Information on EC 2.1.1.6 - catechol O-methyltransferase and Organism(s) Rattus norvegicus and UniProt Accession P22734

-

3'-O-methyl derivatives are consistently the main metabolites, the meta/para ratio of the metabolites is approximately 6:1

-

?

1-carboxy-1-methyl-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

-

?

1-methyl-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

-

?

2-hydroxyestrogen + S-adenosyl-L-methionine

2-methoxyestrogen + S-adenosyl-L-homocysteine

-

690007

-

?

3,4-dihydroxybenzoic acid + S-adenosyl-L-methionine

4-hydroxy-3-methoxybenzoic acid + S-adenosyl-L-homocysteine

-

the meta/para ratio of the metabolites is approximately 4.5

-

?

3,4-dihydroxybenzoic acid + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

441507, 702534

-

?

3,4-dihydroxymandelic acid + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

-

?

3,4-dihydroxyphenylacetic acid + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

-

?

4-hydroxyestrogen + S-adenosyl-L-methionine

4-methoxyestrogen + S-adenosyl-L-homocysteine

-

690007

-

?

adrenaline + S-adenosyl-L-methionine

methanephrine + S-adenosyl-L-homocysteine

-

-

?

adrenaline + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

441543, 441545, 441553

-

?

benzene-1,2-diol + S-adenosyl-L-methionine

? + S-adenosyl-L-homocysteine

-

-

?

catechol + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

441507, 705937

-

?

DL-3,4-dihydroxyamphetamine + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

-

?

DL-3,4-dihydroxyephedrine + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

-

?

dopa + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

-

?

dopamine + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

-

?

epinephrine + S-adenosyl-L-methionine

metanephrine + S-adenosyl-L-homocysteine

-

-

?

epinine + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

441507, 441522

-

?

L-dopa + S-adenosyl-L-methionine

? + S-adenosyl-L-homocysteine

-

-

?

L-dopa + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + 3-O-methyl-L-dopa

-

-

?

L-Dopa + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + 3-O-methyldopa

-

702534

-

?

norepinephrine + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + normetanephrine

-

441507, 441514

-

?

p-nitrocatechol + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

-

?

procyanidin dimer B1 + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

flavanyl units of procyanidins are methylated consecutively, leading to monomethylated and dimethylated dimeric metabolites

-

?

procyanidin dimer B2 + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

flavanyl units of procyanidins are methylated consecutively, leading to monomethylated and dimethylated dimeric metabolites

-

?

procyanidin dimer B3 + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

flavanyl units of procyanidins are methylated consecutively, leading to monomethylated and dimethylated dimeric metabolites

-

?

procyanidin dimer B4 + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

flavanyl units of procyanidins are methylated consecutively, leading to monomethylated and dimethylated dimeric metabolites

-

?

procyanidin dimer B5 + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

flavanyl units of procyanidins are methylated consecutively, leading to monomethylated and dimethylated dimeric metabolites

-

?

procyanidin dimer B7 + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

flavanyl units of procyanidins are methylated consecutively, leading to monomethylated and dimethylated dimeric metabolites

-

?

procyanidin trimer C1 + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

flavanyl units of procyanidins are methylated consecutively, leading to monomethylated, dimethylated, and trimethylated C1 metabolites

-

?

S-adenosyl-L-homocysteine + 4''-O-methyl epigallocatechin gallate

S-adenosyl-L-homocysteine + 4',4''-di-O-methyl epigallocatechin gallate

-

-

?

S-adenosyl-L-methionine + 2-hydroxyestradiol

S-adenosyl-L-homocysteine + ?

-

658885

-

?

S-adenosyl-L-methionine + 3,4-dihydroxy-L-Phe

S-adenosyl-L-homocysteine + ?

-

-

?

S-adenosyl-L-methionine + 3,4-dihydroxybenzoic acid

S-adenosyl-L-homocysteine + ?

-

657525

-

?

S-adenosyl-L-methionine + a catechol

?

-

441508, 441509, 441515

-

?

S-adenosyl-L-methionine + epigallocatechin

S-adenosyl-L-homocysteine + ?

-

-

?

S-adenosyl-L-methionine + epigallocatechin gallate

S-adenosyl-L-homocysteine + 4''-O-methyl epigallocatechin gallate

-

-

?

S-adenosyl-L-methionine + epinephrine

S-adenosyl-L-homocysteine + metanephrine

-

657526

-

?

S-adenosyl-L-methionine + L-Dopa

S-adenosyl-L-homocysteine + ?

-

-

?

S-adenosyl-L-methionine + norepinephrine

S-adenosyl-L-homocysteine + ?

-

657525

-

?

S-adenosyl-L-methionine + norepinephrine

S-adenosyl-L-homocysteine + normetanephrine

-

685455

-

?

salvianolic acid B + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

-

?

tolcapone + S-adenosyl-L-methionine

S-adenosyl-L-homocysteine + ?

-

substrate of both isoform S-COMT and isoform MB-COMT

-

?

additional information

?

-

8 entries

S-adenosyl-L-methionine + a catechol

?

