Information on EC 1.11.1.B6 - iodide peroxidase (vanadium-containing)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.11.1.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
iodide peroxidase (vanadium-containing)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RH + I- + H2O2 + H+ = RI + 2 H2O
show the reaction diagram
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 hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
show the reaction diagram
I- + H2O2
triiodide
show the reaction diagram
I- + H2O2
triiodide + ?
show the reaction diagram
RH + I- + H2O2 + H+
RI + H2O
show the reaction diagram
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
vanadate
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essential for catalytic activity, iodoperoxidases PcI; essential for catalytic activity, iodoperoxidases PcII
Vanadium
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Br-
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competitive versus I-
I-
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; iodoperoxidases PcII
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 0.376
H2O2
1.3 - 4.3
I-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
462
I-
Laminaria digitata
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pH 6.2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 127
I-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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iodoperoxidases PcI
6.5
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iodoperoxidases PcII
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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isoenzyme Ls1
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
166000
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iodoperoxidases PcI, gel filtration
additional information
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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iodoperoxidases PcI and iodoperoxidase PcII differ in their binding to ConA-Sepharose, which implies a different glycosylation pattern
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
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
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 hide
LITERATURE
1-propanol
Acetone
Ethanol
Methanol
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
iodoperoxidases PcI; iodoperoxidases PcII
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