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Ligand dopamine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

(S)-reticuline biosynthesis, catecholamine biosynthesis

KEGG

Alcoholism, Amphetamine addiction, Betalain biosynthesis, Bile secretion, Biosynthesis of alkaloids derived from shikimate pathway, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, cAMP signaling pathway, Cocaine addiction, Dopaminergic synapse, Gap junction, Isoquinoline alkaloid biosynthesis, Morphine addiction, Neuroactive ligand-receptor interaction, Parkinson disease, Prolactin signaling pathway, Synaptic vesicle cycle, Tyrosine metabolism more

MetaCyc

(S)-reticuline biosynthesis I, (S)-reticuline biosynthesis II, aromatic biogenic amine degradation (bacteria), betacyanin biosynthesis (via dopamine), betaxanthin biosynthesis, betaxanthin biosynthesis (via dopamine), catecholamine biosynthesis, dopamine degradation, emetine biosynthesis, L-dopa degradation II (bacterial) more

Show all BRENDA pathways known for dopamine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (23 results)

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Show Natural Substrate (23 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

dopamine + O2 = ?

676649

-

1.14.17.1

3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O

674660, 438597, 438601, 438614, 438610, 438613, 438620, 438621, 438634

-

1.14.17.1

dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O

728562, 744851, 745892, 746431, 744598, 744949, 744950

-

1.14.17.1

dopamine + ascorbate + O2 = norepinephrine + dehydroascorbate + H2O

727633

-

1.14.17.1

3 entries

1.14.18.1

dopamine + O2 = ?

744015

-

1.4.3.4

dopamine + H2O + O2 = (3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2

705940, 724786

-

1.4.3.4

dopamine + H2O + O2 = ?

711407, 711912

-

1.4.3.4

2 entries

1.6.3.5

dopamine + O2 = ?

743215

-

2.3.1.87

acetyl-CoA + dopamine = CoA + N-acetyldopamine

719595

-

2.7.11.22

ATP + dopamine = ADP + phosphorylated dopamine

666401

-

2.8.2.1

2 3'-phosphoadenylyl sulfate + 2 dopamine = 2 adenosine 3',5'-bisphosphate + dopamine 3-O-sulfate + dopamine 4-O-sulfate

671928

2a3r, 3D-view

2.8.2.1

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + ?

675515, 675751, 702738

2a3r, 3D-view

2.8.2.1

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopamine sulfate

723935, 671573

2a3r, 3D-view

2.8.2.1

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopaminyl sulfate

726515

2a3r, 3D-view

2.8.2.1

3'-phosphoadenylylsulfate + dopamine = adenosine 3',5'-bisphosphate + ?

645651

2a3r, 3D-view

2.8.2.1

5 entries

2.8.2.2

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopamine sulfate

760542

-

2.8.2.4

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopamine sulfate

760542

-

4.2.1.78

4-(2-Aminoethyl)benzene-1,2-diol + 4-hydroxyphenylacetaldehyde = (S)-Norcoclaurine + H2O

690826, 690258, 693259, 653569, 652296, 682682

2vq5, 3D-view

4.2.1.78

4-(2-Aminoethyl)benzene-1,2-diol + 4-hydroxyphenylacetaldehyde = ?

5894

2vq5, 3D-view

4.2.1.78

4-hydroxyphenylacetaldehyde + 4-(2-aminoethyl)benzene-1,2-diol = (S)-norcoclaurine + H2O

716518, 715141

2vq5, 3D-view

4.2.1.78

4-hydroxyphenylacetaldehyde + dopamine = (S)-norcoclaurine + H2O

729604, 728793, 730988, 749327, 747310, 747372

2vq5, 3D-view

4.2.1.78

4 entries

4.3.3.3

dopamine + secologanin = (1S)-deacetylisoipecoside + H2O

247116

-

4.3.3.4

dopamine + secologanin = (1R)-deacetylipecoside + H2O

247118, 247116

-

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

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Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.8.2.1

adenosine 3',5'-bisphosphate + dopamine sulfate = 3'-phosphoadenylyl sulfate + dopamine

0

2a3r, 3D-view

4.1.1.25

L-Dopa = dopamine + CO2

0

-

4.1.1.28

3,4-Dihydroxyphenylalanine = Dopamine + CO2

0

-

4.1.1.28

L-3,4-Dihydroxyphenylalanine = Dopamine + CO2

0

-

4.1.1.28

L-Dopa = dopamine + CO2

0, 653366

-

4.1.1.28

3 entries

Substrate in Enzyme-catalyzed Reactions (93 results)

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Show Substrate (93 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

2 dopamine + O2 = 2 4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O

686666, 696393

-

1.10.3.1

dopamine + 1/2 O2 = dopamine quinone + H2O

674774

-

1.10.3.1

dopamine + O2 = 4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O

440427, 440433, 440437, 440426

-

1.10.3.1

dopamine + O2 = ?