-

441508, 441509, 441515

-

?

additional information

?

-

4 entries

Mg2+

Cd2+

-

can substitute for Mg2+

Co2+

-

Co2+ and Mn2+ most effective in activation

Fe2+

-

can substitute for Mg2+

Mg2+

7 entries

Mn2+

-

Co2+ and Mn2+ most effective in activation

Ni2+

-

can substitute for Mg2+

Zn2+

-

can substitute for Mg2+

(-)-epigallocatechin-3-O-gallate

potent non-competitive inhibitor

688418

4'-fluoro-4,5-dihydroxy-biphenyl-3-carboxylic acid [(E)-3-[(2S,4R,5R)-4-hydroxy-5-(6-methyl-purin-9-yl)-tetrahydro-furan-2-yl]-allyl]-amide

-

4'-fluoro-4,5-dihydroxy-biphenyl-3-carboxylic acid [(E)-3-[(2S,4R,5R)-4-hydroxy-5-(6-methylamino-purin-9-yl)-tetrahydro-furan-2-yl]-allyl]-amide

-

4-phenyl-7,8-dihydroxycoumarin

-

9-[(5E)-3,5,6,7-tetradeoxy-3-fluoro-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-xylo-hept-5-enofuranosyl]-N6-methyladenine

-

9-[(5E)-3,5,6,7-tetradeoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-3-methyl-beta-D-xylo-hept-5-enofuranosyl]-N6-propyladenine

-

catechin

-

epicatechin

-

epigallocatechin

-

fisetin

-

N-[(2E)-3-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-(methylamino)-9H-purin-9-yl]tetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

-

N-[(2E)-3-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-(propylamino)-9H-purin-9-yl]tetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

-

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-2,3-dihydroxy-5-nitrobenzamide

-

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

-

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-ethyl-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

-

N-[(2E)-3-[(2R,3S,4R,5R)-5-[6-(cyclopropylamino)-9H-purin-9-yl]-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

-

N-[(2E)-3-[(2R,3S,4R,5R)-5-[6-(ethylamino)-9H-purin-9-yl]-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

-

N-[(2E)-3-[(2R,3S,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-2,3-dihydroxy-5-nitrobenzamide

-

N-[(2E)-3-[(2S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-2,3-dihydroxy-5-nitrobenzamide

-

quercetin

-

(2E)-4,7-anhydro-1,2,3-trideoxy-1-(2,3-dihydroxy-5-nitrobenzamido)-L-ribo-hept-2-enitol

-

1-Carboxysalsoline

-

i.e. 1-carboxy-1-methyl-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline, competitive inhibition of 3,4-dihydroxybenzoic acid methylation

1-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]-4-(trifluoromethyl)-1H-imidazole

-

1-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]benzo[d]imidazole

-

1-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]pyridin-4(1H)-one

-

1-[1-(2-chlorobenzyl)-1H-benzimidazol-4-yl]-3-hydroxypyridin-4(1H)-one

-

1-[3,4-dihydroxy-5-nitrophenyl]-2-phenyl-ethanone

-

658656

1-[3-(5-chloro-1H-pyrrolo[2,3-b]pyridin-4-yl)phenyl]-5-hydroxy-2-(1-hydroxyethyl)pyridin-4(1H)-one

-

3,4,5-trihydroxypyrogallol

-

liver homogenate, 0.03 mM inhibitor: 0.8% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

3,5-dinitrocatechol

-

liver S-COMT, 50% inhibition at 74 nM

441545

3-Carboxysalsolinol

-

441536

3-fluoro-4-[1-[4-(trifluoromethyl)phenyl]-1H-pyrazol-5-yl]benzene-1,2-diol

-

liver homogenate, 0.03 mM inhibitor: 32.3% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

3-nitro-5-(1-p-tolyl-1H-pyrazol-5-yl)benzene-1,2-diol

-

liver homogenate, 0.003 mM inhibitor: 0% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

3-nitro-5-(1-phenyl-1H-pyrazol-5-yl)benzene-1,2-diol

-

liver homogenate, 0.003 mM inhibitor: 0% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

3-nitro-5-(1H-pyrazol-5-yl)benzene-1,2-diol

-

liver homogenate, 0.003 mM inhibitor: 0% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

4-(1-phenyl-1H-pyrazol-5-yl)benzene-1,2,3-triol

-

liver homogenate, 0.03 mM inhibitor: 26.8% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

4-(5-(3,4-dihydroxy-5-nitrophenyl)-1H-pyrazol-1-yl)benzonitrile

-

liver homogenate, 0.003 mM inhibitor: 0.3% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

4-[1-(4-methylphenyl)-1H-pyrazol-5-yl]benzene-1,2-diol

-

liver homogenate, 0.03 mM inhibitor: 41.2% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

4-[4-(4-chlorophenyl)-5-methyl-1H-pyrazol-3-yl]benzene-1,2,3-triol

-

liver homogenate, 0.003 mM inhibitor: 15.6% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

5-(1-methyl-1H-pyrazol-5-yl)-3-nitrobenzene-1,2-diol

-

liver homogenate, 0.003 mM inhibitor: 1.1% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

