Ligand I-

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Basic Ligand Information

Molecular Structure
Picture of I- (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
HI
I-
XMBWDFGMSWQBCA-UHFFFAOYSA-M
Synonyms:
HI, Iodide

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
I- + H2O2 + H+ = HOI + H2O
show the reaction diagram
-
I- + H2O2 = ?
show the reaction diagram
-
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+ = L-thyroxine + reduced acceptor
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (24 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
monoiodoacetate + H2O = glycolate + HI
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (162 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
iodide + O2 = ?
show the reaction diagram
-
iodide + H2O2 = ?
show the reaction diagram
-
I- + H2O2 + H+ = HOI + H2O
show the reaction diagram
-
I- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione = ?
show the reaction diagram
-
iodide + NADPH + O2 = ?
show the reaction diagram
-
3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
show the reaction diagram
-
S-adenosyl-L-methionine + iodide = S-adenosyl-L-homocysteine + methyl iodide
show the reaction diagram
-
S-adenosyl-L-methionine + iodide = S-adenosyl-L-homocysteine + iodomethane
show the reaction diagram
-
S-adenosyl-L-methionine + iodide = 5'-deoxy-5'-iodoadenosine + L-methionine
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (144 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
3-iodo-L-tyrosine + H2O2 = 3-iodo-5-hydroxyl-L-tyrosine + L-dopa + I-
show the reaction diagram
-
-
2-iodobenzoate + NADH + O2 = catechol + iodide + NAD+ + CO2
show the reaction diagram
-
o-iodophenol + NADH + O2 = catechol + iodide + NAD+
show the reaction diagram
-
triiodophenol + NADPH + O2 = diiodohydroquinone + iodide + NADP+ + H2O
show the reaction diagram
-
tetraiodoethene + reduced acceptor = triiodoethene + iodide + acceptor
show the reaction diagram
-
-
CH3I + CO + HS-CoA = CH3-CO-S-CoA + HI
show the reaction diagram
-
5-deoxy-5'-iodoadenosine + fluoride = 5-deoxy-5'-fluoroadenosine + iodide
show the reaction diagram
-
-
5-deoxy-5'-iodoadenosine + fluoride = 5-deoxy-5'-fluoroadenosine + iodide
show the reaction diagram
-
-
6-iodopurine + H2O = hypoxanthine + HI
show the reaction diagram
-
monoiodoacetate + H2O = glycolate + HI
show the reaction diagram
-
-
monoiodoacetate + H2O = glycolate + HI
show the reaction diagram
-
-
4-iodobenzoate + H2O = 4-hydroxybenzoate + I-
show the reaction diagram
-
4-iodobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + iodide
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (10 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
form 1, AE-I, activates below pH 6.0
0.35 M, maximal stimulation
-
stimulation at low concentrations, inhibition above 100 mM
-
stimulates alanine transamination, inhibits lysine transamination
-
activates hydrolysis of 3'-nucleotides and di-p-dinitrophenyl phosphate
-
lower affinity for the enzyme than chloride and higher relative activity
-
activates

Inhibitor in Enzyme-catalyzed Reactions (104 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
100 mM
-
above 0.1 mM at pH 5, no inhibition at pH 7
-
iodoperoxidases PcII
-
62% inactivation at 0.1 M
-
50% inhibition at 0.05 M
-
uncompetitive inhibitor with respect to the substrate amine and noncompetitive inhibitor with respect to dissolved oxygen
-
competitive vs cytochrome b5, reversible by dilution
above 25 mM
-
inhibition above 100 mM, stimulation below
-
87.91% residual activity at 5 mM
-
stimulates alanine transamination, inhibits lysine transamination
-
high concentration
-
lower inhibition than ClO4-, same inhibition as Br-, the kind of cation has no inhibitory effect
-
slight inhibition
-
competitive
-
100-200 mM
-
5 mM, complete inhibition
-
1 mM, 27% inhibition
-
noncompetitive
-
0.06 M, 50% inhibition
-
0.5 M, 50% inhibition of ATP-diphosphate exchange
-

Metals and Ions (14 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
stimulates luminescence activity
-
stimulates
-
retards the oxidative half-reaction
-
activates
-
40% activation at 5 mM
-
absolute requirement for halide ions, the efficacy in decreasing order: Cl-, Br-, I-, F-
-
2 mM, activation
-
enhances activity
stimulation by anions with the following decreasing order of effectiveness: SCN-, I-, NO3-, Br-, Cl-, membrane-associated enzyme
-

3D Structure of Enzyme-Ligand-Complex (PDB) (1382 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (3 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
75
-
in phosphate buffer (100 mM, pH 8.0), at 20°C
462
-
pH 6.2
0.005
-
in 50 mM phosphate buffer (pH 7.9) at 37°C

KM Value (35 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.66
-
-
2.5
-
-
4.47
-
in 20 mM MES (pH 7.0), at 30°C
260
-
in 50 mM phosphate buffer (pH 7.9) at 37°C

Ki Value (21 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
9.7
-
-
0.06
-
-

IC50 Value (5 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
200
-
pH 8.5, 22°C

References & Links