675458, 674142, 676649, 671593, 727645, 675076, 673779, 701760

-

1.10.3.1

dopamine + O2 = dopaminequinone + H2O

686692

-

1.10.3.2

4-(2-aminoethyl)benzene-1,2-diol + O2 = ?

724662

-

1.10.3.2

dopamine + O2 = ?

712159, 724417

-

1.10.3.1

5 entries

1.10.3.2

2 entries

1.11.1.19

dopamine + H2O2 + H+ = ?

765206

-

1.11.2.2

dopamine + H2O2 = ? + H2O

659636

-

1.14.17.1

3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O

438631, 438632, 674660, 438600, 438589, 438597, 438601, 438604, 438614, 438624, 438634, 438602, 438598, 438633, 438636, 438599, 438606, 438607, 438608, 438610, 438611, 438612, 438613, 438615, 438616, 438617, 438618, 438619, 438620, 438621, 438627, 438629, 438626, 438609, 438630, 438603

-

1.14.17.1

dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O

660336, 659287, 728562, 744851, 745892, 746431, 744598, 744949, 744950

-

1.14.17.1

dopamine + ascorbate + O2 = norepinephrine + dehydroascorbate + H2O

727633

-

1.14.17.1

dopamine + D-araboascorbic acid + O2 = ?

438630

-

1.14.17.1

dopamine + D-xyloascorbic acid + O2 = ?

438630

-

1.14.17.1

dopamine + L-araboascorbic acid + O2 = ?

438630

-

1.14.18.1

3,4-dihydroxyphenethylamine + O2 = ?

636402

-

1.14.18.1

dopamine + 1/2 O2 = dopamine quinone + H2O

636393, 636375, 636403, 636452, 686774, 658626, 684423, 688046, 685662, 636353, 659827, 689385, 688438

-

1.14.18.1

dopamine + 1/2 O2 = dopaminequinone + H2O

687250

-

1.14.18.1

dopamine + O2 = ?

674108, 697659, 744015, 674092, 673090, 713302, 745746, 746472

-

1.14.18.1

dopamine + O2 = dopamine quinone + H2O

744015, 636439

-

1.14.99.54

xylan + dopamine + O2 = C1/C4-oxidized oxidized xylo-oligosaccharides + 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O

740210

-

1.14.99.54

xylan + dopamine + O2 = C1/C4-oxidized xylooligosaccharides + 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O

740207

-

1.14.17.1

6 entries

1.14.18.1

5 entries

1.14.99.54

2 entries

1.14.99.56

cellulose + dopamine + O2 = C4-oxidized gluco-oligosaccharides + 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O

740210

-

1.16.3.1

3,4-dihydroxyphenethylamine + Fe2+ + O2 = ?

438006

-

1.4.3.21

dopamine + H2O + O2 = (3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2

725733

-

1.4.3.21

dopamine + H2O + O2 = ?

726290

-

1.4.3.22

2-(3,4-dihydroxyphenyl)-ethylamine + H2O + O2 = 3,4-dihydroxyphenylacetaldehyde + NH3 + H2O2

391951

-

1.4.3.22

dopamine + H2O + O2 = 2-(3,4-dihydroxyphenyl)ethanal + NH3 + H2O2

656323, 672497

-

1.4.3.4

dopamine + H2O + O2 = (3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2

705940, 394553, 394560, 394566, 394562, 394569, 391951, 742990, 742989, 724786, 394552, 672530, 742919, 675073, 394580

-

1.4.3.4

dopamine + H2O + O2 = ?

711407, 711912

-

1.4.9.2

dopamine + acceptor + H2O = 4-(2-oxoethyl)-1,2-benzenediol + NH3 + reduced acceptor

396589, 396594, 396591

-

1.4.9.2

dopamine + H2O + 2,6-dichlorophenol indophenol = (3,4-dihydroxyphenyl)acetaldehyde + NH3 + reduced 2,6-dichlorophenol indophenol

655062

-

1.4.3.21

2 entries

1.4.3.22

2 entries

1.4.3.4

2 entries

1.4.9.2

2 entries

1.6.3.5

dopamine + O2 = ?

743215

-

2.1.1.28

dopamine + S-adenosyl-L-methionine = ? + S-adenosyl-L-homocysteine

639447

-

2.1.1.336

2 S-adenosyl-L-methionine + dopamine = 2 S-adenosyl-L-homocysteine + 4-O-methyldopamine + 3-O-methyldopamine

756959

-

2.1.1.336

S-adenosyl-L-methionine + dopamine = ?

741290

-

2.1.1.6

3-hydroxytyramine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + 3-methoxytyramine

703190

-

2.1.1.6

dopamine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + 3-O-methyldopamine

705926

-

2.1.1.6

dopamine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + ?