5-hydroxy-1-[3-(isoquinolin-4-yl)phenyl]-2-(2,2,2-trifluoro-1-hydroxyethyl)pyridin-4(1H)-one

-

5-Substituted 3-hydroxy-4-methoxybenzaldehydes

-

441537

5-Substituted 3-hydroxy-4-methoxybenzoic acids

-

441537

5-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]-5H-imidazo[4,5-c]pyridine

-

5-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]-5H-pyrrolo[3,2-c]pyridine

-

5-[1-(3-chlorophenyl)-1H-pyrazol-5-yl]-2,3-dihydroxybenzoic acid

-

liver homogenate, 0.03 mM inhibitor: 24.1% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

5-[1-(3-chlorophenyl)-1H-pyrazol-5-yl]-3-nitrobenzene-1,2-diol

-

liver homogenate, 0.003 mM inhibitor: 0% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

5-[1-(3-chlorophenyl)-4-phenyl-1H-pyrazol-5-yl]-3-nitrobenzene-1,2-diol

-

liver homogenate, 0.003 mM inhibitor: 68.6% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

6-methyl-9-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]purine

-

9-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]purine

-

Analogs of S-adenosyl-L-homocysteine

-

overview: inhibition of the liver, heart and brain enzyme

441514

beta-thujaplicin

-

70-100% inhibition at 0.2 mM

Ca2+

-

flavonoids

-

overview: relationship between structure and ability to inhibit

gallic acid

-

high ionic strength

-

-

iodoacetic acid

-

441507, 441509, 441533

L-ascorbic acid

-

L-Dopa

-

Mg2+

N-ethyl-1-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]-1H-imidazole-4-carboxamide

-

N-ethylmaleimide

N-methyl-1-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]-1H-1,2,4-triazole-3-carboxamide

-

N-methyl-1-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]-1H-imidazole-4-carboxamide

-

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-2,3-dihydroxy-5-nitrobenzamide

-

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

-

N6-methyl-9-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]adenine

-

norepinephrine

-

0.01 mM, 41% inhibition of 2-hydroxyestradiol methylation

658885

OR-462

-

disubstituted catechol

441531

OR486

-

depressed COMT activity results in enhanced mechanical and thermal pain sensitivity

689314

p-chloromercuribenzoate

-

441507, 441509

p-hydroxymercuribenzoate

-

70-100% inhibition at 0.2 mM

441515

Phenolic compounds

-

-

Polyphenolic compounds

-

-

pyridin-4-yl (5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-1-thio-beta-D-ribo-hept-5-enofuranoside

-

pyrogallol

quercetin

-

0.01 mM, 90% inhibition of 2-hydroxyestradiol methylation

Ro 41-0960

-

RO-4-4602

-

competitive

441516

Ro41-0960

-

depressed COMT activity results in enhanced mechanical and thermal pain sensitivity

689314

S-adenosyl-L-homocysteine

-

441509, 441514, 441522

Salsolidine

salvianolic acid B

-

weak inhibitor. In vivo, a single intravenous dose of salvianolic acid B decreases the plasma concentration of 3-O-methyldopa, with no obvious effect on the pharmacokinetics of L-dopa

tolcapone

-

strongly inhibits the formation of 3-methylsalvianolic acid B in vitro and in vivo, without any change in its plasma concentration. Tolcapone significantly increases the cumulative bile excretion of salvianolic acid from 3% to 40% in the rat

tropolone

[5-(3,4-dihydroxy-5-nitrophenyl)-4-phenyl-1H-pyrazol-1-yl](4-methylphenyl)methanone

-

liver homogenate, 0.003 mM inhibitor: 2.8% metanephrine formed relative to the control in absence of inhibitor (5 min reaction time), pH 7.8, 37°C

additional information

3 entries

-

0.0009 - 0.345

epinephrine

0.0055 - 0.464

norepinephrine

0.000148 - 0.000407

2-hydroxyestradiol

4 entries

0.0014 - 0.48

adrenaline

9 entries

0.0117

epigallocatechin

-

0.0048

epigallocatechin gallate

-

0.009 - 1

epinephrine

3 entries

0.0055 - 1.856

norepinephrine

15 entries

0.0038

p-nitrocatechol

-

0.00501 - 0.283

S-adenosyl-L-methionine

6 entries

0.0113 - 0.0797

salvianolic acid B

4 entries

additional information

5 entries

-

0.007022

(2E)-4,7-anhydro-1,2,3-trideoxy-1-(2,3-dihydroxy-5-nitrobenzamido)-L-ribo-hept-2-enitol

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.44

1-Carboxysalsoline

-

0.004645

1-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]-4-(trifluoromethyl)-1H-imidazole

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.014

1-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]benzo[d]imidazole

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0749

1-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]pyridin-4(1H)-one

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000019

1-[3,4-dihydroxy-5-nitrophenyl]-2-phenyl-ethanone

-

658656

0.0024

5-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]-5H-imidazo[4,5-c]pyridine

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.002378

5-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]-5H-pyrrolo[3,2-c]pyridine

