Any feedback?
Information on EC 3.2.1.83 - kappa-carrageenase
for references in articles please use BRENDA:EC3.2.1.83Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.83 kappa-carrageenaseIUBMB Comments
The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate . Unlike EC 3.2.1.157 (iota-carrageenase), but similar to EC 3.2.1.81 (beta-agarase), this enzyme proceeds with retention of the anomeric configuration.
Specify your search results
Word Map
- 3.2.1.83
- carrageenovora
-
pseudoalteromonas
-
carrageenases
-
cd19-specific
-
piggybac
-
anti-cd19
-
cd19-targeting
-
tisagenlecleucel
- galactans
- alteromonas
- beta-agarase
- pharmacology
- molecular biology
- analysis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-
Synonyms
car19, kappa-carrageenase, kappa-car, cgk-k142, cgk16a, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carrageenase, kappa-
-
-
-
-
CGK
Cgk-K142
Cgk16A
CgkA
CgkAGH16
kappa-car
kappa-carrageenanase
-
-
-
-
kappa-carrageenase-like protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-
endo or random mechanism
Pseudomonas carrageenovora
-
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-
enzyme has an arginine residue at subsite -1, mechanism
-
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-
enzyme acts in solution as a random hydrolase
-
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-alpha-D-galactopyranosyl-
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
kappa-carrageenan 4-beta-D-glycanohydrolase (configuration-retaining)
The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate [5]. Unlike EC 3.2.1.157 (iota-carrageenase), but similar to EC 3.2.1.81 (beta-agarase), this enzyme proceeds with retention of the anomeric configuration.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37288-59-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
kappa-carrageen + H2O
kappa-neocarrahexaose-sulfate + kappa-neocarrabiose-sulfate + kappa-neocarrahexaose-sulfate
kappa-carrageen + H2O
kappa-neocarraoctaose + kappa-neocarrahexaose + kappa-neocarratetraose + kappa-neocarrabiose
kappa-carrageen + H2O
kappa-neocarraoctaose-sulfate + kappa-neocarrahexaose-sulfate + kappa-neocarratetraose-sulfate + kappa-neocarrabiose-sulfate
-
-
-
-
?
kappa-carrageenan + H2O
kappa-neocarrabiose sulfate + kappa-neocarratetraose sulfate + kappa-neocarrahexaose sulfate + kappa-neocarraoctaose sulfate + kappa-neocarradecaose sulfate + D-galactose
agar + H2O
?
-
1.5% activity compared to kappa-carrageenan
-
-
?
iota-carrageenan + H2O
?
-
1% activity compared to kappa-carrageenan
-
-
?
iota-carrageenan + H2O
?
-
1% activity compared to kappa-carrageenan
-
-
?
kappa-carrageen + H2O
?
the enzyme cleaves in an endo-fashion
-
-
?
kappa-carrageen + H2O
?
the enzyme cleaves in an endo-fashion
-
-
?
kappa-carrageen + H2O
carrageenan oligosaccharide
-
the enzyme cleaves kappa-carrageenan at the internal beta-1,4 linkage of kappa-carrageenan
the enzyme degrades kappa-carrageenan to sulfated oligosaccharides with even-numbered degree of polymerization, of which the tetrasaccharide was the major product, identification and structural analysis by mass spectrometry, overview. Each carrageenan oligosaccharide is composed of An-G4S-type neocarrabiose units, which consisted of a 3,6-anhydro-alpha-D-galactose residue in the nonreducing end and a beta-D-galactose-4-sulfate residue in the reducing end
-
?
kappa-carrageen + H2O
carrageenan oligosaccharide
-
the enzyme cleaves kappa-carrageenan at the internal beta-1,4 linkage of kappa-carrageenan
the enzyme degrades kappa-carrageenan to sulfated oligosaccharides with even-numbered degree of polymerization, of which the tetrasaccharide was the major product, identification and structural analysis by mass spectrometry, overview. Each carrageenan oligosaccharide is composed of An-G4S-type neocarrabiose units, which consisted of a 3,6-anhydro-alpha-D-galactose residue in the nonreducing end and a beta-D-galactose-4-sulfate residue in the reducing end
-
?
kappa-carrageen + H2O
D-galactose + ?
-
the enzyme cleaves the internal beta-(1-4) linkages of kappa-carrageenan yielding a series of even-numbered oligosaccharides
-
-
?
kappa-carrageen + H2O
D-galactose + ?
-
the enzyme cleaves the internal beta-(1-4) linkages of kappa-carrageenan yielding a series of even-numbered oligosaccharides
-
-
?
kappa-carrageen + H2O
D-galactose + ?
-
the enzyme cleaves the internal beta-(1-4) linkages of kappa-carrageenan yielding a series of even-numbered oligosaccharides
-
-
?
kappa-carrageen + H2O
D-galactose + ?
-
the enzyme cleaves the internal beta-(1-4) linkages of kappa-carrageenan yielding a series of even-numbered oligosaccharides
-
-
?
kappa-carrageen + H2O
kappa-neocarrahexaose + kappa-neocarratetraose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarrahexaose + kappa-neocarratetraose
Zobellia galactanivorans DsijT
-
-
-
?
kappa-carrageen + H2O
kappa-neocarrahexaose + kappa-neocarratetraose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarrahexaose + kappa-neocarratetraose + D-galactose
-
-
-
-
?
kappa-carrageen + H2O
kappa-neocarrahexaose + kappa-neocarratetraose + D-galactose
Pedobacter hainanensis NJ-02
-
-
-
-
?
kappa-carrageen + H2O
kappa-neocarrahexaose-sulfate + kappa-neocarrabiose-sulfate + kappa-neocarrahexaose-sulfate
-
the enzyme is specific for the beta-1,4 linkage and hydrolyzes kappa-carrageenan into kappa-neocarraoctaose-sulfate and kappa-neocarrahexaose-sulfate first, and then brakes kappa-neocarraoctaose-sulfate into kappa-neocarrabiose-sulfate and kappa-neocarrahexaose-sulfate, NMR spectroscopy analysis, overview
-
-
?
kappa-carrageen + H2O
kappa-neocarrahexaose-sulfate + kappa-neocarrabiose-sulfate + kappa-neocarrahexaose-sulfate
-
the enzyme is specific for the beta-1,4 linkage and hydrolyzes kappa-carrageenan into kappa-neocarraoctaose-sulfate and kappa-neocarrahexaose-sulfate first, and then brakes kappa-neocarraoctaose-sulfate into kappa-neocarrabiose-sulfate and kappa-neocarrahexaose-sulfate, NMR spectroscopy analysis, overview
-
-
?
kappa-carrageen + H2O
kappa-neocarraoctaose + kappa-neocarrahexaose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarraoctaose + kappa-neocarrahexaose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarraoctaose + kappa-neocarrahexaose + kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
-
?
kappa-carrageen + H2O
kappa-neocarraoctaose + kappa-neocarrahexaose + kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose + D-galactose
-
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose + D-galactose
Pseudoalteromonas carrageenovora CICC 23819
-
-
-
-
?
kappa-carrageenan + H2O
?
