Ligand umbelliferone

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Basic Ligand Information

Molecular Structure
Picture of umbelliferone (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C9H6O3
umbelliferone
ORHBXUUXSCNDEV-UHFFFAOYSA-N
Synonyms:
7-hydroxycoumarin, hydrangin, umbelliferol

Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Substrate in Enzyme-catalyzed Reactions (16 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
7-hydroxycoumarin + [reduced NADPH-hemoprotein reductase] + O2 = ?
show the reaction diagram
-
UDP-glucose + umbelliferone = UDP + skimmin
show the reaction diagram
-
dTDP-L-noviose + 7-hydroxycoumarin = dTDP + ?
show the reaction diagram
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UDPglucose + umbelliferone = UDP + umbelliferyl beta-D-glucoside
show the reaction diagram
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UDP-alpha-D-glucose + 7-hydroxycoumarin = UDP + 2-oxo-2H-1-benzopyran-7-yl beta-D-glucopyranoside
show the reaction diagram
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UDP-alpha-D-glucose + 7-hydroxycoumarin = UDP + 7-[(beta-D-glucopyranosyl)oxy]-coumarin
show the reaction diagram
-
geranyl diphosphate + umbelliferone = diphosphate + 8-geranylumbelliferone
show the reaction diagram
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Product in Enzyme-catalyzed Reactions (12 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
7-methoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2 = umbelliferone + ? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
UDP-glucose + hydrangetin = UDP + hydrangin
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (18 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, almost complete inhibition
-
low competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview
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isolated from Angelica decursiva, forms three hydrogen bonds with the interacting residues Tyr121, Phe288, and Arg289. Residues Phe288 and Arg289 are involved in strong hydrogen bonding interactions with the hydroxyl group at position C-7, and Tyr121 is also involved in hydrogen bonding interactions with the ketone group at position C-2. In particular, important peripheral anionic site (PAS) residues, Trp279 and Tyr334, are involved in hydrogen bonding interactions with umbelliferone
-
0.78 mM, 50% inhibition
-
uncompetitive inhibitor
-
increases the negative cooperativity between the substrate binding sites
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3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

KM Value (10 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.55
-
-

Ki Value (6 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.00338
-
-
0.042
-
pH 7.5, 25°C

IC50 Value (8 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.42
-
in 0.067 M phosphoric acid buffer (pH 6.8), at 25°C
0.1055
-
pH 8.0, 22°C
0.09014
-
pH 8.0, 22°C
0.0026
0.0195
IC50 ketonase reaction 2.6 microM, pH 6.5, room temperatur, IC50 enolase reaction 19.5 microM, pH 6.2, room temperatur

References & Links

Links to other databases for umbelliferone

ChEBI
PubChem
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PubChem