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000001

6-methyl-9-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]purine

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000034

9-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]purine

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0104

N-ethyl-1-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]-1H-imidazole-4-carboxamide

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0156

N-methyl-1-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]-1H-1,2,4-triazole-3-carboxamide

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0199

N-methyl-1-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]-1H-imidazole-4-carboxamide

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000002

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-2,3-dihydroxy-5-nitrobenzamide

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000007

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000007

N6-methyl-9-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]adenine

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000132

pyridin-4-yl (5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-1-thio-beta-D-ribo-hept-5-enofuranoside

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0053 - 0.009

RO-4-4602

3 entries

0.022 - 0.04

S-adenosyl-L-homocysteine

-

441514

0.19

Salsolidine

-

0.0021

salvianolic acid B

-

37°C, pH not specified in the publication

0.0012

(-)-epigallocatechin-3-O-gallate

0.001368

4'-fluoro-4,5-dihydroxy-biphenyl-3-carboxylic acid [(E)-3-[(2S,4R,5R)-4-hydroxy-5-(6-methyl-purin-9-yl)-tetrahydro-furan-2-yl]-allyl]-amide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.001858

4'-fluoro-4,5-dihydroxy-biphenyl-3-carboxylic acid [(E)-3-[(2S,4R,5R)-4-hydroxy-5-(6-methylamino-purin-9-yl)-tetrahydro-furan-2-yl]-allyl]-amide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000011

9-[(5E)-3,5,6,7-tetradeoxy-3-fluoro-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-xylo-hept-5-enofuranosyl]-N6-methyladenine

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000025

9-[(5E)-3,5,6,7-tetradeoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-3-methyl-beta-D-xylo-hept-5-enofuranosyl]-N6-propyladenine

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.012 - 0.019

catechin

0.019 - 0.04

epicatechin

0.02 - 0.039

epigallocatechin

0.0021 - 0.0035

fisetin

0.000011

N-[(2E)-3-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-(methylamino)-9H-purin-9-yl]tetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000026

N-[(2E)-3-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-(propylamino)-9H-purin-9-yl]tetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000009

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-2,3-dihydroxy-5-nitrobenzamide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000035

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000236

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-ethyl-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000082

N-[(2E)-3-[(2R,3S,4R,5R)-5-[6-(cyclopropylamino)-9H-purin-9-yl]-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000043

N-[(2E)-3-[(2R,3S,4R,5R)-5-[6-(ethylamino)-9H-purin-9-yl]-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.028

N-[(2E)-3-[(2R,3S,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-2,3-dihydroxy-5-nitrobenzamide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.00004

N-[(2E)-3-[(2S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-2,3-dihydroxy-5-nitrobenzamide

Rattus norvegicus

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0022 - 0.0045

quercetin

0.0316

(2E)-4,7-anhydro-1,2,3-trideoxy-1-(2,3-dihydroxy-5-nitrobenzamido)-L-ribo-hept-2-enitol

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0209

1-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]-4-(trifluoromethyl)-1H-imidazole

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0628

1-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]benzo[d]imidazole

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.336

1-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]pyridin-4(1H)-one

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0000265 - 0.000881

1-[1-(2-chlorobenzyl)-1H-benzimidazol-4-yl]-3-hydroxypyridin-4(1H)-one

0.0000274 - 0.000237

1-[3-(5-chloro-1H-pyrrolo[2,3-b]pyridin-4-yl)phenyl]-5-hydroxy-2-(1-hydroxyethyl)pyridin-4(1H)-one

0.000013 - 0.000565

5-hydroxy-1-[3-(isoquinolin-4-yl)phenyl]-2-(2,2,2-trifluoro-1-hydroxyethyl)pyridin-4(1H)-one

0.0108

5-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]-5H-imidazo[4,5-c]pyridine

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0107

5-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]-5H-pyrrolo[3,2-c]pyridine

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000006

6-methyl-9-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]purine

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000155

9-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]purine

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0468

N-ethyl-1-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]-1H-imidazole-4-carboxamide

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0703

N-methyl-1-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]-1H-1,2,4-triazole-3-carboxamide

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.0895

N-methyl-1-[(5E)-5,6,7-trideoxy-7-[5-(4-fluorophenyl)-2,3-dihydroxybenzamido]-beta-D-ribo-hept-5-enofuranosyl]-1H-imidazole-4-carboxamide

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000009

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-2,3-dihydroxy-5-nitrobenzamide

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000031

N-[(2E)-3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]prop-2-en-1-yl]-4'-fluoro-4,5-dihydroxybiphenyl-3-carboxamide

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000032

N6-methyl-9-[(5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-beta-D-ribo-hept-5-enofuranosyl]adenine

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

0.000596

pyridin-4-yl (5E)-5,6,7-trideoxy-7-(2,3-dihydroxy-5-nitrobenzamido)-1-thio-beta-D-ribo-hept-5-enofuranoside