-
low-molecular-weight carrageenan oligosaccharides are obtained. Antitumor activities of the oligosaccharides are tested on Sarcoma 180 tumor transplanted in mice. The carrageenan oligosaccharide show much higher tumor inhibition (70.8%) and catalase activity at a dosage of 100 mg/kg compared with the control group
-
-
?
kappa-carrageenan + H2O
?
-
low-molecular-weight carrageenan oligosaccharides are obtained. Antitumor activities of the oligosaccharides are tested on Sarcoma 180 tumor transplanted in mice. The carrageenan oligosaccharide show much higher tumor inhibition (70.8%) and catalase activity at a dosage of 100 mg/kg compared with the control group
-
-
?
kappa-carrageenan + H2O
?
-
on soluble kappa-carrageenan substrate, enzyme produces only large oligosaccharides at 50% of degradation. In contrast, at the same level of degradation in solid phase, enzyme generates terminal products such as kappa-neocarrabiose and kappa-neocarratetraose
-
-
?
kappa-carrageenan + H2O
?
-
the average molecular mass of solid carrageenan decreases very slowly, and tetrasaccharide production is high. kappa-carrageenase is a processive enzyme when acting on solid substrates. It has a random mode of action on soluble substrates. The conditions for processivity not only require that the active site possesses the adapted topology, but also that the substrate is in an appropriate physical and conformational state (processivity is similar for gel and powder)
-
-
?
kappa-carrageenan + H2O
?
-
degradation, analysis of the degradation products by gel filtration, single-helix ordered conformation state for kappa-carrageenan. Degradation of carrageenan in the disordered state leads to a rapid decrease in molecular mass and the production of all possible neo-kappa-carrabiose oligomers
-
-
?
kappa-carrageenan + H2O
kappa-neocarrabiose sulfate + D-galactose
-
the enzyme degrades kappa-carrageenan by hydrolyzing the beta-1,4 linkages to a series of homologous, even numbered oligosaccharides
-
-
?
kappa-carrageenan + H2O
kappa-neocarrabiose sulfate + D-galactose
-
the enzyme degrades kappa-carrageenan by hydrolyzing the beta-1,4 linkages to a series of homologous, even numbered oligosaccharides
-
-
?
kappa-carrageenan + H2O
kappa-neocarrabiose sulfate + kappa-neocarratetraose sulfate + kappa-neocarrahexaose sulfate + kappa-neocarraoctaose sulfate + kappa-neocarradecaose sulfate + D-galactose
-
-
main end-products
-
?
kappa-carrageenan + H2O
kappa-neocarrabiose sulfate + kappa-neocarratetraose sulfate + kappa-neocarrahexaose sulfate + kappa-neocarraoctaose sulfate + kappa-neocarradecaose sulfate + D-galactose
-
-
main end-products
-
?
kappa-carrageenan + H2O
tetrasaccharides
-
100% activity
-
-
?
lambda-carrageenan + H2O
?
-
39.3% activity compared to kappa-carrageenan
-
-
?
lambda-carrageenan + H2O
?
-
39.3% activity compared to kappa-carrageenan
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
kappa-neocarratetraose
?
kappa-carrageenan + H2O
additional information
-
Pseudomonas carrageenovora
-
-
3-O-(3,6-anhydro-alpha-D-galactopyranosyl)-D-galactopyranose-4-O-sulfate, i.e. neocarrabiose-4-O-sufate, as the major degradation product
?
kappa-carrageenan + H2O
additional information
-
Pseudomonas carrageenovora
-
-
3-O-(3,6-anhydro-alpha-D-galactopyranosyl)-D-galactopyranose-4-O-sulfate, i.e. neocarrabiose-4-O-sufate, as the major degradation product
?
additional information
?
-
Bacillus sp. HT19
-
no activity with iota-carrageenan, lambda-carrageenan, agar, and sodium alginate
-
-
?
additional information
?
-
no activity with iota- or lambda-carrageenan, or any other polysaccharides such as agar, alginate, cellulose and starch
-
-
?
additional information
?
-
no activity with iota- or lambda-carrageenan, or any other polysaccharides such as agar, alginate, cellulose and starch
-
-
?
additional information
?
-
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
?
additional information
?
-
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
?
additional information
?
-
-
raffinose and p-nitrophenyl-alpha-D-galactopyranoside are not hydrolyzed
-
-
?
additional information
?
-
-
isolated kappa-carrageenase can successfully generate protoplasts of Kappaphycus alvarezii. No activity with lambda-carrageenan, ioro-carrageenan and LMP agarose
-
-
?
additional information
?
-
-
the enzyme also catalyzes transglycosylation
-
-
?
additional information
?
-
-
hybrid kappa/iota-carrageeans extracted from Gigartina skottsbergii, Chondracanthus chamissoi, and Chondrus crispus are incubated with kappa-carrageenase. The degradation products of the kappa-carrageenase allow discriminating three modes of kappa-carrabiose distribution: blocks of kappa-carrabiose, kappa-carrabiose rich fraction containing iota-carrabiose units probably randomly distributed, and iota-carrabiose rich fraction which corresponds to the resistant fraction
-
-
?
additional information
?
-
the enzyme is incapable of hydrolyzing iota-carrageenan, lambda-carrageenan and agarose
-
-
?
additional information
?
-
-
the enzyme is incapable of hydrolyzing iota-carrageenan, lambda-carrageenan and agarose
-
-
?
additional information
?
