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Information on EC 1.11.1.B6 - iodide peroxidase (vanadium-containing) for references in articles please use BRENDA:EC1.11.1.B6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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1.11.1.B6
preliminary BRENDA-supplied EC number
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iodide peroxidase (vanadium-containing)
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RH + I- + H2O2 + H+ = RI + 2 H2O
Brings about the iodination of a range of organic molecules, forming stable C-I bonds. The enzymes of this group contain vanadium (V) bound to the active centre.
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iodide:hydrogen-peroxide oxidoreductase (vanadium-containing)
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vanadium-dependent iodoperoxidase
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zobellia_1262
gene name
zobellia_1262
gene name
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brenda
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brenda
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brenda
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brenda
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UniProt
brenda
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UniProt
brenda
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Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
RH + I- + H2O2 + H+
RI + H2O
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-
?
thymol blue + 2 I- + 2 H+ + H2O2
diiodothymol blue + 2 H2O
additional information
?
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Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone. Isoenzyme Lh2 shows 5% of the activity with iodide + H2O2, isoenzyme Lh1 is inactive
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone, about 5% of the iodoperoxidase activity, iodoperoxidase PcI
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone, about 5% of the iodoperoxidase activity, iodoperoxidase PcII
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?
I- + H2O2
triiodide
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iodoperoxidase PcI show mainly iodoperoxidase activity, the specific activity of iodoperoxidase I is half of that of iodoperoxidase II
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?
I- + H2O2
triiodide
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iodoperoxidase PcII shows mainly iodoperoxidase activity, the specific activity of iodoperoxidase I is half of that of iodoperoxidase II
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?
I- + H2O2
triiodide + ?
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?
I- + H2O2
triiodide + ?
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?
thymol blue + 2 I- + 2 H+ + H2O2
diiodothymol blue + 2 H2O
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?
thymol blue + 2 I- + 2 H+ + H2O2
diiodothymol blue + 2 H2O
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?
additional information
?
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the enzyme does not catalyze monochlorodimedone bromination
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additional information
?
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no monochlorodimedonebromination activity
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additional information
?
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enzyme shows strict specificity for iodide oxidation
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additional information
?
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enzyme shows strict specificity for iodide oxidation
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vanadate
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essential for catalytic activity, iodoperoxidases PcI; essential for catalytic activity, iodoperoxidases PcII
Vanadium
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the enzyme contains vanadium
Vanadium
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enzyme contains vanadium
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Br-
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competitive versus I-
I-
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; iodoperoxidases PcII
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0.11
H2O2
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iodoperoxidases PcI
0.12
H2O2
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pH 6.7, isoenzyme Ls1
0.137
H2O2
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pH 6.7, isoenzyme Ls2
0.166
H2O2
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pH 6.7, isoenzyme Lh1
0.173
H2O2
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pH 6.7, isoenzyme Lh2
0.2
H2O2