Rattus norvegicus

-

liver homogenate, substrate benzene-1,2-diol, pH 7.6, 37°C

2172

-

441517

additional information

5 entries

7

-

membrane-bound enzyme

7.3 - 8.2

-

7.4

-

membrane-bound activity

7.5 - 8.2

-

7.8

8 - 8.5

-

additional information

submandibular salivary gland

wild-type is independent of pH

50

-

-

-

-

-

-

-

membrane-bound COMT activities in the cerebral cortex are significantly reduced in high-salt loaded Dahl salt-sensitive rats compared with normal-salt loaded Dahl salt-sensitive rats

-

-

-

-

-

-

-

COMT is not located in dopaminergic nigrostriatal projection neurons

-

-

-

-

-

L-COMT is the predominant enzyme form

testis

-

L-COMT is the predominant enzyme form

thymus

-

L-COMT is the predominant enzyme form

additional information

two molecular forms: a soluble form (S-COMT) and in another form associated with membranes (MB-COMT). MB-COMT is an integral membrane protein with the catalytic portion of the enzyme oriented toward the cytoplasmic side of the membrane

-

S-COMT, recombinant enzyme

endoplasmic reticulum

-

MB-COMT, recombinant enzyme

-

-

S-COMT, recombinant enzyme

additional information

P22734 pBLAST

COMT_RAT

264

1

29597

Swiss-Prot

Show Sequence

Secretory Pathway (Reliability: 1)

24889

1 * 24889, ESI Q-pole mass spectrometry

24890

24891

1 * 24891, calculated from amino acid sequence

705404

21000

-

gel filtration

23000

24000

25000

-

gel filtration

441527

25700

-

1 * 25700, liver, SDS-PAGE

28000

47500

-

COMT II, gel filtration, sedimentation data

441508

monomer

?

-

x * 23000, SDS-PAGE

441509

monomer

apo and holo forms of rat catechol-O-methyltransferase, hanging drop vapor diffusion method, the apo crystals are grown from 0.2 M (NH4)2SO4, 30% (w/v) PEG8000, the holo form of crystals are grown from 0.2 M (NH4)2SO4, 26% (w/v) PEG8000, 0.2% (v/v) sucrose

705404

in complex with 4-phenyl-7,8-dihydroxycoumarin, hanging drop vapor diffusion method, using 0.2 M (NH4)2SO4, 0.1 M Tris pH 7.5, 30% (w/v) PEG8000

mutant Y200L, with bound S-adenosyl-L-methionine and 3,5-dinitrocatechol, to 1.6 A resolution

quantum mechanics/molecular mechanics computational analysis of catechol O-methylation in aqueous solution and in the active site. A large fraction of the environmental motions needed to attain the transition state happens during the first stages of the reaction. The incorporation of the solvent coordinate in the definition of the transition state improves the transmission coefficient and the committor histogram in solution, while the changes are much less significant in the enzyme. The equilibrium solvation approach seems then to work better in the enzyme than in aqueous solution because the enzyme provides a preorganized environment where the reaction takes place

734543

sitting drop vapour diffusion method

-

-

K144A

mutation of the proposed catalytic Lys residue, does not abolish COMT activity

K144A/V173Y

shift towards para-selectivity

M91I/Y95C

active site humanized enzyme

W38D

mutation of hydrophobic pocket, approximately +93% regioisomeric excess, and around 50% conversion of substrate 3,4-dihydroxybenzaldehyde

W38K

mutant favors para- over meta-methylation of dihydroxy substrates

W38R

mutant favors para- over meta-methylation of dihydroxy substrates

Y200L

mutant favors meta- over para-methylation of dihydroxy substrates, and exhibits the greatest meta-selectivity whilst retaining relative activity similar to that of the wild-type

37

-

2 h, inactivation

-10°C, 3 months, stable

-

-20°C, or -60°C, 50 mM Tris-HCl, pH 7.5, 20 mM 2-mercaptoethanol, 20% v/v glycerol, 60-80% of activity retained after 6 months

-

441508

-4°C, stable for several weeks

-

-

GST 4B Sepharose resin column chromatography, Super Q-5PW column chromatography, and Superdex 75 gel filtration

GST Sepharose resin column chromatography, GSTrap column chromatography, Super Q-5PW column chromatography, and Superdex 75 gel filtration

-

-

441508, 441509, 441527, 441533, 719299

affinity chromatography

-

microsomal

-

overview on purification of native and recombinant protein

-

recombinant enzyme

-

soluble and microsomal enzyme

-

-

expressed in Escherichia coli BL21 Codon Plus (DE3) cells

702027, 705404

gene expressed in Escherichia coli

-

S-COMT

-

S-COMT and MB-COMT are encoded by a single gene with two different sites of transcription initiation, overview on genetic polymorphism

-

441542

soluble part from M44 to S264 expressed in Escherichia coli W3110[pREP4]

-

there are no effects of gonadectomy itself on COMT-s activity, there are significant effects of hormone replacement (supplementation with testosterone propionate or with estradiol for 28 days) but not gonadectomy on the soluble but not the membrane-bound isoform of catechol-O-methyltransferase in both striatum and brain cortex

-

medicine

Axelrod, J.; Tomchick, R.

Enzymatic O-methylation of epinephrine and other catechols

J. Biol. Chem.

233

702-705

1958

Bos taurus, Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa

13575440

441508

Huh, M.M.O.; Friedhoff, A.J.