-
the enzyme is incapable of hydrolyzing iota-carrageenan, lambda-carrageenan and agarose
-
-
?
additional information
?
-
the enzyme specifically cleaves the internal beta (1-4) linkages of carrageenans and yields a series of homologous even-numbered oligosaccharides
-
-
?
neocarrahexaitol + H2O
additional information
-
-
-
neocarrabiitol and beta-neocarratetraose are initially formed
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
kappa-carrageen + H2O
kappa-neocarraoctaose + kappa-neocarrahexaose + kappa-neocarratetraose + kappa-neocarrabiose
kappa-carrageen + H2O
kappa-neocarraoctaose-sulfate + kappa-neocarrahexaose-sulfate + kappa-neocarratetraose-sulfate + kappa-neocarrabiose-sulfate
-
-
-
-
?
kappa-carrageen + H2O
?
the enzyme cleaves in an endo-fashion
-
-
?
kappa-carrageen + H2O
?
the enzyme cleaves in an endo-fashion
-
-
?
kappa-carrageen + H2O
D-galactose + ?
-
the enzyme cleaves the internal beta-(1-4) linkages of kappa-carrageenan yielding a series of even-numbered oligosaccharides
-
-
?
kappa-carrageen + H2O
D-galactose + ?
-
the enzyme cleaves the internal beta-(1-4) linkages of kappa-carrageenan yielding a series of even-numbered oligosaccharides
-
-
?
kappa-carrageen + H2O
D-galactose + ?
-
the enzyme cleaves the internal beta-(1-4) linkages of kappa-carrageenan yielding a series of even-numbered oligosaccharides
-
-
?
kappa-carrageen + H2O
D-galactose + ?
-
the enzyme cleaves the internal beta-(1-4) linkages of kappa-carrageenan yielding a series of even-numbered oligosaccharides
-
-
?
kappa-carrageen + H2O
kappa-neocarrahexaose + kappa-neocarratetraose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarrahexaose + kappa-neocarratetraose
Zobellia galactanivorans DsijT
-
-
-
?
kappa-carrageen + H2O
kappa-neocarraoctaose + kappa-neocarrahexaose + kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
-
?
kappa-carrageen + H2O
kappa-neocarraoctaose + kappa-neocarrahexaose + kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose + D-galactose
-
-
-
-
?
kappa-carrageen + H2O
kappa-neocarratetraose + kappa-neocarrabiose + D-galactose
Pseudoalteromonas carrageenovora CICC 23819
-
-
-
-
?
additional information
?
-
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
?
additional information
?
-
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
?
additional information
?
-
the enzyme specifically cleaves the internal beta (1-4) linkages of carrageenans and yields a series of homologous even-numbered oligosaccharides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-mercaptoethanol
-
the enzyme activity is significantly promoted at 1 mM 2-mercaptoethanol
Ca2+
dithiothreitol
-
the enzyme activity is significantly promoted at 1 mM dithiothreitol
EDTA
-
the enzyme activity is significantly promoted at 1 mM EDTA
Fe3+
-
the enzyme activity is significantly promoted at 1 mM Fe3+
K+
Mg2+
Na+
SDS
-
the enzyme activity is significantly promoted at 1 mM SDS
Sn2+
-
the enzyme activity is significantly promoted at 1 mM Sn2+
Triton X-100
-
the enzyme activity is significantly promoted at 1 mM Triton X-100
Tween-20
-
the enzyme activity is significantly promoted at 1 mM Tween 20
Tween-80
-
the enzyme activity is significantly promoted at 1 mM Tween 80
Urea
-
the enzyme activity is significantly promoted at 1 mM urea
additional information
K+
-
the enzyme activity is significantly promoted at low concentrations of K+
Na+
-
the enzyme activity is significantly promoted at low concentrations of Na+
additional information
Bacillus sp. HT19
-
Ni2+, Mg2+ and Mn2+ have almost no effect on the enzyme activity
additional information
the enzyme is not significantly influenced by K+, Mg2+ and Zn2+
additional information
-
the enzyme is not significantly influenced by K+, Mg2+ and Zn2+
additional information
poor effects by Li+, Mg2+, NH4+, Ca2+ and K+ at 5 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaI
-
strong inhibition at 200 mM, inhibition is caused by iodide binding
K+
-
the enzyme activity is inhibited by high concentrations of K+
Na+
-
the enzyme activity is inhibited by high concentrations of Na+
Na+
-
85.13%, 84.95% and 46.77% residual activity at 10, 100 and 200 mM, respectively
additional information
-
not inhibited by Sr2+, Ba2+, K+, Ca2+, Mg2+ or Fe2+
-
additional information
no effect by NEM, iodoacetate, 2-phenanthroline, DTT, 2-mercaptoethanol, N-bromosuccimide, and 4-chloromercuribenzoate
-
additional information
-
no effect by NEM, iodoacetate, 2-phenanthroline, DTT, 2-mercaptoethanol, N-bromosuccimide, and 4-chloromercuribenzoate
-
additional information
EDTA, TritonX-100, Tween-80, methanol, and glycerol have minimal effects on the activity of the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
the enzyme does not require NaCl for activity, although its activity is enhanced by NaCl (226.8% activity at 200 mM)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Graft vs Host Disease
[Maintenance therapy following CD19 CAR-T treatment for relapsed B-cell acute lymphoblastic leukemia after allogeneic hematopoietic stem cell transplantation].
Leukemia
Low-cost generation of Good Manufacturing Practice-grade CD19-specific chimeric antigen receptor-expressing T cells using piggyBac gene transfer and patient-derived materials.
Leukemia
[Maintenance therapy following CD19 CAR-T treatment for relapsed B-cell acute lymphoblastic leukemia after allogeneic hematopoietic stem cell transplantation].
Leukemia, Lymphocytic, Chronic, B-Cell
Low-cost generation of Good Manufacturing Practice-grade CD19-specific chimeric antigen receptor-expressing T cells using piggyBac gene transfer and patient-derived materials.
Lymphoma
CAR T cells with dual targeting of CD19 and CD22 in adult patients with recurrent or refractory B cell malignancies: a phase 1 trial.
