Ligand molybdate

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Basic Ligand Information

Molecular Structure
Picture of molybdate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
MoO4
molybdate
MEFBJEMVZONFCJ-UHFFFAOYSA-N
Synonyms:
molybdate[side 2], MoO42-


Show all pahtways known for Show all BRENDA pathways known for molybdate

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
ATP + H2O + molybdate/out = ADP + phosphate + molybdate/in
show the reaction diagram
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In Vivo Product in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + molybdate-[molybdate-binding protein][side 1] = ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
show the reaction diagram
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Substrate in Enzyme-catalyzed Reactions (10 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
P1,P4-bis(5'-adenosyl) tetraphosphate + molybdate = ?
show the reaction diagram
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Product in Enzyme-catalyzed Reactions (3 results)

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

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
induces MoFe protein expression
-
induces enzyme expression activity
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Inhibitor in Enzyme-catalyzed Reactions (89 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
no activity
-
1 mM, strong inhibition
-
5 mM, more than 50% inhibition of glucan phosphorolysis
-
10 mM, complete inhibition
-
little effect
-
1 mM, 70% inhibition
-
12% inhibition at 2.5 mM
-
1 mM, about 15% inhibition
-
strong
-
about 60% residual activity at 10 mM
-
2.3% residual activity at 1 mM
-
slight inhibition at 1 mM
-
-
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partial
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Metals and Ions (5 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
strong induction
-
10-100 mM, stimulates
-
specific binding of tungstate or molybdate, involving residues Ser286, Thr320, Ser323, and Lys340, to the two oxyanion pockets at the shared interface of the enzyme subunits prevents ATPase activity and locks the enzyme in the inward-facing conformation, with the actives sites of the nucleotide-binding subunits separated. The allosteric effect prevents the transporter from switchuing between the inward-facing and outward-facing states, thus interfering with the access and release mechanism, overview
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3D Structure of Enzyme-Ligand-Complex (PDB) (59 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (4 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE

KM Value (17 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.45
-
P1,P4-bis(5'-adenosyl) tetraphosphate-phosphorolysis, pH 8.0, 25°C

Ki Value (17 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.003
-
25°C, pH 5.6
0.00348
-
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IC50 Value (1 result)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.03
-
IC50 is 0.03 mM

References & Links

Links to other databases for molybdate

ChEBI
PubChem
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PubChem