Multiple molecular forms of catechol-O-methyltransferase. Evidence for two distinct forms, and their purification and physical characterization

J. Biol. Chem.

254

299-308

1979

Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus

762061

441509

Borchardt, R.T.

Catechol O-methyltransferase

Methods Enzymol.

77

267-272

1981

Rattus norvegicus

7329304

441511

Lundstr�m, K.; Tilgmann, C.; Per�nen, J.; Kalkkinen, N.; Ulmanen, I.

Expression of enzymatically active rat liver and human placental catechol-O-methyltransferase in Escherichia coli; purification and partial characterization of the enzyme

Biochim. Biophys. Acta

1129

149-154

1992

Homo sapiens, Rattus norvegicus

1730052

441514

Borchardt, R.T.; Cheng, C.F.

Purification and characterization of rat heart and brain catechol methyltransferase

Biochim. Biophys. Acta

522

49-62

1978

Rattus norvegicus

413582

441515

Tong, J.H.; D'Iorio, A.

Solubilization and partial purification of particulate catechol-O-methyltransferase from rat liver

Can. J. Biochem.

55

1108-1113

1977

Rattus norvegicus

912603

441516

Buu, N.T.; Kuchel, O.; Parent, M.T.

Competitive inhibition of catechol O-methyltransferase by RO-4-4602

Can. J. Biochem.

55

771-773

1977

Rattus norvegicus

890572

441517

Borchardt, R.T.; Cheng, C.F.; Thakker, D.R.

Purification of catechol-O-methyltransferase by affinity chromatography

Biochem. Biophys. Res. Commun.

63

69-77

1975

Rattus norvegicus

1125027

Sanft, K.; Thomas, H.

Competitive inhibition of catechol-O-methyltransferase by tetrahydro-isochinoline alkaloids salsolidin and 1-carboxysalsolin

Z. Naturforsch. C

44

173-176

1989

Rattus norvegicus

2490067

441521

Schwabe, K.P.; Flohe, L.

Catechol-O-methyltransferase, 3. Relationship between the structure of flavonoids and their ability to inhibit catechol-O-methyltransferase

Hoppe-Seyler's Z. Physiol. Chem.

353

476-482

1972

Rattus norvegicus

5028212

441522

Coward, J.K.; Slisz, E.P.; Wu, F.Y.H.

Kinetic studies on catechol O-methyltransferase. Product inhibition and the nature of the catechol binding site

Biochemistry

12

2291-2297

1973

Rattus norvegicus

4736330

441527

Tilgmann, C.; Kalkkinen, N.

Purification and partial characterization of rat liver soluble catechol-O-methyltransferase

FEBS Lett.

264

95-99

1990

Homo sapiens, Rattus norvegicus

2338148

441531

Schultz, E.; Nissinen, E.

Inhibition of rat liver and duodenum soluble catechol-O-methyltransferase by a tight-binding inhibitor OR-462

Biochem. Pharmacol.

38

3953-3956

1989

Rattus norvegicus

2597177

Rhee, J.; Myung Un, C.

Rat liver catechol-O-methyltransferase: Purification and general properties

Hanguk Saenghwahakhoe Chi

21

60-67

1988

Rattus norvegicus

-

441536

Tunnicliff, G.; Ngo, T.T.

Kinetics of rat brain soluble catechol-O-methyltransferase and its inhibition by substrate analogues

Int. J. Biochem.

15

733-738

1983

Rattus norvegicus

6862087

441537

Borchardt, R.T.; Huber, J.H.; Houston, M.

Catechol O-methyltransferase. 10. 5-Substituted 3-hydroxy-4-methoxybenzoic acids (isovanillic acids) and 5-substituted 3-hydroxy-4-methoxybenzaldehydes (isovanillins) as potential inhibitors

J. Med. Chem.

25

258-263

1982

Rattus norvegicus

7069704

441539

Ulmanen, I.; Peranen, J.; Tenhunen, J.; Tilgmann, C.; Karhunen, T.; Panula, P.; Bernasconi, L.; Aubry, J.P.; Lundstrom, K.

Expression and intracellular localization of catechol O-methyltransferase in transfected mammalian cells

Eur. J. Biochem.

243

452-459

1997

Homo sapiens, Rattus norvegicus

9030772

441541

Karhunen, T.; Tilgmann, C.; Ulmanen, I.; Julkunen, I.; Panula, P.

Distribution of catechol-O-methyltransferase enzyme in rat tissues

J. Histochem. Cytochem.

42

1079-1090

1994

Rattus norvegicus

8027527

441542

Weinshilboum, R.M.; Otterness, D.M.; Szumlanski, C.L.

Methylation pharmacogenetics: catechol O-methyltransferase, thiopurine methyltransferase, and histamine N-methyltransferase

Annu. Rev. Pharmacol. Toxicol.

39

19-52

1999

Rattus norvegicus, Homo sapiens (P21964)

10331075

441543

Bonifacio, M.J.; Vieira-Coelho, M.A.; Borges, N.; Soares-da-Silva, P.