Lymphoma
CAR T-Cell Therapy Is Effective but Not Long-Lasting in B-Cell Lymphoma of the Brain.
Lymphoma
Development of CAR T-cell lymphoma in two of ten patients effectively treated with piggyBac modified CD19 CAR T-cells.
Lymphoma
Lenalidomide enhances antitumor functions of chimeric antigen receptor modified T cells.
Lymphoma, B-Cell
CAR T cells with dual targeting of CD19 and CD22 in adult patients with recurrent or refractory B cell malignancies: a phase 1 trial.
Lymphoma, Non-Hodgkin
Low-cost generation of Good Manufacturing Practice-grade CD19-specific chimeric antigen receptor-expressing T cells using piggyBac gene transfer and patient-derived materials.
Neoplasms
Anti-CD19 CAR T Cells That Secrete a Biparatopic Anti-CLEC12A Bridging Protein Have Potent Activity Against Highly Aggressive Acute Myeloid Leukemia In Vitro and In Vivo.
Neoplasms
Development of CAR T-cell lymphoma in two of ten patients effectively treated with piggyBac modified CD19 CAR T-cells.
Neoplasms
Low-cost generation of Good Manufacturing Practice-grade CD19-specific chimeric antigen receptor-expressing T cells using piggyBac gene transfer and patient-derived materials.
Neoplasms
Self-driving armored CAR-T cells overcome a suppressive milieu and eradicate CD19+ Raji lymphoma in preclinical models.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Development of CAR T-cell lymphoma in two of ten patients effectively treated with piggyBac modified CD19 CAR T-cells.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Genetic mechanisms of target antigen loss in CAR19 therapy of acute lymphoblastic leukemia.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000385
kappa-carrageen
mutant enzyme Q171A, at pH 7.0 and 40°C
-
0.000683
kappa-carrageen
wild type enzyme, at pH 7.0 and 40°C
-
0.000822
kappa-carrageen
wild type enzyme, at pH 7.0 and 40°C
-
0.000899
kappa-carrageen
mutant enzyme R92A, at pH 7.0 and 40°C
-
0.00115
kappa-carrageen
mutant enzyme R196A, at pH 7.0 and 40°C
-
0.00121
kappa-carrageen
mutant enzyme R151A, at pH 7.0 and 40°C
-
0.00263
kappa-carrageen
mutant enzyme W266A, at pH 7.0 and 40°C
-
additional information
additional information
-
Km-value for kappa-carrageenan is 6.66 mg/ml
-
additional information
additional information
-
Km value for kappa-carrageenan is 1.647 mg/ml at 35°C and pH 7.0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.13
kappa-carrageen
mutant enzyme R196A, at pH 7.0 and 40°C
-
27.36
kappa-carrageen
mutant enzyme W266A, at pH 7.0 and 40°C
-
120.17
kappa-carrageen
mutant enzyme Q171A, at pH 7.0 and 40°C
-
135.84
kappa-carrageen
wild type enzyme, at pH 7.0 and 40°C
-
183.2
kappa-carrageen
mutant enzyme R92A, at pH 7.0 and 40°C
-
478.79
kappa-carrageen
mutant enzyme R151A, at pH 7.0 and 40°C
-
914.65
kappa-carrageen
wild type enzyme, at pH 7.0 and 40°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5310
kappa-carrageen
mutant enzyme R196A, at pH 7.0 and 40°C
-
10400
kappa-carrageen
mutant enzyme W266A, at pH 7.0 and 40°C
-
199000
kappa-carrageen
wild type enzyme, at pH 7.0 and 40°C
-
204000
kappa-carrageen
mutant enzyme R92A, at pH 7.0 and 40°C
-
312000
kappa-carrageen
mutant enzyme Q171A, at pH 7.0 and 40°C
-
397000
kappa-carrageen
mutant enzyme R151A, at pH 7.0 and 40°C
-
1110000
kappa-carrageen
wild type enzyme, at pH 7.0 and 40°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.6
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
For recombinant enzyme, at pH 4.0 or 8.0, the relative activity decreases to approximately 76%
4 - 9
about 25% activity at pH 4.0, about 47% activity at pH 5.0, about 75% activity at pH 6.0, 100% activity at pH 7.0, about 65% activity at pH 8.0, about 30% activity at pH 9.0
4.8 - 9
-
pH 4.8: about 70% of maximal activity, pH 9.0: about 60% of maximal activity
5 - 8
6 - 9
7 - 9
-
more than 70% activity at pH 8.0, more than 60% activity at pH 9.0 in Tris-HCl buffer
5 - 8
-
pH 5.0: about 50% of maximal activity, pH 8.0: about 75% of maximal activity
6 - 9
-
the enzyme maintains more than 70% of total activity between pH 6.0 and 9.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
35
40
50
55
60
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 30
the enzyme shows 81% and 52% of its maximal activity at 20°C and 15°C respectively. The activity vanishes rapidly at 30°C and 40°C
15 - 45
-
15°C: about 40% of maximal activity, 45°C: about 50% of maximal activity
20 - 50
-
about 45% activity at 20°C, about 80% activity at 30°C, 100% activity at 40°C, about 65% activity at 50°C
20 - 60
25 - 50
about 75% activity at 25°C, about 85% activity at 30°C, 100% activity at 35°C, about 95% activity at 40°C, about 90% activity at 45°C, about 55% activity at 50°C
40 - 70
Bacillus sp. HT19
-
about 40% activity at 40°C, about 90% activity at 50°C, 100% activity at 60°C, about 55% activity at 70°C
50 - 55
the recombinant enzyme shows the highest activity at 50°C and its relative activity decreases to 89% at 55°C
20 - 60
Pseudomonas carrageenovora
-
20°C: about 60% of maximal activity, 60°C: about 25% of maximal activity, 15 min assay
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from seaside soil under the stacks of red algae in Hainan province of China
-
-
brenda
Pseudomonas carrageenovora
isolated from the sediment of carrageenan production base in Hainan (Hainan, China)
-
-
brenda
isolated from the sediment of carrageenan production base in Hainan (Hainan, China)
-
-
brenda
isolated from seaside soil under the stacks of red algae in Hainan province of China
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
synthesized and released from resting cells and growing cells
brenda
-
synthesized and released from resting cells and growing cells
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme contains an N-terminal 28-amino acid signal peptide
-
brenda
-
the enzyme contains an N-terminal 28-amino acid signal peptide
-
-
brenda
the enzyme contains a 28-amino acid signal peptide
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycosyl hydrolase family 16, GH16
Show AA Sequence and Transmembrane Helices (279 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
37300
x * 37300, recombinant His-tagged extracellular and intracellular enzyme, SDS-PAGE
40000
45000
x * 45000, catalytic domain of kappa-carrageenase CgkA, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
?
