Information on EC 3.2.1.83 - kappa-carrageenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.1.83
-
RECOMMENDED NAME
GeneOntology No.
kappa-carrageenase
-
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 in kappa-carrageenans
show the reaction diagram
endo or random mechanism
Pseudomonas carrageenovora
-
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans
show the reaction diagram
enzyme has an arginine residue at subsite -1, mechanism
-
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans
show the reaction diagram
enzyme acts in solution as a random hydrolase
-
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of O-glycosyl bond
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
kappa-carrageenan degradation
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carrageenase, kappa-
-
-
-
-
Cgk-K142
Pseudoalteromonas tetraodonis JAM-K142
-
-
CgkZ
Zobellia sp.
gene name
CgkZ
gene name
-
kappa-carrageenanase
-
-
-
-
kappa-carrageenase
-
-
kappa-carrageenase-like protein
-
kappa-carrageenase-like protein
Pseudoalteromonas tetraodonis JAM-K142
-
-
CAS REGISTRY NUMBER
COMMENTARY
37288-59-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Dsij, isolated from Delesseria sanguinea
-
-
Manually annotated by BRENDA team
Calcalispora hiemalis
-
-
-
Manually annotated by BRENDA team
isolated from the sediment of carrageenan production base in Hainan (Hainan, China)
-
-
Manually annotated by BRENDA team
Cellulophaga lytica N5-2
isolated from the sediment of carrageenan production base in Hainan (Hainan, China)
-
-
Manually annotated by BRENDA team
Culicidospora gravida
-
-
-
Manually annotated by BRENDA team
Cytophaga sp. 1k-C783
1k-C783
-
-
Manually annotated by BRENDA team
Cytophaga sp. MCA-2
-
-
-
Manually annotated by BRENDA team
Dactylella aquatica
-
-
-
Manually annotated by BRENDA team
Dendrospora erecta
-
-
-
Manually annotated by BRENDA team
Gyoerffyella speciosa
-
-
-
Manually annotated by BRENDA team
Heliscella stellata
-
-
-
Manually annotated by BRENDA team
Lateriramulosa uni-inflata
-
-
-
Manually annotated by BRENDA team
no activity in Tricladium angulatum
-
-
-
Manually annotated by BRENDA team
Pedobacter sp. 13-Q
isolated from seaside soil under the stacks of red algae in Hainan province of China
-
-
Manually annotated by BRENDA team
Pleuropedium tricladioides
-
-
-
Manually annotated by BRENDA team
Pseudoalteromonas porphyrae LL1
-
-
-
Manually annotated by BRENDA team
Pseudoalteromonas sp. AJ5-1
-
-
-
Manually annotated by BRENDA team
Pseudoalteromonas tetraodonis JAM-K142
-
UniProt
Manually annotated by BRENDA team
Pseudomonas carrageenovora
-
-
-
Manually annotated by BRENDA team
Pseudomonas carrageenovora
strain NCIMB 302 and strain 9
-
-
Manually annotated by BRENDA team
Pyramidospora densa
-
-
-
Manually annotated by BRENDA team
Taeniospora gracilis
-
-
-
Manually annotated by BRENDA team
Tamlana sp.
-
-
-
Manually annotated by BRENDA team
Tamlana sp. HC4
-
-
-
Manually annotated by BRENDA team
Tricellula aquatica
-
-
-
Manually annotated by BRENDA team
Zobellia sp.
i.e. strain ZM-2, gene cgkZ
UniProt
Manually annotated by BRENDA team
i.e. strain ZM-2, gene cgkZ
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Zobellia sp.
the enzyme belongs to the glycosyl hydrolase family 16, GH16
evolution
-
the enzyme belongs to the glycosyl hydrolase family 16, GH16; the enzyme belongs to the glycosyl hydrolase family 16, GH16
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
agar + H2O
?
show the reaction diagram
Pseudoalteromonas porphyrae, Pseudoalteromonas porphyrae LL1
-
1.5% activity compared to kappa-carrageenan
-
-
?
iota-carrageenan + H2O
?
show the reaction diagram
Pseudoalteromonas porphyrae, Pseudoalteromonas porphyrae LL1
-
1% activity compared to kappa-carrageenan
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
-
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
Zobellia sp.
