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Enzyme Nomenclature
Information on EC 3.2.1.157 - iota-carrageenase
for references in articles please use BRENDA:EC3.2.1.157
Word Map on EC 3.2.1.157
- 3.2.1.157
- alteromonas
- fortis
-
iota-carrageenans
-
zobellia
- oligosaccharide
- polysaccharide
-
right-handed
- kappa-carrageenases
-
kappa
- eucheuma
-
double-stranded
-
beta-helix
-
kappa-carrageenan
- cellulophaga
- galactanivorans
- lambda-carrageenan
-
polysaccharidases
- disaccharide
- analysis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.2.1.157
-
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RECOMMENDED NAME
GeneOntology No.
iota-carrageenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in iota-carrageenans
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
iota-carrageenan 4-beta-D-glycanohydrolase (configuration-inverting)
The main products of hydrolysis are iota-neocarratetraose sulfate and iota-neocarrahexaose sulfate. iota-Neocarraoctaose is the shortest substrate oligomer that can be cleaved. Unlike EC 3.2.1.81, beta-agarase and EC 3.2.1.83, kappa-carrageenase, this enzyme proceeds with inversion of the anomeric configuration. iota-Carrageenan differs from kappa-carrageenan by possessing a sulfo group on O-2 of the 3,6-anhydro-D-galactose residues, in addition to that present in the kappa-compound on O-4 of the D-galactose residues.
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CAS REGISTRY NUMBER
COMMENTARY
74191-25-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Alteromonas fortis
gene cgiB_Ce; isolated from the red alga Grateloupia livida collected from Qingdao coastal waters of China Yellow Sea, gene cgiB_Ce
UniProt
gene cgiB_Ce; isolated from the red alga Grateloupia livida collected from Qingdao coastal waters of China Yellow Sea, gene cgiB_Ce
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
evolution
the enzyme belongs to glycohydrolase family 82, GH82, forming a deeply branched cluster in the phylogenetic tree, along with Celly_2571 and CgiA3, distinct from other iota-carrageenases; the enzyme belongs to the glycosyl hydrolase family 82, GH82
evolution
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the enzyme belongs to glycohydrolase family 82, GH82, forming a deeply branched cluster in the phylogenetic tree, along with Celly_2571 and CgiA3, distinct from other iota-carrageenases; the enzyme belongs to the glycosyl hydrolase family 82, GH82
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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
iota-/nu-carrageenan + H2O
hydrolyzed iota/nu-carrageenan
Alteromonas fortis
-
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the smallest hybrid is an octasaccharide with a iota-iota-nu-iota structure, the second fraction is composed of two decasaccharides with iota-iota-iota-nu-iota and iota-[iota/nu]iota-iota structures, the third fraction is a mixture of dodecasaccharides which contains at least a iota-iota-iota-iota-nu-iota oligosaccharide
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?
iota-carrageenan + H2O
neo-iota-carratetraose + neo-iota-carrahexaose
Alteromonas fortis
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-
most abundant products
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?
iota-carrageenan + H2O
hydrolyzed iota-carrageenan
Alteromonas fortis
from an open conformation which allows the initial endo-attack of iota-carrageenan chains, the enzyme switches to a closed-tunnel form, consistent with its highly processive character
-
-
?
iota-carrageenan + H2O
hydrolyzed iota-carrageenan
Alteromonas fortis
-
hybrid kappa/iota-carrageeans extracted from Gigartina skottsbergii, Chondracanthus chamissoi, and Chondrus crispus are incubated with Pseudoalteromonas carrageenovora kappa-carrageenase and Alteromonas fortis iota-carrageenase. A low percentage of degradation is observed after treatment by iota-carrageenase, suggesting that long segments of iota-carrabiose or block of iota-carrageenan are low in abundance
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-
?
iota-carrageenan + H2O
iota-neocarratetraose sulfate + iota-neocarrahexaose sulfate
Alteromonas fortis
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-
-
-
?
iota-carrageenan + H2O
iota-neocarratetraose sulfate + iota-neocarrahexaose sulfate
the enzyme cleaves beta-1,4 linkages in iota-carrageenan to produce a high ratio of iota-carrageenan tetramer, more than 75% of the total product
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-
?
iota-carrageenan + H2O
iota-neocarratetraose sulfate + iota-neocarrahexaose sulfate
the enzyme cleaves beta-1,4 linkages in iota-carrageenan to produce a high ratio of iota-carrageenan tetramer, more than 75% of the total product
-
-
?
iota-carrageenan + H2O
iota-neocarratetraose sulfate + iota-neocarrahexaose sulfate
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endohydrolytic cleavage, the enzyme proceeds with an overall inversion of the anomeric configuration
major end products
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?