x * 45000, catalytic domain of kappa-carrageenase CgkA, SDS-PAGE
?
x * 37300, recombinant His-tagged extracellular and intracellular enzyme, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
processed upon secretion from a 44000 Da preproprotein to a 32000 Da secretion product, first by N-terminal removal of the 25-amino-acid signal peptide, then by cleavage of a 96-amino-acid C-terminal region from amino acids 302-397
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme E168D in complex with kappa-neocarratetraose, hanging drop vapor diffusion method, using 1.0 M sodium citrate and 100 mM cacodylate at pH 6.5
hanging drop vapor diffusion method, 28-29% PEG 3350, 100 mM MES, pH 6.5, and 0.3 M NaNO3
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R260A
the mutant shows less than 1% of wild type activity
additional information
construction of a chimeric fusion protein consisting of the catalytic domains of kappa-carrageenase CgkA and lambda-carrageenase CglA from Pseudoalteromonas carrageenovora fused with a dockerin domain from Clostridium cellulovorans. The recombinant cCgkA and cCglA are assembled with scaffoldin miniCbpA from Clostridium cellulovorans via cohesin and dockerin interaction. Carbohydrate binding module in scaffoldin is used as a tag
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
more than 50% of the enzyme activity is maintained after incubation at pH 5.0-8.0 and 4°C for 6 h
750769
5 - 9
-
the enzyme retains more than 80% of its maximal activity after being incubated for 30 min at pH of 5.0-9.0 below 40°C
750778
6 - 10
-
the enzyme maintains 80% of total activity after 24 h between pH 6.0 and 10.0. At pH 5.0 and 11.0, the activity drops to about 55% and 2%, respectively
751305
6 - 10.5
the enzyme is stable for 1 h between pH 6.0-10.5
750788
6 - 9
7 - 9
-
the enzyme is considerably stable from pH 7.0 to 9.0, where its activity declines by less than 10%
752081
8 - 10
-
the enzyme retains more than 80% of the maximum enzymatic activity after 30 min of incubation at a pH range of 8.0-10.0
751519
6 - 9
-
the activity of the enzyme is stable from pH 6.0 to 9.0, greater than 70.0% of the residual activity is maintained after treatment at pH from 6.0 to 9.0 and 4°C for 6 h, 100% of activity is maintained after treatment at pH 8.0 and 4°C for 6 h
716808
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 50
-
the purified kappa-carrageenase is stable in the range of 0-30°C and the residual enzyme activity is still retained at 96.1% of the control after treatment at 30°C for 1 h. The enzyme is inactivated rapidly at temperatures higher than 30°C and is almost inactivated at 50°C within 1 h
10 - 40
20
-
40% loss of activity within 5 days, complete loss of activity within 12 days
25
42% of residual activity is retained after 24 h at 25°C
28 - 75
-
the enzyme is stable at 28°C, but 95% of the activity is lost at 50-75°C for 30 min
30
35
4
-
the half-life of free enzyme and enzyme immobilized on magnetic iron oxide nanoparticles at 4°C are 17.4 and 20.6 d, respectively
40
40 - 45
-
the enzyme retains more than 95% and 60% of the maximum enzymatic activity after 1 h of incubation at 40°C and below 45°C, respectively
40 - 50
-
over 80% of the total activity is retained after 60 min at 40°C. When the incubation temperature rises above 45°C, the activity of the enzyme decreases rapidly. Furthermore, the enzyme is almost inactivated at 50°C within 60 min
42 - 50
after incubation at 45°C for 4 h, approximately 50% of the enzymatic activity is retained. When the recombinant enzyme is incubated at 42.5°C for 4 h, more than 90% of the enzymatic activity is retained. The recombinant enzyme is stable below 42.5°C. Approximately 50% of the enzymatic activity is lost after 1 h of incubation at 47.5°C and after 30 min of incubation at 50°C
45
purified recombinant enzyme, pH 6.0, 15 min, 20% activity remaining
45 - 60
-
enzyme activity is stable (more than 91%) for 2 h at temperatures of above 45°C. However, 90% of the activity is lost after incubation at 50-60°C for 30 min
50
50 - 70
Bacillus sp. HT19
-
the enzyme retains more than 90% of its initial activity after incubation at 50-60°C for 24 h. The activity declines sharply after 60 min of incubation at 70°C
additional information
10 - 40
-
the enzyme retains more than 90% activity after 3 h at 10-40°C
10 - 40
-
the enzyme maintains more than 90% of total activity after 30 min at 10-40°C. At 50°C, the activity drops to about 20%
30
85% of the enzymatic activities remain after being incubated at 30°C for 1 h
35
the enzyme retains more than 75% of its initial activity after heat treatment below 35°C for 2 h
additional information
no protective effect on enzyme thermal stability by Ca2+, Mg2+, agar, and NaCl
additional information
-
no protective effect on enzyme thermal stability by Ca2+, Mg2+, agar, and NaCl
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the magnetic iron oxide nanoparticles-immobilized enzyme maintains 43.5% of the original activity after being used 4 times
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme without any protective additives, at least 30 days, no loss of activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, CM-cellulose 52 column chromatography, and Sephadex G-200 gel filtration
-
ammonium sulfate precipitation, Sephadex 200 gel filtration, and Sephadex G-75 gel filtration
-
ammonium sulfate precipitation, Sephadex G-200 gel filtration, and DE-cellulose 52 anion-exchange chromatography
-
by metal-affinity chromatography followed by cation exchange chromatography
-
DEAE Sepharose column chromatography and HiTrap column chromatography
-
His Trap column chromatography and Sephacryl S-100 gel filtration
-
native enzyme from culture supernatant by ammonium sulfate fractionation and adsorption chromatography
-
native extracellular enzyme to electrophoretic homogeneity from culture supernatant by ammonium sulfate fractionation, dialysis, and two different steps of gel filtration
