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

for references in articles please use BRENDA:EC1.11.1.B6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


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

EC NUMBER
COMMENTARY hide
1.11.1.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
iodide peroxidase (vanadium-containing)
-
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.
-
-
-
SYSTEMATIC NAME
IUBMB Comments
iodide:hydrogen-peroxide oxidoreductase (vanadium-containing)
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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
-
-
-
-
?
thymol blue + 2 I- + 2 H+ + H2O2
diiodothymol blue + 2 H2O
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
vanadate
-
essential for catalytic activity, iodoperoxidases PcI; essential for catalytic activity, iodoperoxidases PcII
Vanadium
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Br-
-
competitive versus I-
I-
-
; iodoperoxidases PcII
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 0.376
H2O2
1.3 - 4.3
I-
0.02 - 3.45
thymol blue
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
462
I-
-
pH 6.2
0.0007 - 53.27
thymol blue
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 20.25
thymol blue
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 127
I-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
iodoperoxidases PcI
6.5
-
iodoperoxidases PcII
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
isoenzyme Ls1
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
-
x * 65000, SDS-PAGE
66000
-
x * 66000, iodoperoxidases PcI, SDS-PAGE
166000
-
iodoperoxidases PcI, gel filtration
additional information
-
-
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
iodoperoxidases PcI and iodoperoxidase PcII differ in their binding to ConA-Sepharose, which implies a different glycosylation pattern
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
40
-
1 h, stable, iodoperoxidases PcI; 1 h, stable, iodoperoxidases PcII
50
-
1 h, about 25% loss of activity, iodoperoxidases PcII
60
-
1 h, about 50% loss of activity, iodoperoxidases PcII; 1 h, more than 90% loss of activity, iodoperoxidases PcI
70
-
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
-
by extensive dialysis with citratephosphate buffer in the presence of EDTA the enzyme is inactivated due to removal of the prosthetic group
-
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
-
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
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-propanol
Acetone
Ethanol
Methanol
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
iodoperoxidases PcI; iodoperoxidases PcII
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
34% of wild-type activity
-
H360A
-
6% of wild-type activity
-
R410A
-
0.1% of wild-type activity
-
Y263A
-
89% of wild-type activity
-
Y263F
-
38% of wild-type activity
-