Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.157 - iota-carrageenase

for references in articles please use BRENDA:EC3.2.1.157
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: A0A1B1Y261
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The enzyme appears in viruses and cellular organisms
Reaction Schemes
hide
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
PATHWAY SOURCE
PATHWAYS
-
-
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
-
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
iota-carrabiose + iota-carratetraose
show the reaction diagram
-
-
-
?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
show the reaction diagram
additional information
?
-
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
iota-carrabiose + iota-carratetraose
show the reaction diagram
-
-
-
?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
activates at 0.1 M, inhibitory at over 0.3 M
NaCl
activates at 0.1 M, inhibitory at over 0.3 M
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
23% inhibition at 1 mM
Ca2+
6% inhibition at 1 mM
Cd2+
26% inhibition at 1 mM
EDTA
43% inhibition at 1 mM
KCl
activates at 0.1 M, inhibitory at over 0.3 M
Mn2+
13% inhibition at 1 mM
NaCl
activates at 0.1 M, inhibitory at over 0.3 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00112
iota-carrageenan
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
560.75
iota-carrageenan
pH 8.0, 30°C, recombinant enzyme
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.55
substrate iota-carrageenan, pH 8.0, 30°C, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A1B1Y261_9FLAO
513
0
55895
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 55000, recombinant His-tagged enzyme, SDS-PAGE, x * 57196, sequence calculation
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
purified recombinant His-tagged enzyme, stable at
754224
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
purified recombinant His-tagged enzyme, stable up to, 97% and 84% of the initial activity is retained after 24 h at 4°C and 25°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified recombinant His-tagged enzyme, 84% of initial activity remains after 30 days storage at 4°C without any protective additives
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cgi82A, recombinant expression of His6-tagged enzyme in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
the enzyme can be utilized as a potential biocatalyst for producing iota-carrageenan oligosaccharides with different polymerization degrees
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Shen, J.; Chang, Y.; Dong, S.; Chen, F.
Cloning, expression and characterization of a iota-carrageenase from marine bacterium Wenyingzhuangia fucanilytica A biocatalyst for producing iota-carrageenan oligosaccharides
J. Biotechnol.
259
103-109
2017
Wenyingzhuangia fucanilytica (A0A1B1Y261), Wenyingzhuangia fucanilytica, Wenyingzhuangia fucanilytica CZ1127 (A0A1B1Y261)
Manually annotated by BRENDA team