-
Ni affinity column chromatography and Sephadex gel filtration
Ni-Sepharose column chromatography
recombinant CBM-tagged chimeric fusion enzyme cCgkA-cCglA by cellulose affinity purification using cellulose as a support or by nickel affinity chromatography
recombinant extracelluar enzyme 388.6fold from Escherichia coli strain DH5alpha by ammonium sulfate fractionation, dialysis, anion and cation exchange chromatography to homogeneity
recombinant extracellular (24fold) and intracellular (19fold) His-tagged enzyme from Escherichia coli strain BL21 (DE3) cell-free extract and culture supernatant by ammonium sulfate fractionation, dialysis, nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from the periplasm of Escherichia coli strain BL21(DE3) by nickel affinity chromatography and cation exchange chromatography
-
Ni affinity column chromatography and Sephadex gel filtration
Ni affinity column chromatography and Sephadex gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain DH5alpha as extracellular enzyme
expressed in Escherichia coli BL21(DE3) cells
gene cgkA, recombinant expression of functional CBM-tagged chimeric fusion enzyme cCgkA-cCglA, consisting of the catalytic domains of kappa-carrageenase CgkA and lambda-carrageenase CglA from Pseudoalteromonas carrageenovora fused with a dockerin domain, in Escherichia coli strain BL21(DE3), cloning in Escherichia coli strain DH5alpha
gene cgkZ, DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression of His-tagged enzyme with and without signal peptide extracellulary and intracellularly in Escherichia coli strain BL21 (DE3), cloning in Escherichia coli strain DH5alpha
gene cgkZ, recombinant expression of N-terminally His6-tagged extracellular enzyme in Escherichia coli strain BL21(DE3), 51% of the total kappa-carrageenase is secreted into culture medium, and 33% accumulates in the periplasmic space. Low temperature of 23°C and optimal isopropyl-beta-L-thiogalactoside concentration of 0.9 mM favor soluble protein expression, additives such as lactose, glycine, Tween-80, and Triton X-100 promote the release of intracellular enzymes, method optimization and evaluation, overview
His-tagged enzyme expression in the periplasm of Escherichia coli strain BL21(DE3)
-
overexpressed as a His-tagged fusion protein in Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
Pseudomonas carrageenovora
-
potential use in the future in the field of seaweed biotechnology for obtaining protoplasts, and in molecular biology to prevent severe separation problems occuring in the presence of phycocolloid oligomers
pharmacology
Pseudomonas carrageenovora
-
potential use in the future: production of defined phycocolloid oligomers for pharmacy and immunology
additional information
additional information
-
the enzymatic degradation offers an alternative approach to prepare kappa-carrageenan oligosaccharides, which could be used as a powerful tool for further study on biological activity-structure relationship and thorough industrial exploitation of kappacarrageenan
additional information
-
the enzymatic degradation offers an alternative approach to prepare kappa-carrageenan oligosaccharides, which could be used as a powerful tool for further study on biological activity-structure relationship and thorough industrial exploitation of kappacarrageenan
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zemek, J.; Marvanova, L.; Kuniak, L.; Kadlecikova, B.
Hydrolytic enzymes in aquatic hyphomycetes
Folia Microbiol. (Praha)
30
363-372
1985
Alatospora acuminata, Alatospora flagellata, Anguillospora crassa, Amniculicola longissima, Articulospora tetracladia, Calcalispora hiemalis, Clavariopsis aquatica, Culicidospora gravida, Dactylella aquatica, Dendrospora erecta, Aquanectria penicillioides, Gyoerffyella gemellipara, Gyoerffyella rotula, Gyoerffyella speciosa, Heliscella stellata, Neonectria lugdunensis, Lateriramulosa uni-inflata, Lemonniera aquatica, Lemonniera centrosphaera, Lemonniera cornuta, Lemonniera terrestris, Margaritispora aquatica, no activity in Tricladium angulatum, Pleuropedium tricladioides, Pyramidospora densa, Sigmoidea prolifera, Taeniospora gracilis, Tetrachaetum elegans, Tetracladium marchalianum, Tetracladium maxilliforme, Tetracladium setigerum, Tricellula aquatica, Tricladium splendens, Varicosporium elodeae, Ypsilina graminea
-
brenda
Weigl, J.; Yaphe, W.
The enzymic hydrolysis of carrageenan by Pseudomonas carrageenovora: purification of a kappa-carrageenase
Can. J. Microbiol.
12
939-947
1966
Pseudomonas carrageenovora
brenda
McLean, M.M.; Williamson, F.B.
kappa-Carrageenase from Pseudomonas carrageenovora
Eur. J. Biochem.
93
553-558
1979
Pseudomonas carrageenovora
brenda
Benites, L.V.; Macaranas, J.M.
Partial purification of a carragenase from the tropical sea urchin Diadema setosum
Proc. Int. Seaweed Symp.
9
353-359
1977
Diadema setosum
-
brenda
Benites, L.V.; Macaranas, J.M.
Purification and characterization of a kappa-carragenase from the tropical sea urchin, Diadema setosum Leske
Inf. Ser. , N. Z. Dep. Sci. Ind. Res. , 137 (Proc. Int. Symp. Mar. Biogeogr. Evol. South. Hemisphere)
2
371-376
1978
Diadema setosum
-
brenda
McLean, M.W.; Williamson, F.B.
Enzymes from Pseudomonas carrageenovora. Application to studies of carrageenan structure
Proc. Int. Seaweed Symp.
10
479-484
1981
Pseudomonas carrageenovora
-
brenda
Dyrset, N.; Lystad, K.Q.; Levine, D.W.
Development of a fermentation process for production of a kappa-carrageenase from Pseudomonas carrageenovora
Enzyme Microb. Technol.
20
418-423
1997
Pseudomonas carrageenovora
-
brenda
Sarwar, G.; Sakata, T.; Kakimoto, D.
The production and characteristics of carrageenase from marine Cytophaga
Nippon Suisan Gakkaishi
49
1689-1694
1983
Cytophaga sp., Cytophaga sp. 1k-C783
-
brenda
Sarwar, G.; Oda, H.; Sakawa, T.; Kakimoto, D.