441507, 441524, 441544, 441546, 733309, 686075

-

2.1.1.6

S-adenosyl-L-methionine + dopamine = S-adenosyl-L-homocysteine + 3-methoxytyramine

441532

-

2.1.1.6

S-adenosyl-L-methionine + dopamine = S-adenosyl-L-homocysteine + 3-O-methyldopamine

758546

-

2.1.1.6

S-adenosyl-L-methionine + dopamine = S-adenosyl-L-homocysteine + ?

686194, 658517

-

2.1.1.336

2 entries

2.1.1.6

6 entries

2.3.1.110

feruloyl-CoA + dopamine = CoA + feruloyldopamine

486130, 486126, 486127, 486132, 486134, 676598, 660244

-

2.3.1.5

acetyl-CoA + hydroxytyramine = CoA + ?

487116

-

2.3.1.87

acetyl-CoA + 2-(3,4-dihydroxyphenyl)-ethylamine = CoA + N-acetyl-2-(3,4-dihydroxyphenyl)-ethylamine

660441

-

2.3.1.87

acetyl-CoA + dopamine = CoA + N-acetyldopamine

735681, 686212, 719595, 758432, 720470, 672840, 673165, 736685, 735981, 756913

-

2.3.1.87

butanoyl-CoA + dopamine = CoA + N-butanoyldopamine

736107

-

2.4.1.17

UDP-alpha-D-glucuronate + dopamine = UDP + dopamine 3-O-beta-D-glucopyranosiduronic acid

703419

-

2.4.1.17

UDP-alpha-D-glucuronate + dopamine = UDP + dopamine 4-O-beta-D-glucopyranosiduronic acid

703419

-

2.4.1.17

UDP-glucuronate + dopamine = UDP + dopamine beta-D-glucuronoside

735649

-

2.3.1.87

3 entries

2.4.1.17

3 entries

2.7.11.22

ATP + dopamine = ADP + phosphorylated dopamine

666401

-

2.8.2.1

2 3'-phosphoadenylyl sulfate + 2 dopamine = 2 adenosine 3',5'-bisphosphate + dopamine 3-O-sulfate + dopamine 4-O-sulfate

671928

2a3r, 3D-view

2.8.2.1

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + ?

675515, 675751, 760663, 672630, 702738

2a3r, 3D-view

2.8.2.1

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopamine sulfate

723935, 672630, 760968, 671885, 760542, 671573, 671776

2a3r, 3D-view

2.8.2.1

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopaminyl sulfate

726515

2a3r, 3D-view

2.8.2.1

3'-phosphoadenylylsulfate + dopamine = adenosine 3',5'-bisphosphate + ?

702031, 645649, 645651, 645655, 645658, 645659, 645662, 645642, 645644, 645641, 645663, 645688, 645668, 645654, 645671, 645682, 645680, 645664, 645684, 645686, 645669, 645653, 645666, 645675, 645677, 645678, 645660, 663431, 662207, 662515, 660916, 660962

2a3r, 3D-view

2.8.2.2

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopamine sulfate

760542

-

2.8.2.2

3'-phosphoadenylylsulfate + dopamine = adenosine 3',5'-bisphosphate + ?

662862

-

2.8.2.22

4-nitrophenyl sulfate + dopamine = 4-nitrophenol + ?

723897

-

2.8.2.22

4-nitrophenyl sulfate + dopamine = ? + 4-nitrophenol

645841

-

2.8.2.3

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopamine sulfamate

690752

-

2.8.2.3

3'-phosphoadenylylsulfate + dopamine = adenosine 3',5'-bisphosphate + N-sufodopamine

645860

-

2.8.2.4

3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopamine sulfate

760542

-

2.8.2.4

3'-phosphoadenylylsulfate + dopamine = adenosine 3',5'-bisphosphate + dopamine sulfate

645891, 645902

-

2.8.2.1

5 entries

2.8.2.2

2 entries

2.8.2.22

2 entries

2.8.2.3

2 entries

2.8.2.4

2 entries

2.8.2.9

3'-phosphoadenylylsulfate + dopamine = adenosine 3',5'-bisphosphate + ?

644817, 644826, 702031

-

3.2.1.8

dopamine + H2O = ?

696821

-

4.1.1.28

dopamine + O2 = 3,4-dihydroxyphenylacetaldehyde + NH3

650410

-

4.2.1.78

4-(2-aminoethyl)benzene-1,2-diol + (3,4-dihydroxyphenyl)acetaldehyde = ?

678219

2vq5, 3D-view

4.2.1.78

4-(2-aminoethyl)benzene-1,2-diol + 3,4-dihydroxyphenylacetaldehyde = (S)-norlaudanosoline + H2O

5894, 5895, 652296

2vq5, 3D-view

4.2.1.78

4-(2-Aminoethyl)benzene-1,2-diol + 4-hydroxyphenylacetaldehyde = (S)-Norcoclaurine + H2O

5895, 678219, 690826, 690258, 693259, 5894, 653569, 652296, 682682, 680879

2vq5, 3D-view

4.2.1.78

4-(2-Aminoethyl)benzene-1,2-diol + 4-hydroxyphenylacetaldehyde = ?

