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BRENDA support

Ligand Fe3+

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Basic Ligand Information

Molecular Structure
Picture of Fe3+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Fe
Fe3+
VTLYFUHAOXGGBS-UHFFFAOYSA-N
Synonyms:
cytochrome c-550, cytochrome c550, Fe(III), Fe(III)[side 2], Fe3+[side 2]


Show all pahtways known for Show all BRENDA pathways known for Fe3+

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (6 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
alcohol + cytochrome c550 = aldehyde + reduced cytochrome c550
show the reaction diagram
-
NADH + Fe3+ = NAD+ + Fe2+
show the reaction diagram
-
ferrocytochrome c + Fe3+ = ferricytochrome c + Fe2+
show the reaction diagram
-
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (326 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
superoxide + Fe2+ = O2 + Fe3+
show the reaction diagram
-
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
show the reaction diagram
-
protoporphyrin IX + ascorbate + O2 = hematinic acid + a tripyrrole + Fe3+
show the reaction diagram
-
Fe(II) + rusticyanin = Fe(III) + reduced rusticyanin
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (25 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
alcohol + cytochrome c550 = aldehyde + reduced cytochrome c550
show the reaction diagram
-
cellobiose + Fe3+ = cellobiono-1,5-lactone + reduced Fe3+
show the reaction diagram
-
2 Fe3+ + 3 ferrozine + NADH = 2 Fe(II)-ferrozine + NAD+ + H+
show the reaction diagram
-
NADH + Fe3+ = NAD+ + Fe2+
show the reaction diagram
-
methylamine + H2O + cytochrome c-550 = formaldehyde + NH3 + reduced cytochrome c-550
show the reaction diagram
-
ferrocytochrome c + Fe3+ = ferricytochrome c + Fe2+
show the reaction diagram
-
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (401 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
superoxide + Fe2+ = O2 + Fe3+
show the reaction diagram
-
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
show the reaction diagram
-
protoporphyrin IX + ascorbate + O2 = hematinic acid + a tripyrrole + Fe3+
show the reaction diagram
-
2 Fe(II) + NADP+ + H+ = 2 Fe(III) + NADPH
show the reaction diagram
-
Fe2+ + O2 + H+ = Fe3+ + H2O
show the reaction diagram
-
[protein]-N6-(octanoyl)-L-lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = [protein]-N6-[(R)-dihydrolipoyl]-L-lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [2Fe-2S] ferredoxin
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-

Enzyme Cofactor/Cosubstrate (2 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (53 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
pMMO, optimal at 5.0 mM
-
0.5 microM Fe(III)-citrate and 0.5 microM Fe(III)-EDTA induces Fprs
-
strong activation
-
10 mM, 115% of initial activity
-
stimulates galactosaminidase activitiy of form I
-
strong activation
-

Inhibitor in Enzyme-catalyzed Reactions (1474 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM inhibits entirely
-
1 mM, 74% residual activity
-
11% inhibition at 1 nM
-
0-15% inactivation at 1 mM
-
complete inhibition at 1 mM
-
complete inhibition at 1 mM
-
0.5 mM, strong inhibition
-
1 mM, 73% residual activity
-
1 mM, 2% of initial activity with substrate diacetyl, 3.5% with substrate 2,3-butanediol, respectively
-
strong inhibition at 0.5 mM
-
1 mM, 47.3% loss of activity. 5 mM, 95.2% loss of activity
-
complete inhibition at 5 mM
-
27.2% residual activity at 5 mM
-
strong inhibition
-
15% inhibition at 1 mM
-
1 mM, 30% residual activity
-
inhibits diacetyl and (3S/3R)-acetoin reduction
-
1 mM, 44% residual activity
-
0.5 mM, 68% of initial activity
-
10 mM, wild-type enzyme retains approximately 80% of its activity, mutant enzyme Y169C/A211C retains 50-60% activity
-
1 mM, 54% inhibition
-
complete inhibition at 10 mM
-
73% residual activity at 1 mM
-
1 mM, 91% inhibition
-
inhibits the enzyme at 1-10 mM
90% inhibition at 0.1 mM
-
95% inhibition at 0.1 mM
-
complete inhibition at 1 mM
-
inhibits the light emission by dinoflagellate luciferase
-
less than 10% activity at 1 mM
-
2 mM, 68% residual activity
-
1 mM, 56% inhibition
-
1 mM, moderate inhibition
-
inhibits the enzyme activity at 0.5 mM by about 50%
-
0.1 mM, 77% residual activity
-
slight effect, crude enzyme extract
-
3% residual activity at 1 mM
-
0.1 mM inhibits by 23%, 1 mM completely inhibits; complete inhibition at 1 mM
-
2 mM, 67% loss of activity
-
5 mM, 65% inhibition
-
83.5% inhibition at 1 mM
-
complete inhibition at 1 mM
-
1 mM causes complete inhibition
-
10 mM FeCl3, 80% inhibition
-
0.1 mM, 15% residual activity
-
10 mM concentration 35% inhibition
-
91% residual activity at 2 mM Fe3+
-
5 mM, 99% loss of activity
-
52.1% residual activity at 5 mM
-
10 mM, 85% inhibition of reductive amination
-
1 mM, no residual activity
-
0.5 mM, 8% inhibition at pH 8.9, no effect on activity at pH 7.8
-
about 42% residual activity at 1 mM
-
10.78% residual activity at 3 mM
-
2.85 mM, 26% inhibition of pyridoxamine 5'-phosphate oxidation, 50% inhibition of pyridoxine oxidation
-
slight inhibition
-
less potent inhibitor, effect cannot reversed by EDTA