Ligand catechol

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Basic Ligand Information

Molecular Structure
Picture of catechol (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C6H6O2
catechol
YCIMNLLNPGFGHC-UHFFFAOYSA-N
Synonyms:
1,2-dihydroxybenzene, 2,3-catechol, 2-hydroxyphenol, a catechol, benzene-1,2-diol, brenzcatechin, Dihydroxybenzene, o-benzenediol, o-dihydroxybenzene, pyrocatechol


Show all pahtways known for Show all BRENDA pathways known for catechol

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (9 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
catechol + 1/2 O2 = 1,2-benzoquinone + H2O
-
show the reaction diagram
catechol + O2 = ?
-
show the reaction diagram
catechol + O2 = ?
-
show the reaction diagram
S-adenosyl-L-methionine + a catechol = ?
-
show the reaction diagram
catechol + CO2 = 2,3-dihydroxybenzoate
-

In Vivo Product in Enzyme-catalyzed Reactions (20 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
2-chlorobenzoate + NADH + O2 = catechol + chloride + NAD+ + CO2
-
-
show the reaction diagram
phenol + NADH + H+ + O2 = catechol + NAD+ + H2O
-
-
show the reaction diagram
2-nitrophenol + NADPH + H+ + O2 = catechol + NADP+ + H2O + nitrite
-
-
show the reaction diagram
phenol + FADH2 + O2 = catechol + FAD + H2O
-
-
show the reaction diagram
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+ = catechol + NAD(P)H
-
show the reaction diagram
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+ = catechol + CO2 + NADH
-
show the reaction diagram
carboxylic acid diol + NAD+ = catechol + NADH
-
-
show the reaction diagram
2,3-Dihydroxybenzoate = Catechol + CO2
-
-
show the reaction diagram
L-3-4 dihydroxyphenylalanine + H2O = catechol + pyruvate + NH3
-

Substrate in Enzyme-catalyzed Reactions (118 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
catechol + O2 = dibenzo[1,4]dioxin-2,3-dione + H2O
-
show the reaction diagram
catechol + O2 = o-benzoquinone + H2O2
-
show the reaction diagram
catechol + O2 = ?
-
show the reaction diagram
catechol + O2 = ?
-
show the reaction diagram
pyrocatechol + H2O2 = 1,2-benzoquinone + H2O
-
show the reaction diagram
catechol + H2O2 = ?
-
show the reaction diagram
catechol + H2O2 = ?
-
show the reaction diagram
catechol + H2O2 = 2-benzoquinone + H2O
-
show the reaction diagram
catechol + H2O2 + H+ = ?
-
show the reaction diagram
catechol + H2O2 = ? + H2O
-
show the reaction diagram
catechol + H2O2 = ? + H2O
-
show the reaction diagram
catechol + O2 = 2-hydroxy-6-oxohexa-2,4-dienoate
-
show the reaction diagram
catechol + O2 = 2-hydroxymuconic acid semialdehyde
-
show the reaction diagram
catechol + O2 = ?
-
show the reaction diagram
catechol + O2 = ?
-
show the reaction diagram
catechol + O2 = ?
-
show the reaction diagram
catechol + O2 + NAD(P)H + H2O = ?
-
show the reaction diagram
catechol + ? = ?
-
show the reaction diagram
catechol + O2 = ?
-
show the reaction diagram
catechol + O2 = ?
-
show the reaction diagram
NADPH + H+ + catechol = NADP+ + ?
-
show the reaction diagram
S-adenosyl-L-methionine + catechol = S-adenosyl-L-homocysteine + 2-methoxyphenol
-
show the reaction diagram
UDP-glucose + catechol = ?
-
show the reaction diagram
UDPglucose + catechol = UDP + 2-(beta-D-glucopyranosyloxy)phenol
-
show the reaction diagram
sucrose + catechol = D-fructose + catechol glucoside
-
show the reaction diagram
catechol + hesperidin = 2-hydroxyphenyl beta-D-rutinoside + hesperetin
-
show the reaction diagram
catechol + H2O = ?
-
show the reaction diagram
catechol + H2O = ?
-
show the reaction diagram
catechol + CO2 = 2,3-dihydroxybenzoate
-
show the reaction diagram
Catechol + CO2 = 3,4-Dihydroxybenzoate
-