5894

2vq5, 3D-view

4.2.1.78

4-hydroxyphenylacetaldehyde + 4-(2-aminoethyl)benzene-1,2-diol = (S)-norcoclaurine + H2O

716518, 715141

2vq5, 3D-view

4.2.1.78

(2-fluorophenyl)acetaldehyde + dopamine = (1S)-1-[2-(2-fluorophenyl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

(2-methylphenyl)acetaldehyde + dopamine = (1S)-1-[2-(2-methylphenyl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

(3,4-dimethoxyphenyl)acetaldehyde + dopamine = (1S)-1-[2-(3,4-dimethoxyphenyl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

(3-fluorophenyl)acetaldehyde + dopamine = (1S)-1-[2-(3-fluorophenyl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

(3-methylphenyl)acetaldehyde + dopamine = (1S)-1-[2-(3-methylphenyl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

(4-fluorophenyl)acetaldehyde + dopamine = (1S)-1-[2-(4-fluorophenyl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

(4-methoxyphenyl)acetaldehyde + dopamine = (1S)-1-[2-(4-methoxyphenyl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

(4-methylphenyl)acetaldehyde + dopamine = (1S)-1-[2-(4-fluorophenyl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

(5,5-dimethyl-1,3-dioxan-2-yl)acetaldehyde + dopamine = (1S)-1-[2-(5,5-dimethyl-1,3-dioxan-2-yl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

1-butylaldehyde + dopamine = 6,7-dihydroxy-1-propyl-1,2,3,4-tetrahydroisoquinoline

747310

2vq5, 3D-view

4.2.1.78

3,3-dimethylbutanal + dopamine = (1S)-1-(3,3-dimethylbutyl)-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

4-hydroxyphenylacetaldehyde + dopamine = (S)-norcoclaurine + H2O

729604, 749327, 728793, 747372, 747310, 730988

2vq5, 3D-view

4.2.1.78

4-hydroxyphenylacetone + dopamine = 1-(4-hydroxybenzyl)-1-methyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol

748745

2vq5, 3D-view

4.2.1.78

cyclohexylacetaldehyde + dopamine = (1S)-1-(2-cyclohexylethyl)-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

hydrocinnamaldehyde + dopamine = 6,7-dihydroxy-1-phenethyl-1,2,3,4-tetrahydroisoquinoline

747310

2vq5, 3D-view

4.2.1.78

naphthalen-1-ylacetaldehyde + dopamine = (1S)-1-[2-(naphthalen-1-yl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

phenylacetaldehyde + dopamine = (1S)-1-(2-phenylethyl)-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

thiophen-3-ylacetaldehyde + dopamine = (1S)-1-[2-(thiophen-3-yl)ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

[4-(trifluoromethoxy)phenyl]acetaldehyde + dopamine = (1S)-1-[2-[4-(trifluoromethoxy)phenyl]ethyl]-1,2,3,4-tetrahydroisoquinoline-6,7-diol + H2O

730988

2vq5, 3D-view

4.2.1.78

24 entries

4.3.3.3

dopamine + secologanin = (1S)-deacetylisoipecoside + H2O

247116

-

4.3.3.4

dopamine + secologanin = (1R)-deacetylipecoside + H2O

247116, 247118

-

Product in Enzyme-catalyzed Reactions (21 results)

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Show Product (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.2.6

tyramine + H2O2 = dopamine + H2O

0

-

1.14.14.9

tyramine + FMNH + O2 = dopamine + FMN + H2O

0

-

1.14.16.2

tyramine + tetrahydrobiopterin + O2 = dopamine + 4a-hydroxytetrahydrobiopterin

0

6zn2, 3D-view

1.14.16.2

tyramine + tetrahydrobiopterin + O2 = dopamine + 4a-hydroxytetrahydrobiopterin

0

6zvp, 3D-view

1.14.16.2

tyramine + tetrahydrobiopterin + O2 = dopamine + 4a-hydroxytetrahydrobiopterin

0

7pim, 3D-view

1.14.16.2

3 entries

1.14.18.1

tyramine + O2 = dopamine + H2O

0

-

1.14.99.54

cellulose + oxidized dopamine + O2 = C1-oxidized gluco-oligosaccharides + glucooligosaccharides + dopamine + H2O

0

-

2.8.2.1

adenosine 3',5'-bisphosphate + dopamine sulfate = 3'-phosphoadenylyl sulfate + dopamine