-
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
Zobellia sp.
-
-
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
Pedobacter sp. 13-Q
-
-
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
the enzyme cleaves in an endo-fashion
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
-
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
-
-
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
Pseudoalteromonas tetraodonis JAM-K142
the enzyme cleaves in an endo-fashion
-
-
?
kappa-carrageen + H2O
carrageenan oligosaccharide
show the reaction diagram
Pedobacter sp. 13-Q
-
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-carrageenan + H2O
?
show the reaction diagram
-
-
-
-
?
kappa-carrageenan + H2O
?
show the reaction diagram
-
degradation
-
-
?
kappa-carrageenan + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
Cytophaga sp. MCA-2
-
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
kappa-neocarrabiose sulfate + D-galactose
show the reaction diagram
Tamlana sp., Tamlana sp. HC4
-
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
show the reaction diagram
Pseudoalteromonas sp., Pseudoalteromonas sp. AJ5-1
-
-
main end-products
?
kappa-carrageenan + H2O
tetrasaccharides
show the reaction diagram
Pseudoalteromonas porphyrae, Pseudoalteromonas porphyrae LL1
-
100% activity
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
?
show the reaction diagram
-
-
-
-
-
kappa-carrageen + H2O
kappa-neocarrahexaose-sulfate + kappa-neocarrabiose-sulfate + kappa-neocarrahexaose-sulfate
show the reaction diagram
Cellulophaga lytica, Cellulophaga lytica N5-2
-
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-carrageenan + H2O
additional information
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
Pseudomonas carrageenovora
-
-
-
?
kappa-carrageenan + H2O
additional information
-
Pseudomonas carrageenovora
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
Alatospora flagellata, Anguillospora crassa, Anguillospora longissima, Calcalispora hiemalis, Clavariopsis aquatica, Culicidospora gravida, Dactylella aquatica, Dendrospora erecta, Flagellospora penicillioides, Gyoerffyella gemellipara, Heliscella stellata, Neonectria lugdunensis, Lateriramulosa uni-inflata, Lemonniera centrosphaera, Lemonniera cornuta, Margaritispora aquatica, Pleuropedium tricladioides, Pyramidospora densa, Sigmoidea prolifera, Taeniospora gracilis, Tetrachaetum elegans, Tetracladium marchalianum, Tetracladium maxilliforme, Tetracladium setigerum, Tricellula aquatica, Varicosporium elodeae, Volucrispora graminea
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
?
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
?
kappa-carrageenan + H2O
additional information
-
-
-
kappa-neocarratetraose
?
kappa-carrageenan + H2O
additional information
-
Cytophaga sp. 1k-C783
-
-
-
?
kappa-carrageenan + H2O
additional information
-
Cytophaga sp. 1k-C783
-
-
-
?
kappa-carrageenan + H2O
additional information
-
Cytophaga sp. 1k-C783
-
-
-
?
lambda-carrageenan + H2O
?
show the reaction diagram
Pseudoalteromonas porphyrae, Pseudoalteromonas porphyrae LL1
-
39.3% activity compared to kappa-carrageenan
-
-
?
additional information
?
-
-
the enzyme also catalyzes transglycosylation
-
-
-
additional information
?
-
-
raffinose and p-nitrophenyl-alpha-D-galactopyranoside are not hydrolyzed
-
-
-
additional information
?
-
Pseudomonas carrageenovora
-
induction by kappa-carrageenan
-
-
-
additional information
?
-
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
-
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
?
-
-
isolated kappa-carrageenase can successfully generate protoplasts of Kappaphycus alvarezii. No activity with lambda-carrageenan, ioro-carrageenan and LMP agarose
-
-
-
additional information
?