Product in Enzyme-catalyzed Reactions (78 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
benzene dihydrodiol + NADP+ = catechol + NADPH
-
-
show the reaction diagram
phenol + H2O2 = hydroquinone + catechol + H2O
-
-
show the reaction diagram
phenol + NADH + O2 = catechol + hydroquinone + NAD+
-
-
show the reaction diagram
nitrobenzene + NADH + O2 = catechol + nitrite + NAD+
-
-
show the reaction diagram
phenol + NADH + H+ + O2 = catechol + NAD+ + H2O
-
-
show the reaction diagram
phenol + NADH + H+ + O2 = catechol + NAD+ + H2O
-
show the reaction diagram
phenol + ? = catechol + ?
-
-
show the reaction diagram
monophenol + O2 = catechol + H2O
-
-
show the reaction diagram
benzene cis-dihydrodiol + NAD+ = catechol + NADH + H+
-
-
show the reaction diagram
2-hydroxyphenyl sulfate + H2O = 2-hydroxyphenol + sulfate
-
show the reaction diagram
2,3-Dihydroxybenzoate = Catechol + CO2
-
-
show the reaction diagram
protocatechuic acid = catechol + CO2
-
show the reaction diagram
3,4-Dihydroxybenzoate = Catechol + CO2
-
-
show the reaction diagram
2,3-dihydroxybenzoate = 1,2-dihydroxybenzene + CO2
-

Activator in Enzyme-catalyzed Reactions (4 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (63 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
i.e. 1,2-butanediol, inactivation, enzyme regains activity after removal of alcohol
-
75% inhibition at 1 mM
-
field bean PPO obeys Michaelis-Menten kinetics and exhibits the phenomenon of inhibition by excess substrate for catechol, 4-methylcatechol and 4-tert-butylcatechol
-
catechol produces substrate inhibition above 16 mM
-
substrate inhibition at over 0.08 mM substrate concentration
wild-type enzyme: substrate inhibition. Mutant enzyme E286K: no substrate inhibition
-
suicide inhibition
-
45% inhibition at 1 mM
-
0.019 mM, 50% inhibition, uncompetitive
-
0-006 mM, 63% inhibition
IC50: 0.062 mM
-
mixed inhibition
-
0.2 mM, 93% inhibition; 0.2 mM, 93% inhibition
-
the activity of the enzyme is restored after removal of catechol and incubation with ascorbate and FeCl2
-
noncompetitive inhibition
-
the enzyme completely loses its activity towards 2-aminophenol after incubation with catechol for 100 s
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
-
substrate inhibition
-
0.033 mM, 50% inhibition
-
irreversible inactivation
-
enzyme-inhibitor interaction measurement by SPR
-
constituents from the formosan apple (Malus doumeri var. formosana), inhibition 78%, shows substantial cellular tyrosinase inhibitory activity at a concentration of 100 microM
-
constituents from the formosan apple (Malus doumeri var. formosana)
-
0.1 mM and 1 mM, 64% and 98% inhibition of benzaldehyde oxidation, respectively
-
tested at 1.0 mM, 14% inhibition
-
50% inhibition of overall enzyme reaction at 7.4 mM, 50% inhibition of ketoacyl reduction reaction at 21 mM
-
weak
-
89% inhibition
-
competitive
-
0.5 mM, 73% inhibition
-
0.5 mM, 8.5% inhibition
-
irreversibly inactivates the enzyme with a complex radical-based autocatalytic multistep mechanism
competitive
-
inhibits pyruvate formation from L-Tyr, mixed type
-
cleavage of Tyr
-
inhibition of isozyme hCA II
-
inhibition of isozyme hCA I
-
24% inhibition at 0.01 mM, 52% inhibition at 0.05 mM
-
noncompetetive inhibitor
-
and derivatives
-

