Ligand arsenite

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Basic Ligand Information

Molecular Structure
Picture of arsenite (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
H3AsO3
arsenite
GCPXMJHSNVMWNM-UHFFFAOYSA-N
Synonyms:
arsenic III oxide, arsenite[side 1], arsenite[side 2]


Show all pahtways known for Show all BRENDA pathways known for arsenite

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (16 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
show the reaction diagram
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In Vivo Product in Enzyme-catalyzed Reactions (22 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
arseno-mycothiol + mycoredoxin = arsenite + mycothiol-mycoredoxin disulfide
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arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O
show the reaction diagram
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Substrate in Enzyme-catalyzed Reactions (29 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]
show the reaction diagram
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Product in Enzyme-catalyzed Reactions (43 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
arsenate + GSH + NAD+ + glyceraldehyde 3-phosphate = arsenite + ?
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arsenate + glutathione = arsenite + reduced glutathione
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arseno-mycothiol + mycoredoxin = arsenite + mycothiol-mycoredoxin disulfide
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arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O
show the reaction diagram
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arsenate + azurin(red) = arsenite + H2O + azurin(ox)
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ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]
show the reaction diagram
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Activator in Enzyme-catalyzed Reactions (8 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
5 mM concentration slight activation
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treatment of worms with arsenite, a toxic ROS-producing compound, induces a robust phosphorylation of PMK-1, induction of oxidative stress-responsive genes, and eventual lethality. Activation of PMK-1 following arsenite treatment is dependent on SEK-1 but independent of NSY-1, differing from the NSY-1/SEK-1/PMK-1 cascade used during infection and osmotic stress
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Inhibitor in Enzyme-catalyzed Reactions (96 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
weak
-
slight inhibition
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47% residual activity at 1 mM arsenite at pH 9.5, 28% residual activity at 2 mM arsenite at pH 7.4
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probably bind the dithiol group in the lipoic acid
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5 mM, 50% inhibition after min
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pH 7.5, 37°C
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slight inhibition
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low inhibition
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+ NADPH, slightly
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strong inhibition
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the enzyme activity is completely inhibited by elevated concentrations of the substrate arsenite (0.2 mM)
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strong inhibition
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1 mM, 42% inhibition
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45% inhibition at 5 mM, 98% inhibition at 20 mM
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specific for vicinal sulfhydryl sites in proteins, irreversible or very slow reversible, instead of other inhibition with arsenite which is usually rapidly reversed upon addition of competitive dithiol compounds
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in presence of CoA, residual activity 25%
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inhibition of IKKbeta
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weak inhibitor with RNA core as substrate
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together with NADH
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1 mM
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i.e. arsenic trioxide, inhibits CatB in glioblastoma cells, 20% inhibition at 0.022 mM, 50% at 0.020 mM
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3D Structure of Enzyme-Ligand-Complex (PDB) (11 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (3 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
30.4
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pH 5.5, calculated with an Mr of 309000 Da

KM Value (32 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.1
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Ki Value (4 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.5
-
pH 7.5, 37°C
0.08
0.12
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References & Links

Links to other databases for arsenite

ChEBI
PubChem
ChEBI
PubChem