Kinetics of rat brain and liver solubilized membrane-bound catechol-O-methyltransferase

Arch. Biochem. Biophys.

384

361-367

2000

Rattus norvegicus

11368324

441545

Bonifacio, M.J.; Vieira-Coelho, M.A.; Soares-da-Silva, P.

Expression and characterization of rat soluble catechol-O-methyltransferase fusion protein

Protein Expr. Purif.

23

106-112

2001

Rattus norvegicus, Rattus norvegicus S-COMT

11570851

441549

Tilgmann, C.; Ulmanen, I.

Purification methods of mammalian catechol-O-methyltransferases

J. Chromatogr. B

684

147-161

1996

Homo sapiens, Rattus norvegicus

8906471

441553

Borges, N.; Vieira-Coelho, M.A.; Parada, A.; Soares-Da-Silva, P.

Rat liver catechol-O-methyltransferase kinetics and assay methodology

J. Enzyme Inhib.

13

473-483

1998

Rattus norvegicus

9825310

441555

Zheng, Y.; Bruice, T.C.

A theoretical examiniation of the factors controlling the catalytic efficiency of a transmethylation enzyme: Catechol O-methyltransferase

J. Am. Chem. Soc.

119

8137-8145

1997

Rattus norvegicus

-

657525

Masuda, M.; Tsunoda, M.; Imai, K.

High-performance liquid chromatography-fluorescent assay of catechol-O-methyltransferase activity in rat brain

Anal. Bioanal. Chem.

376

1069-1073

2003

Rattus norvegicus

12904944

657526

Tsunoda, M.; Imai, K.

An assay for determination of rat adrenal catechol-O-methyltransferase activity: comparison of spontaneously hypertensive rats and Wistar-Kyoto rats

Anal. Bioanal. Chem.

380

887-890

2004

Rattus norvegicus

15551073

Lu, H.; Meng, X.; Yang, C.S.

Enzymology of methylation of tea catechins and inhibition of catechol-O-methyltransferase by (-)-epigallocatechin gallate

Drug Metab. Dispos.

31

572-579

2003

Homo sapiens, Rattus norvegicus, Sus scrofa

12695345

658656

Bonifacio, M.J.; Vieira-Coelho, M.A.; Soares-da-Silva, P.

Kinetic inhibitory profile of BIA 3-202, a novel fast tight-binding, reversible and competitive catechol-O-methyltransferase inhibitor

Eur. J. Pharmacol.

460

163-170

2003

Rattus norvegicus

12559377

658885

Zaccharia L.C.; Dubey, R.K.; Mi, Z.; Jackson, E.K.

Methylation of 2-hydroxyestradiol in isolated organs

Hypertension

42

82-87

2003

Rattus norvegicus

12771046

685455

Hirano, Y.; Tsunoda, M.; Shimosawa, T.; Fujita, T.; Funatsu, T.

Measurement of catechol-O-methyltransferase activity in the brain of Dahl salt-sensitive rats

Biol. Pharm. Bull.

30

2178-2180

2007

Rattus norvegicus

17978496

686194

Bonifacio, M.J.; Palma, P.N.; Almeida, L.; Soares-da-Silva, P.

Catechol-O-methyltransferase and its inhibitors in Parkinsons disease

CNS Drug Rev.

13

352-379

2007

Oryctolagus cuniculus, Homo sapiens, Mus musculus, Sus scrofa, Rattus norvegicus (P22734)

17894650

687048

Hirano, Y.; Tsunoda, M.; Shimosawa, T.; Matsui, H.; Fujita, T.; Funatsu, T.

Suppression of catechol-O-methyltransferase activity through blunting of alpha2-adrenoceptor can explain hypertension in Dahl salt-sensitive rats

Hypertens. Res.

30

269-278

2007

Homo sapiens, Rattus norvegicus

17510509

688418

Rutherford, K.; Le Trong, I.; Stenkamp, R.E.; Parson, W.W.

Crystal structures of human 108V and 108M catechol O-methyltransferase

J. Mol. Biol.

380

120-130

2008

Sus scrofa, Homo sapiens (P21964), Homo sapiens, Rattus norvegicus (P22734)

18486144

689173

Helkamaa, T.; Reenilae, I.; Tuominen, R.K.; Soinila, S.; Vaeaenaenen, A.; Tilgmann, C.; Rauhala, P.

Increased catechol-O-methyltransferase activity and protein expression in OX-42-positive cells in the substantia nigra after lipopolysaccharide microinfusion

Neurochem. Int.

51

412-423

2007

Rattus norvegicus

17573159

689314

Nackley, A.G.; Tan, K.S.; Fecho, K.; Flood, P.; Diatchenko, L.; Maixner, W.

Catechol-O-methyltransferase inhibition increases pain sensitivity through activation of both beta 2- and beta 3-adrenergic receptors

Pain

128

199-208

2007

Rattus norvegicus

17084978

690007

Wentz, M.J.; Shi, S.Q.; Shi, L.; Salama, S.A.; Harirah, H.M.; Fouad, H.; Garfield, R.E.; Al-Hendy, A.