3D Structure of Enzyme-Ligand-Complex (PDB) (76 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (112 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
pH 7.0
878
-
at pH 7.0 and 55°C
12
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
44.9
-
native wild-type enzyme, pH 5.0, 25°C
4.2
-
pH 3.0, 50°C
115.5
-
pH 3.8, 55°C
34.4
-
pH 4.5, 55°C
403
-
pH 5.0, 25°C
pH 5.0, temperature not specified in the publication
125
-
pH 7.0 37°C
0.042
-
pH 7.0, 25°C
pH 7.0, 30°C
46
-
pH 7.5, 37°C
0.0165
-
pH 9.0, 40°C
412.5
-
pH and temperature not specified in the publication
626
-
recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C
2.18
-
recombinant mutant enzyme MmPPOA-637, pH 5.0, 25°C
0.084
-
recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C
1.53
-
in 50 mM sodium phosphate, pH 7.0, 30°C
12
-
mutant E140G, pH 3.5, 25°C
164
-
mutant E140G/K176G, pH 3.5, 25°C
185.6
-
mutant E140G/P141G, pH 3.5, 25°C
105.6
-
mutant E140G/P141G/K176G, pH 3.5, 25°C
135.7
-
mutant E140G/W164S/K176G, pH 3.5, 25°C
164.8
-
mutant F142G, pH 3.5, 25°C
75
-
mutant K176D, pH 3.5, 25°C
94
-
mutant K176G, pH 3.5, 25°C
80
-
mutant K215G, pH 3.5, 25°C
85
-
mutant K215Q, pH 3.5, 25°C
81
-
mutant P141G, pH 3.5, 25°C
78
-
mutant P76G, pH 3.5, 25°C
99
-
mutant W164S, pH 3.5, 25°C
8
-
wild-type, pH 3.5, 25°C
185
-
wild type enzyme, at pH 3.0 and 22°C
24
-
25°C, pH 5.5
25°C
2
8
in 50 mM Tris/HCl, pH 7.2, 25°C
10.23
-
isoenzyme 1
54
-
isoenzyme 2
49
-
isoenzyme 3
45
-
isoenzyme A
48.7
-
isoenzyme B
31.3
-
mutant enzyme A72G, in100 mM Tris-HCl pH 8.5, temperature not specified in the publication
13.6
-
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
4.42
-
pH 8.0, 35°C, mutant A72G
13.56
-
pH 8.0, 35°C, mutant A72G/L69G
2.04
-
pH 8.0, 35°C, mutant A72P
14.72
-
pH 8.0, 35°C, mutant A72S
15.48
-
pH 8.0, 35°C, mutant L69A
4.81
-
pH 8.0, 35°C, wild-type enzyme
30.03
-
pH not specified in the publication, 25°C
wild type enzyme, in100 mM Tris-HCl pH 8.5, temperature not specified in the publication
24.2
-
25°C, pH 7.2, mutant enzyme E286K
34.7
-
25°C, pH 7.2, wild-type enzyme
31.3
-
H199N mutant enzyme, pH 7.5, 25°C
0.46
-
H246N mutant enzyme, pH 7.5, 25°C
1.6
-
hybrid enzyme, pH 7.5, 25°C
148
-
mutant T249A
1.3
-
mutant T249G
0.8
-
mutant T249S
7.5
-
native enzyme, pH 7.5, 25°C
pH 7.5, 25°C
1.3
-
pH 7.5, 60°C
7.8
-
pH and temperature not specified in the publication
360
-
strain 1YB2, pH 7.5, 25°C
38
-
strain 1YdBTEX2, pH 7.5, 25°C
128
-
wild type enzyme, pH 7.5, 25°C
200
-
wildtype
180
-
Y255F mutant enzyme, pH 7.5, 25°C
8.8
-
-
13.3
-
25°C
25°C, pH 7.5
60°C
50
-
in 50 mM Hepes (pH 7.5) at 25°C
32.5
-
pH 7.5, 30°C
pH 8.0, 20°C
6.7
-
pH 9.0, 40°C, recombinant enzyme
38
-
pH 6.8, 25°C, recombinant enzyme
1080
-
recombinant enzyme, pH 7.2, 37°C
pH 7.5, 25°C
9.67
-
30°C, pH not specified in the publication
0.141
-
pH 6.0, 40°C
0.78
-
recombinant enzyme, L-DOPA formation is measured from dicatechol, pyruvate, and ammonium, pH 8.5, 20°C
2.68
-