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iodoperoxidases PcII
0.217
H2O2
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pH 6.1, isoenzyme Lh2
0.243
H2O2
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pH 6.1, isoenzyme Ls1
0.273
H2O2
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pH 6.1, isoenzyme Ls2
0.275
H2O2
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pH 6.1, isoenzyme Lh1
0.285
H2O2
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pH 5.5, isoenzyme Lh2
0.333
H2O2
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pH 5.5, isoenzyme Ls2
0.334
H2O2
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pH 5.5, isoenzyme Lh1
0.376
H2O2
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pH 5.5, isoenzyme Ls1
1.3
I-
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pH 5.5, isoenzyme Ls1
1.9
I-
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pH 5.5, isoenzyme Lh1
1.9
I-
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pH 5.5, isoenzyme Ls2
2.1
I-
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iodoperoxidases PcI
2.3
I-
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pH 5.5, isoenzyme Lh2
2.4
I-
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iodoperoxidases PcII
2.7
I-
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pH 6.1, isoenzyme Ls2
3.4
I-
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pH 6.1, isoenzyme Lh1
3.4
I-
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pH 6.1, isoenzyme Ls1
3.5
I-
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pH 6.7, isoenzyme Lh1
3.7
I-
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pH 6.7, isoenzyme Ls1
3.8
I-
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pH 6.1, isoenzyme Lh2; pH 6.7, isoenzyme Lh2
4.3
I-
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pH 6.7, isoenzyme Ls2
0.02
thymol blue
mutant H360A, pH 7.2, 20°C
0.03
thymol blue
mutant D322Y, pH 7.2, 20°C
0.05
thymol blue
mutant H360S, pH 7.2, 20°C
0.19
thymol blue
mutant S358A, pH 7.2, 20°C
0.22
thymol blue
wild-type, pH 7.2, 20°C
0.39
thymol blue
mutant W321R, pH 7.2, 20°C
0.44
thymol blue
mutant Y263A, pH 7.2, 20°C
0.79
thymol blue
mutant Y263F, pH 7.2, 20°C
0.91
thymol blue
mutant C320S, pH 7.2, 20°C
1.38
thymol blue
mutant D322L, pH 7.2, 20°C
1.58
thymol blue
mutant Y263S, pH 7.2, 20°C
2.63
thymol blue
mutant F353H, pH 7.2, 20°C
3.45
thymol blue
mutant R410A, pH 7.2, 20°C
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0.0007 - 53.27
thymol blue
0.0007
thymol blue
mutant D322Y, pH 7.2, 20°C
0.002
thymol blue
mutant H360S, pH 7.2, 20°C
0.01
thymol blue
mutant H360A, pH 7.2, 20°C
0.03
thymol blue
mutant R410A, pH 7.2, 20°C
1.78
thymol blue
mutant W321R, pH 7.2, 20°C
1.98
thymol blue
wild-type, pH 7.2, 20°C
2.19
thymol blue
mutant S358A, pH 7.2, 20°C
2.67
thymol blue
mutant Y263F, pH 7.2, 20°C
2.76
thymol blue
mutant C320S, pH 7.2, 20°C
3.53
thymol blue
mutant Y263A, pH 7.2, 20°C
3.86
thymol blue
mutant D322L, pH 7.2, 20°C
13.97
thymol blue
mutant Y263S, pH 7.2, 20°C
53.27
thymol blue
mutant F353H, pH 7.2, 20°C
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0.01
thymol blue
mutant R410A, pH 7.2, 20°C
0.02
thymol blue
mutant D322Y, pH 7.2, 20°C
0.04
thymol blue
mutant H360S, pH 7.2, 20°C
0.5
thymol blue
mutant H360A, pH 7.2, 20°C
2.8
thymol blue
mutant D322L, pH 7.2, 20°C
3.03
thymol blue
mutant C320S, pH 7.2, 20°C
3.38
thymol blue
mutant Y263F, pH 7.2, 20°C
4.56
thymol blue
mutant W321R, pH 7.2, 20°C
8.02
thymol blue
mutant Y263A, pH 7.2, 20°C
8.84
thymol blue
mutant Y263S, pH 7.2, 20°C
9
thymol blue
wild-type, pH 7.2, 20°C
11.53
thymol blue
mutant S358A, pH 7.2, 20°C
20.25
thymol blue
mutant F353H, pH 7.2, 20°C
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0.06
I-
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iodoperoxidases PcII
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6.5
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iodoperoxidases PcII
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brenda
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65000
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x * 65000, SDS-PAGE
66000
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x * 66000, iodoperoxidases PcI, SDS-PAGE
166000
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iodoperoxidases PcI, gel filtration
additional information
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67000
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x * 67000, SDS-PAGE
67000
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x * 67000, SDS-PAGE
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additional information
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?
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x * 67000, SDS-PAGE
?
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x * 65000, SDS-PAGE; x * 67000, SDS-PAGE
?