0

2a3r, 3D-view

3.1.6.1

dopamine 3-sulfate + H2O = dopamine + sulfate

0

-

3.1.6.1

dopamine 4-sulfate + H2O = dopamine + sulfate

0

-

3.1.6.1

2 entries

4.1.1.22

3,4-Dihydroxyphenylalanine = Dopamine + CO2

0

-

4.1.1.25

L-3,4-Dihydroxyphenylalanine = Dopamine + CO2

0

-

4.1.1.25

L-Dopa = dopamine + CO2

653443, 0, 653473, 653346, 651348, 653447

-

4.1.1.28

3,4-Dihydroxyphenylalanine = 3-Hydroxytyramine + CO2

0, 4201

-

4.1.1.28

3,4-dihydroxyphenylalanine = 4-(2-aminoethyl)benzene-1,2-diol + CO2

653346

-

4.1.1.28

L-(3,4-dihydroxyphenyl)alanine = 4-(2-aminoethyl)benzene-1,2-diol + CO2

649601

-

4.1.1.28

3,4-Dihydroxyphenylalanine = Dopamine + CO2

0, 650436

-

4.1.1.28

DOPA = dopamine + CO2

651068

-

4.1.1.28

L-3,4-Dihydroxyphenylalanine = Dopamine + CO2

0

-

4.1.1.28

L-Dopa = dopamine + CO2

0, 653443, 653352, 653356, 651417, 653366, 649696, 650410

-

4.1.1.25

2 entries

4.1.1.28

7 entries

4.1.1.53

3,4-Dihydroxyphenylalanine = Dopamine + CO2

0

-

Activator in Enzyme-catalyzed Reactions (12 results)

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Show Activating Compound (12 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.99.1

-

438392

-

1.14.99.1

3,4-dihydroxyphenylethylamine, stimulates

438389

-

1.14.99.1

2 entries

2.6.1.5

slight activation

640113

-

3.1.4.11

small stimulatory effect of about 30% on the enzyme acting on PtdIns(4,5)P2. GTPgammaS enhances this effect

653351

-

4.2.1.1

-

696635, 696648, 702675

-

4.2.1.1

activation constant of 0.0276 mM

702616

-

4.2.1.1

high activator

729371

-

4.6.1.1

140% activation at 0.1 mM, activation in hippocampus and striatum, the stimulation is partially inhibited, up to 48%, by oxotremorine, inhibition of stimulation is blocked by muscarinic toxin MT3, purified from Dendroaspis angusticeps snake venom, overview

694363

-

4.6.1.1

a dopamine receptor agonist, the activation by can be reversed by D1-receptor antagonists SCH23390, SKF83566, and butaclamol

693830

-

4.6.1.1

about 2fold activation by 0.1 mM

709677

-

4.6.1.1

activation

34771

-

4.2.1.1

3 entries

4.6.1.1

4 entries

6.3.3.2

0.02 mM, increases the initial rapid phase of folate turnover by 4%

671613

-

Inhibitor in Enzyme-catalyzed Reactions (65 results)

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Show Inhibitors (65 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.153

slight; slight inhibition

286023

-

1.1.1.75

noradrenalin

287299

-

1.10.3.1

at high dopamine concentration, a decrease in activity is observed, indicating substrate inhibition

686692

-

1.10.3.1

dopamine produces substrate inhibition above 2 mM

696393

-

1.10.3.1

2 entries

1.14.11.4

-

439156

-

1.14.16.1

-

438714, 438719

5pah, 3D-view

1.14.16.1

0.025 mM, 50% inhibition

438655

5pah, 3D-view

1.14.16.1

0.5 mM, approx. 40% inhibition

438733

5pah, 3D-view

1.14.16.2

-

438688, 438691, 671818, 688523, 699645, 714235, 727798, 745893

6zn2, 3D-view

1.14.16.2

-

438688, 438691, 671818, 688523, 699645, 714235, 727798, 745893

6zvp, 3D-view

1.14.16.2

-

438688, 438691, 671818, 688523, 699645, 714235, 727798, 745893

7pim, 3D-view

1.14.16.2

1.8% residual activity at 0.01 mM

745240

6zn2, 3D-view

1.14.16.2

1.8% residual activity at 0.01 mM

745240

6zvp, 3D-view

1.14.16.2

1.8% residual activity at 0.01 mM

745240

7pim, 3D-view

1.14.16.2

binding kinetics and regulatory function, overview, phosphorylation of Ser40 abolishes the binding of dopamine to a high affinity site on the enzyme, thereby increasing the activity of the enzyme. Binding of dopamine to the high-affinity site also decreases Vmax and increases the Km for the cofactor tetrahydrobiopterin, while binding of dopamine to the low affinity site regulates tyrosine hydroxylase activity by increasing the Km for tetrahydrobiopterin

688519

6zn2, 3D-view

1.14.16.2

binding kinetics and regulatory function, overview, phosphorylation of Ser40 abolishes the binding of dopamine to a high affinity site on the enzyme, thereby increasing the activity of the enzyme. Binding of dopamine to the high-affinity site also decreases Vmax and increases the Km for the cofactor tetrahydrobiopterin, while binding of dopamine to the low affinity site regulates tyrosine hydroxylase activity by increasing the Km for tetrahydrobiopterin