iota-carrageenan + H2O
neo-iota-carratetraose
yielding neo-iota-carratetraose as the main product in the absence of NaCl
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-
?
iota-carrageenan + H2O
neo-iota-carratetraose
the endo-type iota-carrageenase hydrolyzes beta-1,4-linkages of iota-carrageenan
neo-carratetraose is the main product with more than 80% of the total product
-
?
iota-carrageenan + H2O
neo-iota-carratetraose
the endo-type iota-carrageenase hydrolyzes beta-1,4-linkages of iota-carrageenan yielding neo-iota-carratetraose as the main product in the absence of NaCl, mass and NMR spectrometric product analysis, overview
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-
?
iota-carrageenan + H2O
neo-iota-carratetraose
yielding neo-iota-carratetraose as the main product in the absence of NaCl
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-
?
iota-carrageenan + H2O
neo-iota-carratetraose
the endo-type iota-carrageenase hydrolyzes beta-1,4-linkages of iota-carrageenan
neo-carratetraose is the main product with more than 80% of the total product
-
?
iota-carrageenan + H2O
neo-iota-carratetraose
the endo-type iota-carrageenase hydrolyzes beta-1,4-linkages of iota-carrageenan yielding neo-iota-carratetraose as the main product in the absence of NaCl, mass and NMR spectrometric product analysis, overview
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-
?
additional information
?
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no activity towards jota-carrageenan, kappa-carrageenan or agarose
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additional information
?
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no activity towards jota-carrageenan, kappa-carrageenan or agarose
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additional information
?
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the enzyme does not cleave the beta-1,4 linkages in kappa- or lambda-carrageenan
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-
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additional information
?
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the enzyme does not cleave the beta-1,4 linkages in kappa- or lambda-carrageenan
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additional information
?
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the enzyme does not cleave the beta-1,4 linkages in kappa- or lambda-carrageenan
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additional information
?
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the enzyme shows no activity with kappa-carrageenan, lambda-carrageenan, agar or agarose
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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
iota-carrageenan + H2O
neo-iota-carratetraose
R9UQG9
yielding neo-iota-carratetraose as the main product in the absence of NaCl
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-
?
iota-carrageenan + H2O
neo-iota-carratetraose
R9UQG9
yielding neo-iota-carratetraose as the main product in the absence of NaCl
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cs+
in the presence of 0.1 M CsCl, 63% of maximal activity is observed
K+
Li+
Na+
NaCl
although its activity is enhanced by NaCl, the enzyme is active in the absence of NaCl
Ca2+
Alteromonas fortis
-
enzyme contains three calcium binding sites involved in stabilizing the enzyme structure
K+
in the presence of 0.1 M KCl, 86% of maximal activity is observed
Li+
in the presence of 0.1 M LiCl, 42% of maximal activity is observed
Na+
the enzyme requires the Na+ ion for full activity, maximal activity is observed in the presence of 0.1 M NaCl. In buffer containing 10 mM NaCl, the enzyme activity decreases to 28% during 16 h incubation on ice
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
iota-carrageenan
Alteromonas fortis
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mutant enzyme H281A, at 40°C in 10 mM Tris, pH 8.0, and 100 mM NaCl
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2.4
iota-carrageenan
Alteromonas fortis
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mutant enzyme E310Q, at 40°C in 10 mM Tris, pH 8.0, and 100 mM NaCl
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8.5
iota-carrageenan
Alteromonas fortis
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wild type enzyme, at 40°C in 10 mM Tris, pH 8.0, and 100 mM NaCl
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.1
iota-carrageenan
Alteromonas fortis
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mutant enzyme H281A, at 40°C in 10 mM Tris, pH 8.0, and 100 mM NaCl
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13.8
iota-carrageenan
Alteromonas fortis
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mutant enzyme E310Q, at 40°C in 10 mM Tris, pH 8.0, and 100 mM NaCl
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726.6
iota-carrageenan
Alteromonas fortis
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wild type enzyme, at 40°C in 10 mM Tris, pH 8.0, and 100 mM NaCl
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.42
iota-carrageenan
Alteromonas fortis
-
mutant enzyme H281A, at 40°C in 10 mM Tris, pH 8.0, and 100 mM NaCl
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5.75
iota-carrageenan
Alteromonas fortis
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mutant enzyme E310Q, at 40°C in 10 mM Tris, pH 8.0, and 100 mM NaCl
