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Information on EC 3.2.1.157 - iota-carrageenase

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IUBMB Comments
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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UNIPROT: E3W9G3
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhyd
Synonyms
iota-carrageenase, cgib_ce, cgi82a, cgia2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
the enzyme hydrolyses the beta-(1->4) linkages in iota-carrageenans to produce a series of homologous, even-numbered oligosaccharides. The cleavage of glycosidic linkage catalyzed by iota-carrageenases also involves carboxylic acid-containing amino acid residues but, in contrast to kappa-carrageenases, it occurs via a direct, single displacement reaction by a water molecule, so that the configuration in the anomeric position is inverted
PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
74191-25-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
iota-carrageenan + H2O
?
show the reaction diagram
-
-
-
?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose + iota-carrabiose
show the reaction diagram
-
-
-
?
iota-carrageenan + H2O
iota-carratetraose
show the reaction diagram
-
-
-
?
iota-carrageenan + H2O
iota-neocarratetraose sulfate + iota-neocarrahexaose sulfate
show the reaction diagram
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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-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
iota-carrageenan + H2O
?
show the reaction diagram
-
-
-
?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose + iota-carrabiose
show the reaction diagram
-
-
-
?
iota-carrageenan + H2O
iota-carratetraose
show the reaction diagram
-
-
-
?
additional information
?
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kappa-, iota- and lambda-carrageenase display strict specificity for their substrates, namely kappa-, iota- and lambda-carrageenans, respectively. The enzymes discriminate the substrate probably by recognizing the sulfation pattern of the digalactose reapeting unit of the polysaccharide. iota-Carrageenas present conserved arginine residues in the catalytic site which are believed to interact with carrageenans in which both sugar residues in the disaccharide units are negatively charged
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cs+
in the presence of 0.1 M CsCl, 63% of maximal activity is observed
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
Mg2+
activates 83% at 1 mM
NaCl
absolutely required for activity, maximal activity at 0.2 M, about 70% of maximal activity at 0.1 M, 60% at 1.0 M
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
87% inhibition at 1 mM
Fe2+
18% inhibition at 1 mM
Fe3+
96% inhibition at 1 mM
K+
25% inhibition at 1 mM
Mn2+
69% inhibition at 1 mM
SDS
96% inhibition at 1 mM
Zn2+
95.5% inhibition at 1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
124.55
purified recombinant enzyme, pH 8.0, 45°C
7.8
culture supernatant, at pH 7.5 and 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
activity range, recombinant enzyme, profile overview
7 - 10
in a range of pH 7.0-10.0, the enzyme retains more than 80% of the original activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
in 50 mM Tris-HCl, pH 7.5, containing 0.1 M NaCl and 1 mM CaCl2
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
activity range, recombinant enzyme, profile overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
the most important types of commercial carrageenans, namely kappa-, iota- and lambda-carrageenan, are esterified with one, two, and three sulfate groups per repeating disaccharide unit, being also called carrageenose 4'-sulfate, carrageenose 2,4'-disulfate, and carrageenose 2,6,2'-trisulfate, respectively. kappa-Carrageenans occur in the cell wall of some species of marine red algae, such as Chondrus sp., Gigartina sp., Eucheuma sp. and Iridaea sp. but is mostly extracted from tropical seaweed Euchema cottoni (also known as Kappaphycus alvarezii), while iota-carrageenans are mainly extracted from Eucheuma spinosum (also known as Eucheuma denticulatum). Because kappa- and iota-carrageenans are produced from my- and ny-carrageenans, respectively, during the extraction under alkaline at high temperatures or biosynthetically by a reaction catalyzed by the enzyme sulfohydrolase, these polysaccharides are often found in commercial samples. lambda-Carrageenans are extracted from red algae within the Gigartina and Chondrus genera, which produces this