Ligand 3,4-Dihydroxyphenylacetate

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Basic Ligand Information

Molecular Structure
Picture of 3,4-Dihydroxyphenylacetate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C8H8O4
3,4-Dihydroxyphenylacetate
CFFZDZCDUFSOFZ-UHFFFAOYSA-N
Synonyms:
(3,4-dihydroxyphenyl)acetate, (3,4-dihydroxyphenyl)acetic acid, 3,4 dihydroxyphenylacetate, 3,4-dihydroxyphenyl acetate, 3,4-dihydroxyphenylacetic acid, 3,4-Dihydroxyphenyl acetic acid, Dihydroxyphenylacetate, dihydroxyphenylacetic acid, Homoprotocatechuate, Homoprotocatechuic acid
Pathway Source
Pathways
BRENDA
4-hydroxyphenylacetate degradation
KEGG
Alcoholism, Amphetamine addiction, Cocaine addiction, Degradation of aromatic compounds, Dopaminergic synapse more
MetaCyc
4-hydroxyphenylacetate degradation, aromatic biogenic amine degradation (bacteria), dopamine degradation


Show all pahtways known for Show all BRENDA pathways known for 3,4-Dihydroxyphenylacetate

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (15 results)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
3,4-dihydroxyphenylacetate + NAD(P)H + O2 = 2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
-
show the reaction diagram
homoprotocatechuic acid + S-adenosyl-L-methionine = ?
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show the reaction diagram
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?
-
show the reaction diagram
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?
-
show the reaction diagram
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?
-
show the reaction diagram
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?
-
show the reaction diagram
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?
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In Vivo Product in Enzyme-catalyzed Reactions (9 results)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O = 3,4-dihydroxyphenylacetic acid + NADH + H+
-
-
show the reaction diagram
3,4-dihydroxyphenylacetyl-CoA + H2O = 3,4-dihydroxyphenylacetate + CoA
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Substrate in Enzyme-catalyzed Reactions (48 results)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
3,4-dihydroxyphenylacetate + O2 = ? + H2O
-
show the reaction diagram
3,4-dihydroxyphenylacetic acid + H2O2 = ? + H2O
-
show the reaction diagram
3,4-dihydroxyphenylacetic acid + H2O2 = ? + H2O
-
show the reaction diagram
3,4-dihydroxyphenylacetate + O2 = ?
-
show the reaction diagram
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?
-
show the reaction diagram
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?
-
show the reaction diagram
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?
-
show the reaction diagram
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?
-
show the reaction diagram
(3,4-dihydroxyphenyl)acetate + H+ = 4-methylcatechol + CO2
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Product in Enzyme-catalyzed Reactions (24 results)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O = 3,4-dihydroxyphenylacetate + NADH + H+
-
-
show the reaction diagram
3,4-dihydroxyphenylacetyl-CoA + H2O = CoA + 3,4-dihydroxyphenylacetate
-
-
show the reaction diagram
3,4-dihydroxyphenylacetyl-CoA + H2O = 3,4-dihydroxyphenylacetate + CoA
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Inhibitor in Enzyme-catalyzed Reactions (22 results)

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COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
able to prevent the formation of the tubulin/aldose reductase complex and the activation of aldose reductase by tubulin
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0.75 mM, 50% inhibition, noncompetitive
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0.006 mM, 92% inhibition
1 mM, 48% inhibition, substrate analogue
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IC50: 0.3 mM
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competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
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66% inhibition at 4.5 mM
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88% inhibition with tyrosine at 3 mM and dihydroxyphenylacetic acid at 3 mM
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90% residual activity at 0.5 mM
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3D Structure of Enzyme-Ligand-Complex (PDB) (54 results)

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Enzyme Kinetic Parameters

kcat Value (Turnover Number) (27 results)

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COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
wild-type
10
-
pH 7.5, 4°C
3.2
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pH 7.5, 25°C, in presence of ascorbate
63.5
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pH 7.5, 25°C
62.4
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pH 7.5, 22°C
10
-
mutant H200F
0.12
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24°C, pH 7.5, wild-type enzyme
10
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24°C, pH 7.5, mutant enzyme H20N
3
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24°C, pH 7.5, mutant enzyme H200Q
4
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24°C, pH 7.5, mutant enzyme H200F
0.21
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24°C, pH 7.5, mutant enzyme H200E
0.9
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24°C, pH 7.5, mutant enzyme H200A
0.3
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23°C, pH 7.5, wild-type enzyme
4.6
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23°C, pH 7.5, mutant enzyme H200Q
3.6
-
23°C, pH 7.5, mutant enzyme H200N
2.67
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23°C, pH 7.5, mutant enzyme H200A
0.067
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recombinant enzyme, pH 7.2, 37°C
in 100 mM Tris-HCl, pH 7.5, 40 mM NaCl, 5 mM MgCl2, 5 mM (NH4)2SO4, 5 mM cysteine, 25 mM substrate, and 5 mM dithiothreitol, at 30°C

KM Value (48 results)

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COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
for Cucumis melo L. inodorus cv. Amarillo
6.66
-
for Cucumis melo L. cantalupensis cv. Charentais
7.18
-
-
2.9
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for Cucumis melo L. inodorus cv. Amarillo
5.05
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for Cucumis melo L. cantalupensis cv. Charentais
24
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25°C, pH 5.5
21°C
0.0047
-
recombinant enzyme
0.011
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pH 7.5, 25°C, in presence of ascorbate
0.058
-
pH 7.5, 25°C
0.067
-
pH 7.5, 22°C
0.025
-
Mn-MndD
0.014
-
Mn-HPCD
0.035
-
Fe-MndD
0.015
-
Fe-HPCD
0.031
-
47°C
0.0074
-
38°C
0.0058
-
32°C
0.0034
-
28°C
0.004
-
24°C, pH 7.5, wild-type enzyme
0.03
-
24°C, pH 7.5, mutant enzyme H20N
0.01
-
24°C, pH 7.5, mutant enzyme H200Q
0.028
-
24°C, pH 7.5, mutant enzyme H200F
0.031
-
24°C, pH 7.5, mutant enzyme H200E
0.0004
-
24°C, pH 7.5, mutant enzyme H200A
0.005
-
23°C, pH 7.5, mutant enzyme H200A
0.012
-
23°C, pH 7.5, mutant enzyme H200E
0.017
-
23°C, pH 7.5, wild-type enzyme
0.021
-
23°C, pH 7.5, mutant enzyme H200Q
0.018
-
23°C, pH 7.5, mutant enzyme H200N
0.021
-
recombinant enzyme, pH 7.2, 37°C
-
0.64
-
pH 5.8, 37°C
0.01
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isoform Sult1d1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C
0.0209
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in 100 mM Tris-HCl, pH 7.5, 40 mM NaCl, 5 mM MgCl2, 5 mM (NH4)2SO4, 5 mM cysteine, 25 mM substrate, and 5 mM dithiothreitol, at 30°C
0.41
-
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0.5
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in 100 mM Tris-HCl, pH 7.5, 40 mM NaCl, 5 mM MgCl2, 5 mM (NH4)2SO4, 5 mM cysteine, 25 mM substrate, and 5 mM dithiothreitol, at 30°C
0.388
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Ki Value (5 results)

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COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE

IC50 Value (3 results)

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COMMENTARY
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
LITERATURE
IC50: 0.3 mM
0.3
-
pH 7.4, 37°C
0.019
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at pH 7.8 and 37°C
0.019
-

References & Links

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Links to other databases for 3,4-Dihydroxyphenylacetate

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ChEBI
PubChem
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PubChem