688519

6zvp, 3D-view

1.14.16.2

binding kinetics and regulatory function, overview, phosphorylation of Ser40 abolishes the binding of dopamine to a high affinity site on the enzyme, thereby increasing the activity of the enzyme. Binding of dopamine to the high-affinity site also decreases Vmax and increases the Km for the cofactor tetrahydrobiopterin, while binding of dopamine to the low affinity site regulates tyrosine hydroxylase activity by increasing the Km for tetrahydrobiopterin

688519

7pim, 3D-view

1.14.16.2

binds to the iron ion at the active site

686696

6zn2, 3D-view

1.14.16.2

binds to the iron ion at the active site

686696

6zvp, 3D-view

1.14.16.2

binds to the iron ion at the active site

686696

7pim, 3D-view

1.14.16.2

competitive

659762

6zn2, 3D-view

1.14.16.2

competitive

659762

6zvp, 3D-view

1.14.16.2

competitive

659762

7pim, 3D-view

1.14.16.2

end product inhibition

690099

6zn2, 3D-view

1.14.16.2

end product inhibition

690099

6zvp, 3D-view

1.14.16.2

end product inhibition

690099

7pim, 3D-view

1.14.16.2

feedback inhibition, in the presence of 0.02 mM dopamine tyrosine hydroxylase enzyme specific activity is reduced by about 60%

698830

6zn2, 3D-view

1.14.16.2

feedback inhibition, in the presence of 0.02 mM dopamine tyrosine hydroxylase enzyme specific activity is reduced by about 60%

698830

6zvp, 3D-view

1.14.16.2

feedback inhibition, in the presence of 0.02 mM dopamine tyrosine hydroxylase enzyme specific activity is reduced by about 60%

698830

7pim, 3D-view

1.14.16.2

feedback inhibitor and catecholamine product, binding inhibits and stabilizes the enzyme, reversible and competitive inhibition with respect to tetrahydrobiopterin

688521

6zn2, 3D-view

1.14.16.2

feedback inhibitor and catecholamine product, binding inhibits and stabilizes the enzyme, reversible and competitive inhibition with respect to tetrahydrobiopterin

688521

6zvp, 3D-view

1.14.16.2

feedback inhibitor and catecholamine product, binding inhibits and stabilizes the enzyme, reversible and competitive inhibition with respect to tetrahydrobiopterin

688521

7pim, 3D-view

1.14.16.2

feedback inhibitor, competitively with tetrahydrobiopterin

713957

6zn2, 3D-view

1.14.16.2

feedback inhibitor, competitively with tetrahydrobiopterin

713957

6zvp, 3D-view

1.14.16.2

feedback inhibitor, competitively with tetrahydrobiopterin

713957

7pim, 3D-view

1.14.16.4

-

438661

-

1.14.16.4

0.022 mM, 50% inhibition

438673

-

1.14.16.4

50% inhibition at 32 microM

675511

-

1.14.16.4

noncompetitive vs. L-tryptophan and (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin

438669

-

1.14.16.1

3 entries

1.14.16.2

27 entries

1.14.16.4

4 entries

1.14.18.1

10% inhibition at 0.1 mM

672587

-

1.17.3.2

23% inhibition at 1 mM and at 0.1 mM

654034

-

1.2.3.1

0.1 mM, 80% and 93% inhibition of phenanthridine and N-methylphthalazine oxidation, respectively; 0.1 mM and 1 mM, 59% and 100% inhibition of benzaldehyde oxidation, respectively

654034

-

1.4.3.21

-

725733

-

1.4.9.2

substrate inhibition at higher concentrations

655062

-

1.5.1.34

-

484984

-

1.5.1.34

0.1 mM, 50% inhibition

484973

-

1.5.1.34

no inhibition below 0.2 mM

484978

-

1.5.1.34

noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine

484988

-

1.5.1.34

4 entries

1.8.1.7

competitive

742814

-

2.1.1.28

competitive inhibition with respect to phenylethanolamine

639447

-

2.1.1.6

competitive to dobutamine

441544

-

2.6.1.5

100% inhibition with tyrosine at 3 mM and dopamine at 12 mM

640109

-

2.7.1.35

-

641414

-

2.7.1.35

0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 52% inhibition

641424

-

2.8.2.1

substrate inhibition at concentrations higher than 0.03 mM

723935

2a3r, 3D-view

2.8.2.1

substrate inhibition at high concentrations, SULT1A3; wild-type enzyme SULT1A1 shows no substrate inhibition, mutant enzyme F247L shows substrate inhibition