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85.18
iota-carrageenan
Alteromonas fortis
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wild type enzyme, at 40°C in 10 mM Tris, pH 8.0, and 100 mM NaCl
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1870
pH 6.5, 45°C, with iota-carrageenan; purified enzyme, pH 6.5, 45°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
in a range of pH 7.0-10.0, the enzyme retains more than 80% of the original activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
in 50 mM Tris-HCl, pH 7.5, containing 0.1 M NaCl and 1 mM CaCl2
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48071
x * 48071, sequence calculation; x * 48071, sequence calculation, x * 54000, recombinant His-tagged enzyme, SDS-PAGE
54000
54000
x * 48071, sequence calculation, x * 54000, recombinant His-tagged enzyme, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
x * 48071, sequence calculation; x * 48071, sequence calculation, x * 54000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 48071, sequence calculation; x * 48071, sequence calculation, x * 54000, recombinant His-tagged enzyme, SDS-PAGE
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
concentration to 6 mg/ml using a dialyzing concentrator. The structure of iota-carrageenase bound to iota-carrageenan fragments is solved at 2.0 A resolution
Alteromonas fortis
hanging-drop vapour-diffusion method using polyethylene glycol (MW = 6000) as a precipitant. Crystals belong to space group P2(1), with unit-cell parameters a = 56.75 A, b = 91.04 A, c = 125.01 A, beta = 93.4°. The unit cell contains two molecules in the asymmetric unit related by a non-crystallographic twofold axis. Crystals diffracted to 2.0 A resolution on a synchrotron beamline
Alteromonas fortis
-
native and selenomethionyl-iota-carrageenase. Single crystals are obtained with polyethylene glycol, and the presence of Ca2+ appears to be crucial for crystallization. High quality crystals, typically 0.25 * 0.25 * 0.15 mM in dimension are grown with 0.1 M sodium cacodylate at pH 6.5, 15-17% polyethylene glycol and 200 mM calcium acetate. Crystallization of Se-Met-iota-carrageenase is performed under similar conditions except for the addition of 1 mM dithiothreitol and the replacement of sodium cacodylate by imidazole to avoid the reaction between cacodylate and dithiothreitol. Crystal structure at 1.6 A resolution
Alteromonas fortis
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
purified recombinant His-tagged enzyme, 45°C, 24 h, 60% activity remaining
731522
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
purified recombinant His-tagged enzyme, pH 6.5, 1 h, 80% activity remaining; purified recombinant His-tagged enzyme, pH 6.5, 1 h, inactivation; stable up to
45
the enzyme is stable up to 45°C in 50 mM Tris/HCl, pH 7.5, containing 0.1 M NaCl and 1 mM CaCl2 for 1 h. Incubation at 45°C inactivates the enzyme completely within 5 min at either condition of low NaCl concentration (less than 10 mM) or presence of 10 mM EDTA
50
purified recombinant His-tagged enzyme, pH 6.5, 1 h, 60% activity remaining
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme contains three calcium binding sites involved in stabilizing the enzyme structure
Alteromonas fortis
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, butyl-Toyopearl column chromatography, heparin affinity column chromatography, and Superdex 200 gel filtration
Ni-Sepharose column chromatography, Source 15S column chromatography, gel filtration
Alteromonas fortis
-
recombinant enzyme from Escherichia coli strain BL21(DE3) culture supernatant by affinity chromatography; recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Origami (DE3) pLysS, BL21 (DE3), C41 (DE3), and C43 (DE3) cells
Alteromonas fortis
-
gene cgiB_Ce, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21(DE3); gene cgiB_Ce, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene encoding iota-carrageenase flanked by a C-terminal hexahistidine tag and a N-terminal PelB signal peptide for targeting the gene product into Escherichia coli periplasm. The recombinant plasmid, referred to as pETIAf, is used to transform Escherichia coli BL21(DE3) strain harbouring pLysS plasmid
Alteromonas fortis
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E310Q
Alteromonas fortis
-
the Km value is reduced by a factor of about 4, the reduction in kcat by 50fold results in a substantial decrease in the overall enzyme efficiency (about 10fold)
H281A
Alteromonas fortis
-
the mutant shows 7fold decreased Km and 180fold decreased kcat value compared to the wild type enzyme with 4% relative efficiency
D359N
D359N
the mutant shows reduced activity compared to the wild type enzyme. Asp359 is not critical for catalysis
D359N
-
the mutant shows reduced activity compared to the wild type enzyme. Asp359 is not critical for catalysis
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
Alteromonas fortis
-
usage of the enzyme for the analysis of the distribution of the carrabiose moieties in hybrid carrageenan chains, hybrid iota-/alpha-carrageenan, by Pseudoalteromonas atlantica a 4S-iota carrageenan sulfatase that converts iota-carrabiose into alapha-carrabiose units
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LINKS TO OTHER DATABASES (specific for EC-Number 3.2.1.157)
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