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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.B6preliminary BRENDA-supplied EC number
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1.11.1.B6 iodide peroxidase (vanadium-containing)Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
iodoperoxidases PcI, iodoperoxidases PcII, vanadium-dependent iodoperoxidase, vIPO, zobellia_1262, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
zobellia_1262
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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SYSTEMATIC NAME
IUBMB Comments
iodide:hydrogen-peroxide oxidoreductase (vanadium-containing)
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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
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
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
?
-
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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-
?
thymol blue + 2 I- + 2 H+ + H2O2
diiodothymol blue + 2 H2O
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-
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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
?
-
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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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
vanadate
Vanadium
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G0LAH5_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
450
0
50465
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
67000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
40
60
70
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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 citrate–phosphate 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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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1-propanol
Acetone
Ethanol
Methanol
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
-
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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