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Enzyme Nomenclature
Information on EC 1.11.1.B6 - iodide peroxidase (vanadium-containing)
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.11.1.B6
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
iodide peroxidase (vanadium-containing)
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
?
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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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?
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
vanadate
-
essential for catalytic activity, iodoperoxidases PcI; essential for catalytic activity, iodoperoxidases PcII
Vanadium
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INHIBITORS
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
67000
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SUBUNITS
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
40
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1 h, stable, iodoperoxidases PcI; 1 h, stable, 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
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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
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50% v/v, 30 day incubation, about 70% loss of activity of isoenzyme Lh2
Methanol
-
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.11.1.B6)
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