Information on EC 3.2.1.162 - lambda-carrageenase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
3.2.1.162
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RECOMMENDED NAME
GeneOntology No.
lambda-carrageenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-beta-linkages in the backbone of lambda-carrageenan, resulting in the tetrasaccharide alpha-D-Gal-p2,6S2-(1->3)-beta-D-Gal-p2S-(1->4)-alpha-D-Gal-p2,6S2-(1->3)-D-Gal-p2-S
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
lambda-carrageenan degradation
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CAS REGISTRY NUMBER
COMMENTARY hide
5093637-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a thermophilic strain isolated from a hot spring in Indonesia
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-
Manually annotated by BRENDA team
Bacillus sp. Lc50-1
a thermophilic strain isolated from a hot spring in Indonesia
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-
Manually annotated by BRENDA team
ATCC43555
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-
Manually annotated by BRENDA team
strain CL19
SwissProt
Manually annotated by BRENDA team
strain CL19
SwissProt
Manually annotated by BRENDA team
Pseudomonas carrageenovora
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-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
delta-carrageenan + H2O
neo-delta-carrabiose + ?
show the reaction diagram
lambda-carrageenan + H2O
alpha-D-Galp2,6S2-(1-3)-beta-D-Galp2S-(1-4)-alpha-D-Galp2,6S2-(1-3)-D-Galp2S + ?
show the reaction diagram
lambda-carrageenan + H2O
neo-carrabiose oligosaccharides
show the reaction diagram
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-
-
-
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
neo-lambda-carrahexaose + H2O
neo-lambda-carratetraose + neo-lambda-carrabiose
show the reaction diagram
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-
-
-
?
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
delta-carrageenan + H2O
neo-delta-carrabiose + ?
show the reaction diagram
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates
Co2+
-
activates
CsCl
maximal activity in presence of 0.4 M NaCl. CsCl is able to compensate for KCl
K+
-
activates
KCl
maximal activity in presence of 0.4 M NaCl. KCl is able to compensate for KCl
LiCl
maximal activity in presence of 0.4 M NaCl. LiCl is able to compensate for KCl
Na+
-
activates
NaCl
maximal activity in presence of 0.4 M NaCl
RbCl
maximal activity in presence of 0.4 M NaCl. RbCl is able to compensate for KCl
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cd2+
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-
Cu2+
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Fe2+
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Hg2+
Pseudomonas carrageenovora
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-
Mg2+
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Mn2+
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-
Sr2+
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105.9
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purified native enzyme, pH 7.5, 75°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
pH 6.0: about 40% of maximal activity, pH 8.5: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
20°C: about 40% of maximal activity, 40°C: about 65% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
gel filtration
105000
pre-protein, calculated from the deduced amino acid sequence
109000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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purified native enzyme, stable at
731525
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
120 min, stable
30
0.5 M sorbitol, 120 min, enzyme is stable up to
35
Pseudomonas carrageenovora
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30 min, inactivated
85
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purified native enzyme, 10 min, over 50% activity remaining
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated by freezing, by dialysis against distilled water
Pseudomonas carrageenovora
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sorbitol, sucrose and trehalose improve stability
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 37.8fold from culture supernatant, by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant chimeric protein cCgkA and cCglA containing the catalytic domain of kappa-carrageenase CgkA and delta-carrageenase CglA fused with a dockerin domain from Escherichia coli strain BL21(DE3) by cellulose affinity chromatography using carbohydrate binding module in scaffoldin miniCbpA as a tag
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli, formation of inclusion bodies that are solved in 8 M urea; expression in Escherichia coli as insoluble inclusion bodies. These inclusion bodies are purified and solubilized in 8 M urea
expression in Escherichia coli
subcloning in Escherichia coli strain DH5alpha, recombinant expression of a chimeric protein cCgkA and cCglA containing the catalytic domain of kappa-carrageenase CgkA and delta-carrageenase CglA fused with a dockerin domain in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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generation of a chimeric protein cCgkA and cCglA containing the catalytic domain of kappa-carrageenase CgkA and delta-carrageenase CglA fused with a dockerin domain, miniCbpA, cCgkA and cCglA assemble into a complex, the dockerin-fused enzymes on the scaffoldin have synergistic activity in the degradationof carrageenan showing enhancement of activity by carrageenolytic complex 3.1fold higher compared with the corresponding enzymes alone
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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the assemblies of advancement of active enzyme complexes, i.e. of kappa-carrageenase CgkA and delta-carrageenase CglA, will facilitate the commercial production of useful products from red algae biomass whichrepresents inexpensive and sustainable feed-stocks