KM Value (248 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
at 22°C, pH not specified in the publication
1.15
-
at pH 7.0 and 37°C
23.52
-
at pH 7.5 and 25°C
0.213
-
in 20 mM Tris-HCl buffer at pH 7.1 and 28°C
6.3
-
isoenzyme A
6.6
-
isoenzyme B
4.2
-
isoenzyme C
7
-
isoenzyme D
36
-
isozyme PPO 1, in 0.2 M sodium phosphate buffer pH 7.0, 25°C
44
-
Km of pawpaw fruit PPO is comparable with the Km of PPO from other fruits
326.6
-
pH 4.5, 25°C
0.414
-
pH 5.0, 20°C
203.8
-
pH 5.0, 25°C
5.95
-
pH 5.8, 25°C, MES buffer
1.25
-
pH 5.8, 25°C, sodium phosphate buffer
0.87
-
pH 6.0, 25°C, MES buffer
0.68
-
pH 6.0, 40°C
53.8
-
pH 6.2, 25°C, sodium phosphate buffer
0.41
-
pH 6.5
1.2
-
pH 6.5, 25°C
pH 6.8, 25°C
36.6
-
pH 7.0
0.1
-
pH 7.0, 12°C, leaf enzyme
2.34
-
pH 7.0, 12°C, stem enzyme
2.64
-
pH 7.0, 50°C
8
-
pH 8.0, 25°C
1.62
-
pH 8.0, 40°C
3.48
-
SDS-activated hemocyanin
7.174
-
at pH 7.0 and 55°C
19
-
30°C, pH 3.0
1.72
-
40°C, pH 4.5
0.025
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
3.434
-
immobilized enzyme
0.147
-
immobilized enzyme in presence of 1-hydroxybenzotriazole
0.261
-
in 50 mM sodium malonate buffer, pH 4.5 at 37°C
0.23
-
in McIlvaine buffer (pH 4.0), at 30°C
8.06
-
native wild-type enzyme, pH 5.0, 25°C
0.011
-
pH 3.0, 50°C
0.881
-
pH 5.0, 25°C
pH 5.0, temperature not specified in the publication
4.08
-
pH 7.0 37°C
1.24
-
pH 7.0, 25°C
3.65
-
pH 7.0, 30°C
1.05
-
pH 7.5, 37°C
1.48
-
pH 9.0, 40°C
0.0773
-
pH and temperature not specified in the publication
0.529
-
recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C
0.018
-
recombinant mutant enzyme MmPPOA-637, pH 5.0, 25°C
1.478
-
recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C
0.022
-
in 50 mM sodium phosphate, pH 7.0, 30°C
19
-
mutant E140G, pH 3.5, 25°C
4.26
-
mutant E140G/K176G, pH 3.5, 25°C
2.63
-
mutant E140G/P141G, pH 3.5, 25°C
10.5
-
mutant E140G/P141G/K176G, pH 3.5, 25°C
4.72
-
mutant E140G/W164S/K176G, pH 3.5, 25°C
0.034
-
mutant F142G, pH 3.5, 25°C
5.15
-
mutant K176D, pH 3.5, 25°C
1.86
-
mutant K176G, pH 3.5, 25°C
3.68
-
mutant K215G, pH 3.5, 25°C
4.26
-
mutant K215Q, pH 3.5, 25°C
4.04
-
mutant P141G, pH 3.5, 25°C
5.11
-
mutant P76G, pH 3.5, 25°C
4.79
-
mutant W164S, pH 3.5, 25°C
7.76
-
wild-type, pH 3.5, 25°C
5.04
-
wild type enzyme, at pH 3.0 and 22°C
19
-
30°C, pH 5.0
18.2
-
in 50 mM sodium acetate buffer, at pH 5.5
125
-
25°C, pH 5.5
25°C
0.0093
-
at pH 7.0 and 30°C
0.01753
-
at pH 7.2 and 45°C
0.00185
-
at pH 7.5 and 30°C
0.0092
-
free enzyme
0.0075
-
free protein
0.002
-
immobilized enzyme
0.0015
-
immobilized protein
0.0166
-
in 50 mM Tris/HCl, pH 7.2, 25°C
0.003
-
IsoA
0.0028
-
IsoB
0.001
-
isoenzyme 2
0.002
-
isoenzymes 1 and 3
0.0019
-
mutant A72D
0.0691
-
mutant A72G
0.0093
-
mutant A72N
0.00235
-
mutant A72S
0.01
-
mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.0093
-
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.00576
-
mutant L69A
0.00576
-
mutant L69G/A72G
0.0428
-
pH 8.0, 40°C
0.0128
-
pH not specified in the publication, 25°C
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.00204
-
wild-type enzyme
0.00204
-
25°C, pH 7.2
0.0234
-
25°C, pH 7.2, mutant enzyme E286K
0.00248
-
25°C, pH 7.2, wild-type enzyme
0.00147
-
57°C
0.011
-
H199N mutant enzyme, pH 7.5, 25°C
0.434
-
H246N mutant enzyme, pH 7.5, 25°C
0.714
-
hybrid enzyme, pH 7.5, 25°C
0.02
-
metapyrocatechase 1
0.0041
-
metapyrocatechase 2
0.002
-
mutant T249A
0.037
-
mutant T249G
0.0636
-
mutant T249S
0.0225
-