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x * 66000, iodoperoxidases PcI, SDS-PAGE
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glycoprotein
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iodoperoxidases PcI and iodoperoxidase PcII differ in their binding to ConA-Sepharose, which implies a different glycosylation pattern
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to 1.8 A resolution, revealing a monomeric structure mainly folded into alpha-helices. The vanadate binding site is strictly conserved with the fungal VCPO active site. Specific amino acids and the associated hydrogen bonding network around the vanadate center are essential for the catalytic properties and also the iodide specificity
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40
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1 h, stable, iodoperoxidases PcI; 1 h, stable, iodoperoxidases PcII
50
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1 h, about 25% loss of activity, iodoperoxidases PcII
60
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1 h, about 50% loss of activity, iodoperoxidases PcII; 1 h, more than 90% loss of activity, iodoperoxidases PcI
70
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1 h, about 60% loss of activity, iodoperoxidase PcII; 1 h, complete inactivation, iodoperoxidases PcI
30 - 50
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stable
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by extensive dialysis with citrate-phosphate buffer in the presence of EDTA the enzyme is inactivated due to removal of the prosthetic group
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by extensive dialysis with citratephosphate buffer in the presence of EDTA the enzyme is inactivated due to removal of the prosthetic group
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iodoperoxidase PcI is inactivated by extensive diafiltration using a Centricon-30 (Amicon) device against 100 mM citrate/phosphate pH 3.8 buffer in the presence of 1 mM EDTA, followed by a second diafiltration with 50 mM Tris-HCl (pH 9.0), reactivation by vanadium, iodoperoxidase PcI
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iodoperoxidase PcII is inactivated by extensive diafiltration using a Centricon-30 (Amicon) device against 100 mM citrate/phosphate pH 3.8 buffer in the presence of 1 mM EDTA, followed by a second diafiltration with 50 mM Tris-HCl (pH 9.0), reactivation by vanadium, iodoperoxidase PcI
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1-propanol
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50% v/v, 30 day incubation, about 70% loss of activity of isoenzyme Lh2
1-propanol
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50% v/v, 30 day incubation, more than 95% loss of activity of isoenzyme Ls1, about 75% loss of activity of isoenzyme Ls2
Acetone
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50% v/v, 30 day incubation, about 80% loss of activity of isoenzyme Lh2
Acetone
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50% v/v, 30 day incubation, more than 90% loss of activity of isoenzyme Ls1 and Ls2
Ethanol
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50% v/v, 30 day incubation, about 90% loss of activity of isoenzyme Lh2
Ethanol
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50% v/v, 30 day incubation, more than 90% loss of activity of isoenzyme Ls1 and Ls2
Methanol
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50% v/v, 30 day incubation, about 70% loss of activity of isoenzyme Lh2
Methanol
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50% v/v, 30 day incubation, more than 90% loss of activity of isoenzyme Ls1 and Ls2
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iodoperoxidases PcI; iodoperoxidases PcII
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expression in Escherichia coli
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C320S
34% of wild-type activity
D322L
31% of wild-type activity
D322Y
0.3% of wild-type activity
F353H
225% of wild-type activity
H360A
6% of wild-type activity
H360S
0.4% of wild-type activity
R410A
0.1% of wild-type activity
S358A
128% of wild-type activity
W321R
51% of wild-type activity
Y263A
89% of wild-type activity
Y263F
38% of wild-type activity
Y263S
98% of wild-type activity
C320S
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34% of wild-type activity
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H360A
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6% of wild-type activity
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R410A
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0.1% of wild-type activity
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Y263A
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89% of wild-type activity
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Y263F
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38% of wild-type activity
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G0LAH5_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
450
50465
TrEMBL
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Colin, C.; Leblanc, C.; Michel, G.; Wagner, E.; Leize-Wagner, E.; van Dorsselaer, A.; Potin, P.
Vanadium-dependent iodoperoxidases in Laminaria digitata, a novel biochemical function diverging from brown algal bromoperoxidases
J. Biol. Inorg. Chem.
10
156-166
2005
Laminaria digitata
brenda
Almeida, M.G.; Humanes, M.; Melo, R.; Silva, J.A.; da Silva,J.J.; Wever, R.
Purification and characterisation of vanadium haloperoxidases from the brown alga Pelvetia canaliculata
Phytochemistry
54
5-11
2005
Pelvetia canaliculata
brenda
Almeida, M.; Filipe, S.; Humanes, M.; Maia, M.F.; Melo, R.; Severino, N.; da Silva, J.A.; Frausto da Silva, J.J.; Wever, R.
Vanadium haloperoxidases from brown algae of the Laminariaceae family
Phytochemistry
57
633-642
2001
Laminaria hyperborea, Laminaria ochroleuca
brenda
Fournier, J.B.; Rebuffet, E.; Delage, L.; Grijol, R.; Meslet-Cladiere, L.; Rzonca, J.; Potin, P.; Michel, G.; Czjzek, M.; Leblanc, C.
The vanadium iodoperoxidase from the marine flavobacteriaceae species Zobellia galactanivorans reveals novel molecular and evolutionary features of halide specificity in the vanadium haloperoxidase enzyme family
Appl. Environ. Microbiol.
80
7561-7573
2014
Zobellia galactanivorans (G0LAH5), Zobellia galactanivorans DSM 12802 (G0LAH5)
brenda
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