Potentiality of artificial sea water salts for the production of carrageenase by a marine Cytophaga sp
Microbiol. Immunol.
29
405-411
1985
Cytophaga sp., Cytophaga sp. 1k-C783
brenda
Sarwar, G.; Matayoshi, S.; Oda, H.
Purification of a kappa-carrageenase from marine Cytophaga species
Microbiol. Immunol.
31
869-877
1987
Cytophaga sp., Cytophaga sp. 1k-C783
brenda
Michel, G.; Barbeyron, T.; Flament, D.; Vernet, T.; Kloareg, B.; Dideberg, O.
Expression, purification, crystallization and preliminary X-ray analysis of the kappa-carrageenase from Pseudomonas carrageenovora
Acta Crystallogr. Sect. D
55
918-920
1999
Pseudoalteromonas carrageenovora
brenda
Potin, P.; Richard, C.; Barbeyron, T.; Henrissat, B.; Gey, C.; Petillot, Y.; Forest, E.; Dideberg, O.; Rochas, C.; Kloareg, B.
Processing and hydrolytic mechanism of the cgkA-encoded kappa-carrageenase of Alteromonas carrageenovora
Eur. J. Biochem.
228
971-975
1995
Pseudoalteromonas carrageenovora
brenda
Potin, P.; Sanseau, A.; le Gall, Y.; Rochas, C.; Kloareg, B.
Purification and characterization of a new kappa-carrageenase from a marine Cytophaga-like bacterium
Eur. J. Biochem.
201
241-247
1991
Bacteria
brenda
Michel, G.; Chantalat, L.; Duee, E.; Barbeyron, T.; Henrissat, B.; Kloareg, B.; Dideberg, O.
The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases
Structure
9
513-525
2001
Pseudoalteromonas carrageenovora
brenda
Helbert, W.; Nyvall-Collen, P.; Michel, G.; Czjzek, M.
Mircoscopic and molecular insights into heterogenous phase degradation of agars and carrageenans by marine bacterial galactanases
Macromol. Symp.
231
11-15
2006
Pseudoalteromonas carrageenovora
-
brenda
Guibet, M.; Boulenguer, P.; Mazoyer, J.; Kervarec, N.; Antonopoulos, A.; Lafosse, M.; Helbert, W.
Composition and distribution of carrabiose moieties in hybrid kappa-/iota-carrageenans using carrageenases
Biomacromolecules
9
408-415
2008
Pseudoalteromonas carrageenovora
brenda
Khambhaty, Y.; Mody, K.; Jha, B.
Purification and characterization of k-carrageenase from a novel gamma-proteobacterium, Pseudomonas elongata (MTCC 5261) syn. Microbulbifer elongatus comb. Nov
Biotechnol. Bioprocess Eng.
12
668-675
2007
Microbulbifer elongatus
-
brenda
Hu, X.; Jiang, X.; Aubree, E.; Boulenguer, P.; Critchley, A.T.
Preparation and in vivo antitumor activity of kappa-carrageenan oligosaccharides
Pharm. Biol.
44
646-650
2006
Cytophaga sp., Cytophaga sp. MCA-2
-
brenda
Lemoine, M.; Nyvall Collen, P.; Helbert, W.
Physical state of kappa-carrageenan modulates the mode of action of kappa-carrageenase from Pseudoalteromonas carrageenovora
Biochem. J.
419
545-553
2009
Pseudoalteromonas carrageenovora
brenda
Collen, P.N.; Lemoine, M.; Daniellou, R.; Guegan, J.P.; Paoletti, S.; Helbert, W.
Enzymatic degradation of kappa-carrageenan in aqueous solution
Biomacromolecules
10
1757-1767
2009
Pseudoalteromonas carrageenovora
brenda
Sun, F.; Ma, Y.; Wang, Y.; Liu, Q.
Purification and characterization of novel kappa-carrageenase from marine Tamlana sp. HC4
Chin. J. Oceanol. Limnol.
28
1139-1145
2010
Tamlana sp., Tamlana sp. HC4
-
brenda
Ma, Y.; Dong, S.; Jiang, X.; Li, J.; Mou, H.
PURIFICATION AND CHARACTERIZATION OF ?-CARRAGEENASE FROM MARINE BACTERIUM MUTANT STRAIN PSEUDOALTEROMONAS SP. AJ5-13 AND ITS DEGRADED PRODUCTS
J. Food Biochem.
34
661-678
2010
Pseudoalteromonas sp., Pseudoalteromonas sp. AJ5-1
brenda
Liu, G.; Li, Y.; Chi, Z.; Chi, Z.
Purification and characterization of kappa-carrageenase from the marine bacterium Pseudoalteromonas porphyrae for hydrolysis of kappa-carrageenan
Process Biochem.
46
265-271
2011
Pseudoalteromonas porphyrae, Pseudoalteromonas porphyrae LL1
-
brenda
Liu, Z.; Li, G.; Mo, Z.; Mou, H.
Molecular cloning, characterization, and heterologous expression of a new kappa-carrageenase gene from marine bacterium Zobellia sp. ZM-2
Appl. Microbiol. Biotechnol.
97
10057-10067
2013
Zobellia sp. M-2 (S5U3X4)
brenda
Kobayashi, T.; Uchimura, K.; Koide, O.; Deguchi, S.; Horikoshi, K.
Genetic and biochemical characterization of the Pseudoalteromonas tetraodonis alkaline kappa-carrageenase
Biosci. Biotechnol. Biochem.
76
506-511
2012
Pseudoalteromonas tetraodonis (E7FKF4), Pseudoalteromonas tetraodonis, Pseudoalteromonas tetraodonis JAM-K142 (E7FKF4), Pseudoalteromonas tetraodonis JAM-K142
brenda
Yao, Z.; Wang, F.; Gao, Z.; Jin, L.; Wu, H.
Characterization of a kappa-carrageenase from marine Cellulophaga lytica strain N5-2 and analysis of its degradation products
Int. J. Mol. Sci.
14
24592-24602
2013
Cellulophaga lytica, Cellulophaga lytica N5-2
brenda
Sun, Y.; Liu, Y.; Jiang, K.; Wang, C.; Wang, Z.; Huang, L.