mutated C23O: A229C, H294C
0.04
-
native enzyme, pH 7.5, 25°C
pH 5.0, 35°C, mutant R296Q
0.037
-
pH 7.0, 35°C, mutant A23T/F212S
0.04
-
pH 7.0, 35°C, mutant H24R/F168S/Q275R
0.053
-
pH 7.0, 35°C, wild-type enzyme
0.09
-
pH 7.5, 25°C
0.0016
-
pH 7.5, 60°C
0.0059
-
pH and temperature not specified in the publication
0.3
-
strain 1YB2, pH 7.5, 25°C
0.0011
-
strain 1YdBTEX2, pH 7.5, 25°C
0.0025
-
wild type C23O
0.01
-
wild type enzyme, at pH 7.0 and 35°C
0.09774
-
wild type enzyme, pH 7.5, 25°C
0.0015
-
wildtype
0.001
-
Y255F mutant enzyme, pH 7.5, 25°C
0.005
-
-
0.033
-
pH 7.5, 38°C
0.014
-
25°C
25°C, pH 7.5
2.4
-
60°C
0.12
-
60°C, pH 7.5
0.1
-
Glu79His mutant
0.67
-
in 50 mM Hepes (pH 7.5) at 25°C
0.0589
-
mutant enzyme E79H, at pH 7.5, temperature not specified in the publication
0.67
-
pH 7.5, 30°C
pH 8.0, 20°C
0.281
-
pH 9.0, 25°C, recombinant His-tagged enzyme
0.625
-
pH 9.0, 40°C, recombinant enzyme
0.606
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
1.13
-
at pH 6.0, 20°C
15.4
-
calculated from the Lineweaver-Burk graphs for substrates
2.17
-
detected in dormant saffron corms
2
3
in 0.1 M sodium phosphate buffer (pH 7.0) at 25°C
0.25
-
in 0.1M sodium phosphate buffer (pH 7.0) at 25°C
2.5
-
in 0.2 mM phosphate buffer at pH 6.8 and 30°C
3.8
-
isoenzyme A1
0.09
-
isoenzyme A2
0.091
-
isoenzyme A3
0.014
-
isoenzyme B1
0.087
-
isoenzyme B2
0.104
-
isoenzyme B3
0.018
-
isoenzymes A and B
5
-
isozyme A1, at pH 6.0 and 30°C
0.09
-
isozyme A2, at pH 6.0 and 30°C
0.091
-
isozyme A3, at pH 6.0 and 30°C
0.014
-
isozyme B1, at pH 6.0 and 30°C
0.087
-
isozyme B2, at pH 6.0 and 30°C
0.104
-
isozyme B3, at pH 6.0 and 30°C
0.018
-
Lineweaver-Burk plot of pyrocatechol oxidation by the mushroom PPO
0.4
-
pH 5.6, 37°C
pH 6.5, 28°C
6.47
-
pH 6.8, 25°C, recombinant enzyme
4.65
-
pH 6.8, 25°C, ST94
9.3
-
pH 6.8, 25°C, ST94t
7.3
-
pH 6.8, 30°C
18
-
pH 7.0, 20°C
0.604
-
pH 7.0, 25°C
15.14
-
pH 7.0, 50°C
8
-
pH 8.5, 15°C
0.28
-
pH 8.5, 42°C
34.05
-
pH and temperature not specified in the publication
3.1
-
polyphenol oxidase shows the best activity toward catechol and 4-methyl catechol
12.34
-
recombinant enzyme, pH 7.2, 37°C
pH 7.5, 25°C
0.00836
-
pH not specified in the publication, temperature not specified in the publication
recombinant enzyme expressed in Escherichia coli, membrane-bound enzyme form
0.01
-
recombinant enzyme expressed in Escherichia coli, soluble enzyme form
0.108
-
isozyme I
2
-
30°C, pH not specified in the publication
19.4
-
pH 6.0, 40°C
24.9
-
-
40
-
recombinant enzyme, L-DOPA formation is measured from dicatechol, pyruvate, and ammonium, pH 8.5, 20°C
15.62
-

Ki Value (17 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
approximate value
10
-
pH and temperature not specified in the publication
0.0104
-
30°C, pH 7.8
0.09
-
at pH 7.5 and 20°C
0.0102
-
pH 7.4, temperature not specified in the publication
pH 8.3, 22°C

IC50 Value (7 results)

COMMENTARY
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
LITERATURE
-
1.2
-
pH 7.0, 23°C
0.056
-
IC50: 0.062 mM
0.062
-
cellular tyrosinase-reducing activities, reduction of tyrosinase in HEMn cells
0.022
-
potent hydroxyl radical-scavenging, phloretin, quercetin, 3-hydroxyphloretin, catechol, and pinosylvin have the strongest hydroxyl radical-scavenging properties
0.0011
-
37°C, pH not specified in the publication
7.7
-
pH not specified in the publication, 37°C
7.7
-

References & Links

Links to other databases for catechol

ChEBI
PubChem
-
PubChem