental one
-
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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
Pilgaard, B.; Vuillemin, M.; Munk, L.; Holck, J.; Meier, S.; Wilkens, C.; Meyer, A.S.
Discovery of a novel glucuronan lyase system in Trichoderma parareesei
Appl. Environ. Microbiol.
88
e0181921
2022
Trichoderma parareesei (A0A2H2ZIP6), Trichoderma parareesei, Trichoderma parareesei CBS125925 (A0A2H2ZIP6), Trichoderma parareesei CBS125925
brenda
Baklouti, Z.; Delattre, C.; Pierre, G.; Gardarin, C.; Abdelkafi, S.; Michaud, P.; Dubessay, P.
Biochemical characterization of a bifunctional enzyme constructed by the fusion of a glucuronan lyase and a chitinase from Trichoderma sp.
Life (Basel)
10
234
2020
Trichoderma harzianum
brenda
Baklouti, Z.; Delattre, C.; Pierre, G.; Gardarin, C.; Abdelkafi, S.; Michaud, P.; Dubessay, P.
Biochemical characterization of a bifunctional enzyme constructed by the fusion of a glucuronan lyase and a chitinase from Trichoderma sp.
Life
10
234
2020
Trichoderma sp.
brenda
Kikuchi, M.; Konno, N.; Suzuki, T.; Fujii, Y.; Kodama, Y.; Isogai, A.; Habu, N.
A bacterial endo-beta-1,4-glucuronan lyase, CUL-I from Brevundimonas sp. SH203, belonging to a novel polysaccharide lyase family
Protein Expr. Purif.
166
105502
2020
Brevundimonas sp. SH203
brenda
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