-
Zobellia sp., Zobellia sp. M-2
the enzyme specifically cleaves the internal beta (1-4) linkages of carrageenans and yields a series of homologous even-numbered oligosaccharides
-
-
-
additional information
?
-
Cytophaga sp. 1k-C783
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
-
neocarrahexaitol + H2O
additional information
-
-
-
neocarrabiitol and beta-neocarratetraose are initially formed
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
kappa-carrageen + H2O
?
show the reaction diagram
Zobellia sp.
-
-
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
Pedobacter sp. 13-Q
-
-
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
E7FKF4
the enzyme cleaves in an endo-fashion
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
-
-
-
-
?
kappa-carrageen + H2O
?
show the reaction diagram
Pseudoalteromonas tetraodonis JAM-K142
E7FKF4
the enzyme cleaves in an endo-fashion
-
-
?
kappa-carrageenan + H2O
?
show the reaction diagram
-
degradation
-
-
?
additional information
?
-
Pseudomonas carrageenovora
-
induction by kappa-carrageenan
-
-
-
additional information
?
-
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
-
additional information
?
-
Zobellia sp., Zobellia sp. M-2
S5U3X4
the enzyme specifically cleaves the internal beta (1-4) linkages of carrageenans and yields a series of homologous even-numbered oligosaccharides
-
-
-
additional information
?
-
Cytophaga sp. 1k-C783
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
116.5% activity at 10 mM
Fe2+
-
105.9% activity at 10 mM
Na+
-
the activity is optimum in the presence of 50 mM NaCl
Na+
Zobellia sp.
-
activates, best at 100 mM
NaCl
-
optimal activity at 150 mM
Mg2+
-
119% activity at 10 mM
additional information
Zobellia sp.
-
poor effects by Li+, Mg2+, NH4+, Ca2+ and K+ at 5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
63.3% residual activity at 5 mM
AgNO3
-
1 mM, complete inhibition
AlCl3
-
1 mM, 39.7% inhibition
Ba2+
Tamlana sp.
-
53.25% residual activity at 1 mM
Ba2+
Zobellia sp.
-
-
BaCl2
-
1 mM, 26.8% inhibition
Ca2+
Tamlana sp.
-
70.84% residual activity at 1 mM
Ca2+
-
96.9% residual activity at 10 mM
CaCl2
-
1 mM, 50.7% inhibition
Co2+
-
almost complete inhibition at 1 mM
Co2+
-
13.2% residual activity at 10 mM
Cu2+
Tamlana sp.
-
9.67% residual activity at 1 mM
Cu2+
-
almost complete inhibition at 1 mM
Cu2+
-
48.3% residual activity at 10 mM
Cu2+
Zobellia sp.
-
-
CuSO4
-
1 mM, 31.3% inhibition
EDTA
Tamlana sp.
-
56.26% residual activity at 1 mM
EDTA
-
26% inhibition at 1 mM
EDTA
-
50.4% residual activity at 5 mM
EDTA
Zobellia sp.
-
-
EGTA
-
51.4% residual activity at 5 mM
Fe3+
Tamlana sp.
-
24.09% residual activity at 1 mM
Fe3+
-
11.4% residual activity at 10 mM
FeCl3
-
1 mM, 36.5% inhibition
Hg2+
-
3% residual activity at 10 mM
HgCl2
-
1 mM, complete inhibition
HgCl2
-
1 mM, 40.9% inhibition
iodoacetic acid
-
79.7% residual activity at 5 mM
K+
Tamlana sp.
-
49.13% residual activity at 1 mM
K+
-
96% residual activity at 10 mM
KCl
-
1 mM, 27.4% inhibition
KCl
-
1 mM, 38% inhibition
Li+
-
83.1% residual activity at 10 mM
Mg2+
Tamlana sp.
-
65.93% residual activity at 1 mM
MgCl2
-
1 mM, 15.4% inhibition
MgCl2
-
1 mM, 52.9% inhibition
Mn2+
Tamlana sp.