662207

2a3r, 3D-view

2.8.2.1

substrate inhibition, enzyme form SULT1D1

660962

2a3r, 3D-view

2.7.1.35

2 entries

2.8.2.1

3 entries

3.1.3.1

0.1 mM

665873

-

3.1.6.1

-

135516, 135519

-

4.1.1.15

-

3980

-

4.1.1.28

-

4204, 4208, 705269

-

4.1.1.28

complete inhibition at 0.5 mM

743978

-

4.1.1.28

the conversion of 5-hydroxy-L-tryptophan is strongly inhibited by dopamine

681948

-

4.1.1.28

3 entries

6.3.2.18

effective inhibitor, 1 mM inhibits Nalpha-gamma-L-glutamylhistamine synthesis by 84%

1102

-

7.2.2.13

negative modulator

677134

-

3D Structure of Enzyme-Ligand-Complex (PDB) (79 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (79 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.10.99.2

2qmz, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

4dtz, 3D-view

1.14.14.1

4du2, 3D-view

1.14.14.1

4dub, 3D-view

1.14.14.1

36 entries

1.14.16.1

5pah, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

6zn2, 3D-view

1.14.16.2

6zvp, 3D-view

1.14.16.2

7pim, 3D-view

1.14.16.2

36 entries

1.15.1.1

4a7v, 3D-view

1.5.3.5

3nk2, 3D-view

2.8.2.1

2a3r, 3D-view

4.1.1.86

7cwz, 3D-view

4.2.1.78

2vq5, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (54 results)

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Show Turnover Number (54 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.10.3.1

4.9

-

-

686666

1.10.3.1

5.7

-

at substrate concentrations above 4 mM, substrate inhibition is observed and the data are fitted to a simple model for substrate inhibition. KM, kcat and KI are obtained for the inhibitory binding site