Electrospray ionization mass spectrometric analysis of ?-carrageenan oligosaccharides obtained by degradation with kappa-carrageenase from Pedobacter hainanensis
J. Agric. Food Chem.
62
2398-2405
2014
Pedobacter hainanensis, Pedobacter hainanensis 13-Q
brenda
Liu, Z.; Tian, L.; Chen, Y.; Mou, H.
Efficient extracellular production of kappa-carrageenase in Escherichia coli: effects of wild-type signal sequence and process conditions on extracellular secretion
J. Biotechnol.
185
8-14
2014
Zobellia sp. M-2 (S5U3X4)
brenda
Kang, D.H.; Hyeon, J.E.; You, S.K.; Kim, S.W.; Han, S.O.
Efficient enzymatic degradation process for hydrolysis activity of the carrageenan from red algae in marine biomass
J. Biotechnol.
192
108-113
2014
Pseudoalteromonas carrageenovora (P43478)
brenda
Chauhan, P.S.; Saxena, A.
Bacterial carrageenases an overview of production and biotechnological applications
3 Biotech
6
146
2016
Pseudoalteromonas carrageenovora, Cellulosimicrobium cellulans, Microbulbifer elongatus, Kappaphycus alvarezii
brenda
Xiao, A.; Xu, C.; Lin, Y.; Ni, H.; Zhu, Y.; Cai, H.
Preparation and characterization of kappa-carrageenase immobilized onto magnetic iron oxide nanoparticles
Electron. J. Biotechnol.
19
1-7
2016
Pseudoalteromonas sp. ASY5
-
brenda
Yu, Y.; Liu, Z.; Yang, M.; Chen, M.; Wei, Z.; Shi, L.; Li, L.; Mou, H.
Characterization of full-length and truncated recombinant kappa-carrageenase expressed in Pichia pastoris
Front. Microbiol.
8
1544
2017
Zobellia sp. M-2 (S5U3X4)
brenda
Cui, H.; Peng, Y.; Zhao, B.; Liu, Y.; Chen, F.; Wu, H.; Yao, Z.
Cloning, identification and characterization of a novel kappa-carrageenase from marine bacterium Cellulophaga lytica strain N5-2
Int. J. Biol. Macromol.
105
509-515
2017
Cellulophaga lytica (A0A2I4KDZ0), Cellulophaga lytica N5-2 (A0A2I4KDZ0)
brenda
Zhu, B.; Ni, F.; Ning, L.; Yao, Z.; Du, Y.
Cloning and biochemical characterization of a novel kappa-carrageenase from newly isolated marine bacterium Pedobacter hainanensis NJ-02
Int. J. Biol. Macromol.
108
1331-1338
2018
Pedobacter hainanensis, Pedobacter hainanensis NJ-02
brenda
Shen, J.; Chang, Y.; Chen, F.; Dong, S.
Expression and characterization of a kappa-carrageenase from marine bacterium Wenyingzhuangia aestuarii OF219 A biotechnological tool for the depolymerization of kappa-carrageenan
Int. J. Biol. Macromol.
112
93-100
2018
Wenyingzhuangia aestuarii (A0A223FUT7), Wenyingzhuangia aestuarii, Wenyingzhuangia aestuarii OF219 (A0A223FUT7)
brenda
Matard-Mann, M.; Bernard, T.; Leroux, C.; Barbeyron, T.; Larocque, R.; Prechoux, A.; Jeudy, A.; Jam, M.; Nyvall Collen, P.; Michel, G.; Czjzek, M.
Structural insights into marine carbohydrate degradation by family GH16 kappa-carrageenases
J. Biol. Chem.
292
19919-19934
2017
Pseudoalteromonas carrageenovora (P43478), Pseudoalteromonas carrageenovora ATCC 43555T (P43478), Zobellia galactanivorans (G0L921), Zobellia galactanivorans DsijT (G0L921)
brenda
Zhu, B.; Ning, L.
Purification and characterization of a new kappa-carrageenase from the marine bacterium Vibrio sp. NJ-2
J. Microbiol. Biotechnol.
26
255-262
2016
Vibrio sp. NJ-2
brenda
Wang, L.; Li, S.; Zhang, S.; Li, J.; Yu, W.; Gong, Q.
A new kappa-carrageenase CgkS from marine bacterium Shewanella sp. Kz7
J. Ocean Univ. China
14
759-763
2015
Shewanella sp. Kz7 (W8V7X4)
-
brenda
Li, J.; Pan, A.; Xie, M.; Zhang, P.; Gu, X.
Characterization of a thermostable kappa-carrageenase from a hot spring bacterium and plant protection activity of the oligosaccharide enzymolysis product
J. Sci. Food Agric.
99
1812-1819
2019
Bacillus sp. HT19
brenda
Li, J.; Ni, H.; Cai, H.; Zhu, Y.; Xiao, A.
Cloning, expression, and enzymatic properties of kappa-carrageenase from Pseudoalteromonas carrageenovora
Mod. Food Sci. Technol.
32
72-77
2016
Pseudoalteromonas carrageenovora, Pseudoalteromonas carrageenovora ASY5
-
brenda
Guo, J.; Zhang, L.; Lu, X.; Zeng, S.; Zhang, Y.; Xu, H.; Zheng, B.
Medium optimization and fermentation kinetics for kappa-carrageenase production by Thalassospira sp. Fjfst-332
Molecules
21
E1479
2016
Thalassospira sp. Fjfst-332
brenda
Xu, C.; Lin, Y.; Ni, H.; Zhu, Y.; Cai, H.; Xiao, A.
Characterization of immobilized carrageenase on superparamagnetic nanoparticles for oligosaccharide preparation
Nanosci. Nanotechnol. Lett.
7
855-860
2015
Pseudoalteromonas carrageenovora, Pseudoalteromonas carrageenovora CICC 23819
-
brenda
Zhao, Y.; Chi, Z.; Xu, Y.; Shi, N.; Chi, Z.; Liu, G.
High-level extracellular expression of kappa-carrageenase in Brevibacillus choshinensis for the production of a series of kappa-carrageenan oligosaccharides
Process Biochem.
64
83-92
2018
Pseudoalteromonas porphyrae, Pseudoalteromonas porphyrae LL1
-
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.2.1.83)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