-
76.39% residual activity at 1 mM
Mn2+
-
2.5% residual activity at 10 mM
Mn2+
Zobellia sp.
-
-
MnCl2
-
1 mM, 15.4% inhibition
Na+
Tamlana sp.
-
85.13%, 84.95% and 46.77% residual activity at 10, 100 and 200 mM, respectively
Na+
-
the activity is inhibited by more than 50 mM NaCl
Na+
-
90.5% residual activity at 10 mM
NaCl
-
1.5% or above, complete inhibition
NaCl
-
above 150 mM
NaI
-
strong inhibition at 200 mM, inhibition is caused by iodide binding
Ni2+
-
9.7% residual activity at 10 mM
Pb2+
Zobellia sp.
-
-
phenylmethylsulfonyl fluoride
-
58.6% residual activity at 5 mM
SDS
-
81% inhibition at 1 mM
SDS
-
22.6% residual activity at 5 mM
SDS
Zobellia sp.
-
-
Tris
-
strong inhibition at 200 mM
Zn2+
Tamlana sp.
-
16.17% residual activity at 1 mM
Zn2+
-
almost complete inhibition at 1 mM
Zn2+
-
47.3% residual activity at 10 mM
ZnCl2
-
1 mM, 50% inhibition
MnCl2
-
1 mM, 36% inhibition
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
Zobellia sp.
-
-
Triton X-100
Zobellia sp.
-
-
Tween 80
Zobellia sp.
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
kappa-carrageen
Zobellia sp.
-
pH 6.0, 39C, recombinant enzyme
-
0.244
kappa-carrageenan
-
-
-
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 35C and pH 7.0
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
ZnCl2
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0774
Tamlana sp.
-
cell-free culture supernatant, in 25 mM Tris-HCl (pH 8.0) at 30C
6
-
measurement of production of reducing sugar
6.192
Tamlana sp.
-
after 80.38fold purification, in 25 mM Tris-HCl (pH 8.0) at 30C
8.16
purified recombinant enzyme, pH 6.0, 50C
19.8
-
crude enzyme, at pH 8.0, 55C
61
-
cell-free culture supernatant, in 25 mM Tris-HCl (pH 8.0) at 32C
700.5
Pedobacter sp. 13-Q
-
purified enzyme, pH 7.0, 40C
1170
-
purified enzyme, pH 7.0, 35C
4040
-
after 202.6fold purification, at pH 8.0, 55C
5778
-
after 95fold purification, in 25 mM Tris-HCl (pH 8.0) at 32C
additional information
Pseudomonas carrageenovora
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
-
and a second optimum at pH 7.7
6
Zobellia sp.
-
-
6
Zobellia sp.
-
assay at
7
-
in MOPS buffer
7
Pedobacter sp. 13-Q
-
-
7.2
-
in Tris buffer
7.5
Pseudomonas carrageenovora
-
-
7.7
-
and a second optimum at pH 5.6
8
Pseudomonas carrageenovora
-
15 min assay
8
Tamlana sp.
-
-
8
recombinant enzyme, at 50C
8.8
recombinant enzyme, at 30C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9.5
Zobellia sp.
-
activity range
4.8 - 9
-
pH 4.8: about 70% of maximal activity, pH 9.0: about 60% of maximal activity
5 - 8
-
pH 5.0: about 50% of maximal activity, pH 8.0: about 75% of maximal activity
5 - 8
-
activity range
5 - 9
-
broad range of activity
6 - 10
Pseudomonas carrageenovora
-
about 45% of maximal activity
7.4 - 8.4
-
about 60% of maximal activity at pH 7.4 and at pH 8.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at room temperature
25 - 50
-
-
30
Tamlana sp.
-
-
39
Zobellia sp.
