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Information on EC 3.2.1.162 - lambda-carrageenase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.2.1.162
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RECOMMENDED NAME
GeneOntology No.
lambda-carrageenase
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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
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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
proceeds according to an endolytic mode of action and a mechanism of inversion of the anomeric configuration
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
proceeds according to an endolytic mode of action and a mechanism of inversion of the anomeric configuration
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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CAS REGISTRY NUMBER
COMMENTARY
5093637-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a thermophilic strain isolated from a hot spring in Indonesia
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Bacillus sp. (in: Bacteria) Lc50-1
a thermophilic strain isolated from a hot spring in Indonesia
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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
lambda-carrageenan + H2O
alpha-D-Galp2,6S2-(1-3)-beta-D-Galp2S-(1-4)-alpha-D-Galp2,6S2-(1-3)-D-Galp2S + ?
lambda-carrageenan + H2O
neo-carrabiose oligosaccharides
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?
delta-carrageenan + H2O
neo-delta-carrabiose + ?
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Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
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?
delta-carrageenan + H2O
neo-delta-carrabiose + ?
Bacillus sp. (in: Bacteria) Lc50-1
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Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
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?
lambda-carrageenan + H2O
alpha-D-Galp2,6S2-(1-3)-beta-D-Galp2S-(1-4)-alpha-D-Galp2,6S2-(1-3)-D-Galp2S + ?
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?
lambda-carrageenan + H2O
alpha-D-Galp2,6S2-(1-3)-beta-D-Galp2S-(1-4)-alpha-D-Galp2,6S2-(1-3)-D-Galp2S + ?
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?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
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main reaction products, after prolonged incubation (22-50 h) increasing ratio of neo-lambda-carratetraose suggesting also the rise of a dimeric product arising from the cleavage of the hexamer
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?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
CglA hydrolase proceeds according to an endolytic mode of action and a mechanism of inversion of the anomeric configuration
neo-lambda-carratetraose is the main degradation product
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?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
sole known depolymerizing enzyme of lambda-carrageenan, hydrolyses the beta(1-4) linkage of lambda-carrageenan
main reaction products
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?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
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main reaction products, after prolonged incubation (22-50 h) increasing ratio of neo-lambda-carratetraose suggesting also the rise of a dimeric product arising from the cleavage of the hexamer
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?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
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sole known depolymerizing enzyme of lambda-carrageenan, hydrolyses the beta(1-4) linkage of lambda-carrageenan
main reaction products
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?
neo-lambda-carrahexaose + H2O
neo-lambda-carratetraose + neo-lambda-carrabiose
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?
neo-lambda-carrahexaose + H2O
neo-lambda-carratetraose + neo-lambda-carrabiose
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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
delta-carrageenan + H2O
neo-delta-carrabiose + ?
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Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
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?
delta-carrageenan + H2O
neo-delta-carrabiose + ?
Bacillus sp. (in: Bacteria) Lc50-1
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Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
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?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
Q0JRK4
sole known depolymerizing enzyme of lambda-carrageenan, hydrolyses the beta(1-4) linkage of lambda-carrageenan
main reaction products
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?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
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sole known depolymerizing enzyme of lambda-carrageenan, hydrolyses the beta(1-4) linkage of lambda-carrageenan
main reaction products
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CsCl
maximal activity in presence of 0.4 M NaCl. CsCl is able to compensate for KCl
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
RbCl
maximal activity in presence of 0.4 M NaCl. RbCl is able to compensate for KCl
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
pH 6.0: about 40% of maximal activity, pH 8.5: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
20°C: about 40% of maximal activity, 40°C: about 65% of maximal activity
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
pre-protein, calculated from the deduced amino acid sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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
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
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
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LINKS TO OTHER DATABASES (specific for EC-Number 3.2.1.162)
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