type of polysaccharide during the sporophytic stage. These algae are also a source of kappa- and iota-carrageenans when they are in the gametophytic stage, but because they produce mixed chain polysaccharide chains containing both kappa- and iota-units, extraction of kappa- and iota-carrageenans from the mentioned algae is preferred. Carrageenan classes based on the number and position of sulfate groups in the chain, overview. The sulfate and AD contents of commercial kappa-, iota-, and lambda-carrageenans have been determined by acid hydrolysis, infrared spectroscopy, and nuclear magnetic resonance (NMR) analyses and found to be, respectively, 25-30 and 28-35% for the kappa-type, 28-30 and 25-30% for iota-type and 32-39% and 0 for lambda-type, respectively
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
E3W9G3_9GAMM
569
0
62872
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 58000, recombinant enzyme, SDS-PAGE
monomer
1 * 55000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D359N
the mutant shows reduced activity compared to the wild type enzyme. Asp359 is not critical for catalysis
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
purified recombinant enzyme, over 60% activity remaining
755283
7 - 10
purified enzyme, over 80% activity remaining
755018
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
purified recombinant enzyme, stable up to, inactivation at 50°C
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, butyl-Toyopearl column chromatography, heparin affinity column chromatography, and Superdex 200 gel filtration
native enzyme 10.3fold by gel filtration
recombinant His-tagged enzyme from Brevibacillus choshinensis strain HPD31-SP3 by dialysis, nickel affinity chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Bacillus subtilis
gene cgiA, sequence comparisons and phylogenetic analysis
synthetic gene CGIOP, locus MF459059 in GenBank, codon-optimized gene encoding the iota-carrageenase without a signal peptide, cloned from gene cgiA of Microbulbifer thermotolerans strain JAMB-A94, construction of the integrative vector pBCGA, recombinant expression of extracellular His-tagged enzyme in Brevibacillus choshinensis strain HPD31-SP3, real-time PCR expression analysis, copy numbers of the CGIOP gene in different lines are approximately 5-6, respectively
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hatada, Y.; Mizuno, M.; Li, Z.; Ohta, Y.
Hyper-production and characterization of the iota-carrageenase useful for iota-carrageenan oligosaccharide production from a deep-sea bacterium, Microbulbifer thermotolerans JAMB-A94T, and insight into the unusual catalytic mechanism
Mar. Biotechnol.
13
411-422
2011
Microbulbifer thermotolerans (E3W9G3), Microbulbifer thermotolerans, Microbulbifer thermotolerans JAMB-A94T (E3W9G3)
Manually annotated by BRENDA team
Zhu, B.; Ni, F.; Sun, Y.; Zhu, X.; Yin, H.; Yao, Z.; Du, Y.
Insight into carrageenases major review of sources, category, property, purification method, structure, and applications
Crit. Rev. Biotechnol.
38
1261-1276
2018
Alteromonas macleodii (Q9F5I8), Cellulophaga sp. QY3 (R9UQG9), Flavobacterium sp. YS-80-122 (A0A1W5QBK3), Microbulbifer thermotolerans (E3W9G3), Microbulbifer thermotolerans JAMB-A94T (E3W9G3), Wenyingzhuangia fucanilytica (A0A1B1Y261), Zobellia galactanivorans (D9UAT1), Zobellia galactanivorans (Q9F284), Zobellia galactanivorans CCUG 47099 (D9UAT1), Zobellia galactanivorans CCUG 47099 (Q9F284), Zobellia galactanivorans CIP 106680 (D9UAT1), Zobellia galactanivorans CIP 106680 (Q9F284), Zobellia galactanivorans Dsij (D9UAT1), Zobellia galactanivorans Dsij (Q9F284), Zobellia galactanivorans DSM 12802 (D9UAT1), Zobellia galactanivorans DSM 12802 (Q9F284), Zobellia galactanivorans NCIMB 13871 (D9UAT1), Zobellia galactanivorans NCIMB 13871 (Q9F284)
Manually annotated by BRENDA team
Ghanbarzadeh, M.; Golmoradizadeh, A.; Homaei, A.
Carrageenans and carrageenases versatile polysaccharides and promising marine enzymes
Phytochem. Rev.
17
535-571
2018
Cellulophaga sp. QY3 (R9UQG9), Microbulbifer thermotolerans (E3W9G3), Microbulbifer thermotolerans JAMBA94T (E3W9G3), uncultured bacterium
-
Manually annotated by BRENDA team
Xu, Y.; Mao, W.; Gao, W.; Chi, Z.; Chi, Z.; Liu, G.
Efficient production of a recombinant iota-carrageenase in Brevibacillus choshinensis using a new integrative vector for the preparation of iota-carrageenan oligosaccharides
Process Biochem.
76
68-76
2019
Microbulbifer thermotolerans (E3W9G3), Microbulbifer thermotolerans JAMB-A94 (E3W9G3)
-
Manually annotated by BRENDA team