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
3.2.1.162
-
RECOMMENDED NAME
GeneOntology No.
lambda-carrageenase
-
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
show the reaction diagram
-
-
-
-
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
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
show the reaction diagram
proceeds according to an endolytic mode of action and a mechanism of inversion of the anomeric configuration
Pseudoalteromonas carrageenovora ATCC43555
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-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
lambda-carrageenan degradation
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-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cga-L50
-
-
Cga-L50
Bacillus sp. Lc50-1
-
-
-
CglA
Pseudoalteromonas carrageenovora ATCC43555
-
-
-
delta-carrageenase
-
-
delta-carrageenase
Bacillus sp. Lc50-1
-
-
-
delta-carrageenase
-
-
endo-beta-1,4-carrageenose 2,6,2'-trisulfate-hydrolase
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endo-beta-1,4-carrageenose 2,6,2'-trisulfate-hydrolase
-
-
endo-type delta-carrageenase
-
-
endo-type delta-carrageenase
Bacillus sp. Lc50-1
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
5093637-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a thermophilic strain isolated from a hot spring in Indonesia
-
-
Manually annotated by BRENDA team
Bacillus sp. Lc50-1
a thermophilic strain isolated from a hot spring in Indonesia
-
-
Manually annotated by BRENDA team
Pseudoalteromonas carrageenovora ATCC43555
ATCC43555
-
-
Manually annotated by BRENDA team
strain CL19
SwissProt
Manually annotated by BRENDA team
strain CL19
SwissProt
Manually annotated by BRENDA team
Pseudomonas carrageenovora
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
delta-carrageenan + H2O
neo-delta-carrabiose + ?
show the reaction diagram
Bacillus sp., Bacillus sp. 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
-
?
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
-
-
-
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
-
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
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
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
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
sole known depolymerizing enzyme of lambda-carrageenan, hydrolyses the beta(1-4) linkage of lambda-carrageenan
main reaction products
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
Pseudoalteromonas carrageenovora ATCC43555
-
-
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
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
Pseudoalteromonas carrageenovora ATCC43555
-
sole known depolymerizing enzyme of lambda-carrageenan, hydrolyses the beta(1-4) linkage of lambda-carrageenan
main reaction products
?
neo-lambda-carrahexaose + H2O
neo-lambda-carratetraose + neo-lambda-carrabiose
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
delta-carrageenan + H2O
neo-delta-carrabiose + ?
show the reaction diagram
Bacillus sp., Bacillus sp. Lc50-1
-
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
-
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
Q0JRK4
sole known depolymerizing enzyme of lambda-carrageenan, hydrolyses the beta(1-4) linkage of lambda-carrageenan
main reaction products
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
Pseudoalteromonas carrageenovora ATCC43555
-
sole known depolymerizing enzyme of lambda-carrageenan, hydrolyses the beta(1-4) linkage of lambda-carrageenan
main reaction products
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
Cd2+
-
-
Cu2+
-
-
EDTA
Pseudomonas carrageenovora
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0.0001 mM
EDTA
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-
Fe2+
-
-
Hg2+
Pseudomonas carrageenovora
-
-
Mg2+
-
-
Mn2+
-
-
Sr2+
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105.9
-
purified native enzyme, pH 7.5, 75C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
20C: about 40% of maximal activity, 40C: about 65% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
containing lambda-carrageenan as a carbon source
Manually annotated by BRENDA team
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containing lambda-carrageenan as a carbon source
-
Manually annotated by BRENDA team
Pseudomonas carrageenovora
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-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Bacillus sp. Lc50-1
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
78000
gel filtration
667539
100000
gel filtration
669161
105000
pre-protein, calculated from the deduced amino acid sequence
667539
109000
-
gel filtration
732212
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 37000, SDS-PAGE
?
-
x * 109000, His-tagged enzyme, SDS-PAGE
?
Bacillus sp. Lc50-1
-
x * 37000, SDS-PAGE
-
monomer
1 * 97000, SDS-PAGE
monomer
1 * 100000, SDS-PAGE
monomer
-
1 * 100000, SDS-PAGE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
purified native enzyme, stable at
731525
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
120 min, stable
669161
30
0.5 M sorbitol, 120 min, enzyme is stable up to
669161
35
Pseudomonas carrageenovora
-
30 min, inactivated
668129
85
-
purified native enzyme, 10 min, over 50% activity remaining
731525
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sorbitol, sucrose and trehalose improve stability
inactivated by freezing, by dialysis against distilled water
Pseudomonas carrageenovora
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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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expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
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