Treatment with an inhibitor of catechol-O-methyltransferase activity reduces preterm birth and impedes cervical resistance to stretch in pregnant rats

Reproduction

134

831-839

2007

Rattus norvegicus

18042640

Tsuji, E.; Okazaki, K.; Takeda, K.

Crystal structures of rat catechol-O-methyltransferase complexed with coumarine-based inhibitor

Biochem. Biophys. Res. Commun.

378

494-497

2009

Rattus norvegicus (P22734)

19056347

Overbye, A.; Seglen, P.O.

Phosphorylated and non-phosphorylated forms of catechol O-methyltransferase in rat liver, brain and other tissues

Biochem. J.

417

535-545

2009

Rattus norvegicus

18831714

702534

Reenilae, I.; Rauhala, P.

Simultaneous analysis of catechol-O-methyl transferase activity, S-adenosylhomocysteine and adenosine

Biomed. Chromatogr.

24

294-300

2010

Rattus norvegicus

19629963

705404

Tsuji, E.; Okazaki, K.; Isaji, M.; Takeda, K.

Crystal structures of the apo and holo form of rat catechol-O-methyltransferase

J. Struct. Biol.

165

133-139

2009

Rattus norvegicus (P22734)

19111934

705937

Meyers, B.; DAgostino, A.; Walker, J.; Kritzer, M.

Gonadectomy and hormone replacement exert region- and enzyme isoform-specific effects on monoamine oxidase and catechol-O-methyltransferase activity in prefrontal cortex and neostriatum of adult male rats

Neuroscience

165

850-862

2010

Rattus norvegicus

19909795

Ellermann, M.; Lerner, C.; Burgy, G.; Ehler, A.; Bissantz, C.; Jakob-Roetne, R.; Paulini, R.; Allemann, O.; Tissot, H.; Gruenstein, D.; Stihle, M.; Diederich, F.; Rudolph, M.G.

Catechol-O-methyltransferase in complex with substituted 3-deoxyribose bisubstrate inhibitors

Acta Crystallogr. Sect. D

68

253-260

2012

Rattus norvegicus (P22734)

22349227

Ellermann, M.; Paulini, R.; Jakob-Roetne, R.; Lerner, C.; Borroni, E.; Roth, D.; Ehler, A.; Schweizer, W.B.; Schlatter, D.; Rudolph, M.G.; Diederich, F.

Molecular recognition at the active site of catechol-O-methyltransferase (COMT): adenine replacements in bisubstrate inhibitors

Chemistry

17

6369-6381

2011

Rattus norvegicus

21538606

Kiss, L.E.; Ferreira, H.S.; Torrao, L.; Bonifacio, M.J.; Palma, P.N.; Soares-da-Silva, P.; Learmonth, D.A.

Discovery of a long-acting, peripherally selective inhibitor of catechol-O-methyltransferase

J. Med. Chem.

53

3396-3411

2010

Rattus norvegicus

20334432

Robinson, R.G.; Smith, S.M.; Wolkenberg, S.E.; Kandebo, M.; Yao, L.; Gibson, C.R.; Harrison, S.T.; Polsky-Fisher, S.; Barrow, J.C.; Manley, P.J.; Mulhearn, J.J.; Nanda, K.K.; Schubert, J.W.; Trotter, B.W.; Zhao, Z.; Sanders, J.M.; Smith, R.F.; McLoughlin, D.; Sharma, S.; Hall, D.L.; Walker, T.L.; Kershner, J.L.; , B.

Characterization of non-nitrocatechol pan and isoform specific catechol-O-methyltransferase inhibitors and substrates

ACS Chem. Neurosci.

3

129-140

2012

Homo sapiens, Rattus norvegicus

22860182

Weinert, C.; Wiese, S.; Rawel, H.; Esatbeyoglu, T.; Winterhalter, P.; Homann, T.; Kulling, S.

Methylation of catechins and procyanidins by rat and human catechol-o-methyltransferase: Metabolite profiling and molecular modeling studies

Drug Metab. Dispos.

40

353-359

2012

Homo sapiens, Rattus norvegicus

22071171

734543

Garcia-Meseguer, R.; Zinovjev, K.; Roca, M.; Ruiz-Pernia, J.J.; Tunon, I.

Linking electrostatic effects and protein motions in enzymatic catalysis. A theoretical analysis of catechol O-methyltransferase

J. Phys. Chem. B

119

873-882

2015

Rattus norvegicus (P22734)

25159911

735089

Schendzielorz, N.; Oinas, J.P.; Myoehaenen, T.T.; Reenilae, I.; Raasmaja, A.; Maennistoe, P.T.

Catechol-O-methyltransferase (COMT) protein expression and activity after dopaminergic and noradrenergic lesions of the rat brain

PLoS ONE

8

e61392

2013

Rattus norvegicus

23613844

Qi, Q.; Cao, L.; Li, F.; Wang, H.; Liu, H.; Hao, H.; Hao, K.

Salvianolic acid B as a substrate and weak catechol-O-methyltransferase inhibitor in rats

Xenobiotica

45

820-827

2015

Rattus norvegicus

25869243