-
-
40
Pseudomonas carrageenovora
-
15 min assay
40
Pedobacter sp. 13-Q
-
-
55
recombinant enzyme, pH 8.0
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 45
-
15C: about 40% of maximal activity, 45C: about 50% of maximal activity
20 - 60
Pseudomonas carrageenovora
-
20C: about 60% of maximal activity, 60C: about 25% of maximal activity, 15 min assay
20 - 60
-
activity range
25 - 60
Tamlana sp.
-
-
30 - 55
Zobellia sp.
-
high activity within this range
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
sequence calculation
8.5
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Pseudomonas carrageenovora
-
-
Manually annotated by BRENDA team
-
synthesized and released from resting cells and growing cells
Manually annotated by BRENDA team
Cytophaga sp. 1k-C783
-
synthesized and released from resting cells and growing cells
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Pseudomonas carrageenovora
-
-
-
Manually annotated by BRENDA team
Zobellia sp.
-
the enzyme contains a signal peptide
-
Manually annotated by BRENDA team
the enzyme contains an N-terminal 28-amino acid signal peptide
-
Manually annotated by BRENDA team
Zobellia sp.
-
the enzyme contains a 28-amino acid signal peptide
-
Manually annotated by BRENDA team
Cytophaga sp. 1k-C783
-
-
-
-
Manually annotated by BRENDA team
Pseudoalteromonas tetraodonis JAM-K142
-
the enzyme contains an N-terminal 28-amino acid signal peptide
-
-
Manually annotated by BRENDA team
-
the enzyme contains a 28-amino acid signal peptide; the enzyme contains a signal peptide
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32940
-
electrospray mass spectrometry
208835
85000
recombinant enzyme, gel filtration
731501
128000
-
gel filtrration
678856
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Pseudomonas carrageenovora
-
x * 35000, SDS-PAGE
?
-
x * 100000, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
Tamlana sp.
-
x * 66400, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
Zobellia sp.
-
x * 37300, recombinant His-tagged extracellular and intracellular enzyme, SDS-PAGE
?
-
x * 40800, SDS-PAGE
?
Pedobacter sp. 13-Q
-
x * 55000, SDS-PAGE
?
x * 45000, catalytic domain of kappa-carrageenase CgkA, SDS-PAGE
?
Cellulophaga lytica N5-2
-
x * 40800, SDS-PAGE
-
?
Cytophaga sp. 1k-C783
-
x * 100000, SDS-PAGE
-
?
Pseudoalteromonas porphyrae LL1
-
x * 40000, SDS-PAGE
-
?
Pseudoalteromonas sp. AJ5-1
-
x * 35000, SDS-PAGE
-
?
Tamlana sp. HC4
-
x * 66400, SDS-PAGE
-
?
-
x * 37300, recombinant His-tagged extracellular and intracellular enzyme, SDS-PAGE
-
homodimer
2 * 41809, sequence calculation
homodimer
Pseudoalteromonas tetraodonis JAM-K142
-
2 * 41809, sequence calculation
-
monomer
-
1 * 128000, SDS-PAGE
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme expressed in Escherichia coli
-
seleno-methionyl derivative of protein
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
1 h, about 65% loss of activity
208838
4.5
-
1 h, about 40% loss of activity
208838
5
Zobellia sp.
-
purified recombinant enzyme, 20C, 2 h, 65% activity remaining
731197
6
-
1 h, about 30% loss of activity
208838
6 - 8
Zobellia sp.
-
purified recombinant enzyme, 20C, 2 h, 85% activity remaining
731197
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 4C for 6 h, 100% of activity is maintained after treatment at pH 8.0 and 4C for 6 h
716808
6.6 - 8.6
-
-
715775
7
-
1 h, stable
208838
7.2 - 8.6
Tamlana sp.
-
the enzyme is stable over the range of pH 7.2-8.6 below 45C
714755
8.5
-
1 h, about 50% loss of activity
208838
9
-
1 h, about 75% loss of activity
208838
9
Zobellia sp.
-
purified recombinant enzyme, 20C, 2 h, 65% activity remaining
731197
10
Zobellia sp.
