Information on EC 3.2.1.162 - lambda-carrageenase

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The expected taxonomic range for this enzyme is: Pseudoalteromonas

EC NUMBER
COMMENTARY
3.2.1.162
-
RECOMMENDED NAME
GeneOntology No.
lambda-carrageenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-, Q0JRK4
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
-
-
PATHWAY
KEGG Link
MetaCyc Link
lambda-carrageenan degradation
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CglA
Pseudoalteromonas carrageenovora ATCC43555
-
-
-
CglA hydrolase
Q0JRK4
-
endo-beta-1,4-carrageenose 2,6,2'-trisulfate-hydrolase
Q05JY7
-
endo-beta-1,4-carrageenose 2,6,2'-trisulfate-hydrolase
Q05JY7
-
-
CAS REGISTRY NUMBER
COMMENTARY
5093637-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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 + ?
show the reaction diagram
Q05JY7
-
-
-
?
lambda-carrageenan + H2O
neo-carrabiose oligosaccharides
show the reaction diagram
-
-
-
-
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
-, Q0JRK4
-
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
-, Q0JRK4
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
-, 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
-
-
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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 ACCESSION NO.
COMMENTARY
LITERATURE
CsCl
Q05JY7
maximal activity in presence of 0.4 M NaCl. CsCl is able to compensate for KCl
KCl
Q05JY7
maximal activity in presence of 0.4 M NaCl. KCl is able to compensate for KCl
LiCl
Q05JY7
maximal activity in presence of 0.4 M NaCl. LiCl is able to compensate for KCl
NaCl
Q05JY7
maximal activity in presence of 0.4 M NaCl
RbCl
Q05JY7
maximal activity in presence of 0.4 M NaCl. RbCl is able to compensate for KCl
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
Pseudomonas carrageenovora
-
0.0001 mM
Hg2+
Pseudomonas carrageenovora
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8.5
Q05JY7
pH 6.0: about 40% of maximal activity, pH 8.5: about 45% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
40
Q05JY7
20°C: about 40% of maximal activity, 40°C: about 65% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q05JY7
containing lambda-carrageenan as a carbon source
Manually annotated by BRENDA team
-
containing lambda-carrageenan as a carbon source
-
Manually annotated by BRENDA team
Pseudomonas carrageenovora
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
78000
-
-, Q0JRK4
gel filtration
97000
-
-, Q0JRK4
SDS-PAGE
100000
-
Q05JY7
gel filtration
105000
-
-, Q0JRK4
pre-protein, calculated from the deduced amino acid sequence
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-, Q0JRK4
1 * 97000, SDS-PAGE
monomer
Q05JY7
1 * 100000, SDS-PAGE
monomer
-
1 * 100000, SDS-PAGE
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
Q05JY7
120 min, stable
30
-
Q05JY7
0.5 M sorbitol, 120 min, enzyme is stable up to
35
-
Pseudomonas carrageenovora
-
30 min, inactivated
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sorbitol, sucrose and trehalose improve stability
Q05JY7
inactivated by freezing, by dialysis against distilled water
Pseudomonas carrageenovora
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; from host strain
-, Q0JRK4
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-, Q0JRK4
expression in Escherichia coli
Q05JY7