-
purified recombinant enzyme, 20C, 2 h, inactivation
731197
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 50
-
the purified kappa-carrageenase is stable in the range of 0-30C and the residual enzyme activity is still retained at 96.1% of the control after treatment at 30C for 1 h. The enzyme is inactivated rapidly at temperatures higher than 30C and is almost inactivated at 50C within 1 h
716808
5
Pseudomonas carrageenovora
-
stable for 2 weeks
208826
20
-
40% loss of activity within 5 days, complete loss of activity within 12 days
678856
28 - 75
-
the enzyme is stable at 28C, but 95% of the activity is lost at 50-75C for 30 min
715775
30
-
2 h, stable
208838
35
Zobellia sp.
-
purified recombinant enzyme, pH 6.0, 3 h, 95% activity remaining
731197
37
-
5 days, 50% loss of activity
678856
40
Pseudomonas carrageenovora
-
stable for 3.5 h
208826
40
-
stable for up to 1 h
208838
40
Zobellia sp.
-
purified recombinant enzyme, pH 6.0, 1 h, 50% activity remaining
731197
40
-
purified enzyme, pH 7.0, 2.5 h, stable at
731952
45
Zobellia sp.
-
purified recombinant enzyme, pH 6.0, 15 min, 20% activity remaining
731197
45 - 60
Tamlana sp.
-
enzyme activity is stable (more than 91%) for 2 h at temperatures of above 45C. However, 90% of the activity is lost after incubation at 50-60C for 30 min
714755
50
Pseudomonas carrageenovora
-
10 min, inactivated
208826
50
-
15 min, more than 70% loss of activity
208832
50
-
purified enzyme, pH 7.0, inactivation within 90 min
731952
55
-
10 min, complete inactivation
208832
60
-
purified enzyme, pH 7.0, inactivation within 60 min
731952
70
-
purified enzyme, pH 7.0, inactivation within 30 min
731952
additional information
no protective effect on enzyme thermal stability by Ca2+, Mg2+, agar, and NaCl
731501
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freezing and thawing drastically reduces activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 16 months
-
-20C, stable for several months
-
20C, 5 days, 40% loss of activity
-
frozen, stable for 15 days
-
4C, 0.2 M Tris-HCl buffer
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native extracellular enzyme to electrophoretic homogeneity from culture supernatant by ammonium sulfate fractionation, dialysis, and two different steps of gel filtration
-
native enzyme from culture supernatant by ammonium sulfate fractionation and adsorption chromatography
Pedobacter sp. 13-Q
-
by metal-affinity chromatography followed by cation exchange chromatography
-
recombinant CBM-tagged chimeric fusion enzyme cCgkA-cCglA by cellulose affinity purification using cellulose as a support or by nickel affinity chromatography
recombinant enzyme expressed in Escherichia coli
-
recombinant His-tagged enzyme from the periplasm of Escherichia coli strain BL21(DE3) by nickel affinity chromatography and cation exchange chromatography
-
DEAE Sepharose column chromatography and HiTrap column chromatography
-
ammonium sulfate precipitation, CM-cellulose 52 column chromatography, and Sephadex G-200 gel filtration
-
recombinant extracelluar enzyme 388.6fold from Escherichia coli strain DH5alpha by ammonium sulfate fractionation, dialysis, anion and cation exchange chromatography to homogeneity
-
Pseudomonas carrageenovora
-
ammonium sulfate precipitation, Sephadex G-200 gel filtration, and DE-cellulose 52 anion-exchange chromatography
Tamlana sp.
-
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
Zobellia sp.
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
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
His-tagged enzyme expression in the periplasm of Escherichia coli strain BL21(DE3)
-
overexpressed as a His-tagged fusion protein in Escherichia coli
-
DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain DH5alpha as extracellular enzyme
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
Zobellia sp.
-
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 23C 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
Zobellia sp.
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
Pseudomonas carrageenovora
-
studies of carrageenan structure
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
Pedobacter sp. 13-Q
-
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