686692

1.10.3.1

6

-

substrate range 0.3-4 mM

686692

1.10.3.1

29.9

-

pH 6.8, 10°C, in methanol-glycerol cryosolvent

673090

1.10.3.1

133.2

-

pH 6.8, 25°C, in methanol-glycerol cryosolvent

673090

1.10.3.1

282

-

pH 6.5, 25°C

675076

1.10.3.1

439

-

-

675458

1.10.3.1

439

-

pH 6.8, 25°C, in aqueous buffer

673090

1.10.3.1

439

-

pH 7.0

674142

1.10.3.1

875

-

-

675458

1.10.3.1

1350

-

-

675458

1.10.3.2

4.4

-

pH 5.0, 25°C

724417

1.10.3.2

116

-

pH 5.0, 25°C

724417

1.10.3.2

184

-

pH 5.0, 25°C

724417

1.10.3.2

186

-

pH 5.0, 25°C

724417

1.11.2.2

0.0000001

-

25°C, pH 5.5

659636

1.11.2.2

0.0000016

-

25°C, pH 5.5

659636

1.14.17.1

13

-

-

438620

1.14.17.1

110

-

-

438616

1.14.18.1

29.9

-

pH 6.8, 10°C, in methanol-glycerol cryosolvent

673090

1.14.18.1

61

-

recombinant enzyme, pH 7.2, 37°C

745746

1.14.18.1

133.2

-

pH 6.8, 25°C, in methanol-glycerol cryosolvent

673090

1.14.18.1

135

-

inhibitor is phenylthiourea

689385

1.14.18.1

144

-

inhibitor is mimosine

689385

1.14.18.1

210

-

recombinant enzyme, pH 7.2, 37°C

745746

1.14.18.1

433

-

pH 6.8, 25°C, in methanol-glycerol cryosolvent

673090

1.14.18.1

439

-

-

636439

1.14.18.1

439

-

pH 6.8, 25°C, in aqueous buffer

673090

1.14.18.1

1590

-

-

685662

1.14.18.1

2540

-

pH 6.8, 25°C, recombinant enzyme

746472

1.4.3.21

0.54

-

at pH 7.4, 37°C

726290

1.4.3.21

1.9

-

isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.10.3.1

11 entries

1.10.3.2

4 entries

1.11.2.2

2 entries

1.14.17.1

2 entries

1.14.18.1

11 entries

1.4.3.21

2 entries

1.4.3.22

135

-

-

391951

1.4.3.4

0.249

-

11°C

394552

1.4.3.4

4.03

-

at 25°C in 50 mM potassium phosphate, pH 7.4

724786

1.4.9.2

9.1

-

-

396594

1.4.9.2

27.1

-

-

396594

1.4.3.4

2 entries

1.4.9.2

2 entries

2.1.1.336

0.06

-

at pH 8.8 and 37°C

741290

2.1.1.6

0.088

-

S-COMT, 0.1 mM S-adenosyl-L-methionine

686075

2.1.1.6

0.19

-

MB-COMT, 0.1 mM S-adenosyl-L-methionine

686075

2.3.1.87

2.8

-

cosubstrate acetyl-CoA, pH 7.0, 25°C

758432

2.3.1.87

3.65

-

pH 7.3, 22°C, recombinant aaNAT2

719595

2.3.1.87

7.3

-

pH 7.3, 22°C, recombinant aaNAT1

719595

2.3.1.87

21

-

wild-type, pH 8.0, 22°C

735681

2.8.2.1

0.028

-

mutant enzyme D247L, enzyme form SULT1D1

660962

2.8.2.1

0.09

-

mutant enzyme O86D, enzyme form SULT1D1

660962

2.8.2.1

0.18

-

wild-type enzyme, enzyme form SULT1D1

660962

2.1.1.6

2 entries

2.3.1.87

4 entries

2.8.2.1

3 entries

2.8.2.9

0.07

-

pH 5.5, 37°C

644817

4.1.1.28

0.7

-

mutant enzyme K303A, in 50 mM HEPES, pH 7.5, at 25°C

701921

4.1.1.28

2.48

-

wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C

701921

4.2.1.78

2.4

-

pH 7.3, 37°C

749327

4.2.1.78

5.8

-

pH 7.3, 37°C

749327

4.2.1.78

6.4

-

cosubstrate: 4-(2-aminoethyl)benzene-1,2-diol

678219

4.2.1.78

7

-

cosubstrate: (3,4-dihydroxyphenyl)acetaldehyde

678219

4.1.1.28

2 entries

4.2.1.78

4 entries

K_M Value (140 results)

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Show KM Value (140 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.10.3.1

0.181

-

SDS-activated hemocyanin

696393

1.10.3.1

0.28

-

-

675458

1.10.3.1

0.427

-

pH 6.5, 25°C

675076

1.10.3.1

0.6

-

pH 6.5, 25°C

676649

1.10.3.1

0.72

-

pH 7.0

674142

1.10.3.1

1.22

-

at substrate concentrations above 4 mM, substrate inhibition is observed and the data are fitted to a simple model for substrate inhibition. KM, kcat and KI are obtained for the inhibitory binding site

686692

1.10.3.1

1.45

-

substrate range 0.3-4 mM

686692

1.10.3.1

1.5

-

-

686666

1.10.3.1

2.2

-

-

675458

1.10.3.1

2.8

-

-

440433

1.10.3.1

11.9

-

-

675458

1.10.3.2

0.006

-

pH 5.0, 25°C

724417

1.10.3.2

0.17

-

pH 5.0, 25°C

724417

1.10.3.2

0.29

-

pH 5.0, 25°C

724417

1.10.3.2

2.1

-

pH 5.0, 25°C

724417

1.11.2.2

0.64

-

25°C, pH 5.5

659636

1.11.2.2

136.3

-

25°C, pH 5.5

659636

1.14.17.1

0.2

-

-

438603

1.14.17.1

1

-

-

438620

1.14.18.1

0.047

-

-

636402

1.14.18.1

0.11

-

-

636353

1.14.18.1

0.2

-

soluble enzyme

684423

1.14.18.1

0.25

-

-

636393

1.14.18.1

0.39

-

pH 6.8, 25°C, ST94t

658626

1.14.18.1

0.4

-

pH 6.8, 10°C, in methanol-glycerol cryosolvent

673090

1.14.18.1

0.67

-

using tyrosinase immobilized on eggshell membrane. Km is 0.67 mM and Vmax 0.08 mM min-1. Increase in Km (compared to soluble enzyme for which Km is 0.20 mM) indicate that the affinity of enzyme for substrate has decreased to some extent after immobilization, which may be due to glutaraldehyde treatment

684423

1.14.18.1

0.84

-

in 0.1 M sodium phosphate buffer (pH 7.0) at 25°C

697659

1.14.18.1

0.892

-

pH 8.5, 42°C

659827

1.14.18.1

0.93

-

pH 6.8, 25°C, in methanol-glycerol cryosolvent

673090

1.14.18.1

1.09

-

-

636375

1.14.18.1

1.3

-

pH 6.8, 25°C, ST94

658626

1.14.18.1

1.67

-

calculated from the Lineweaver-Burk graphs for substrates

688046

1.14.18.1

2.2

-

-

636439

1.14.18.1

2.2

-

pH 6.8, 25°C, in aqueous Hepes buffer

673090

1.14.18.1

3.4

-

inhibitor is phenylthiourea

689385

1.14.18.1

4.2

-

inhibitor is mimosine

689385

1.14.18.1

8.4

-

-

688438

1.14.18.1

11

-

in 0.1M sodium phosphate buffer (pH 7.0) at 25°C

697659

1.14.18.1

15.2

-

pH 6.8, 25°C, recombinant enzyme

746472

1.14.18.1

16

-

recombinant enzyme, pH 7.2, 37°C

745746

1.14.18.1

50

-

recombinant enzyme, pH 7.2, 37°C

745746

1.14.18.1

122

-

-

685662

1.10.3.1

11 entries

1.10.3.2

4 entries

1.11.2.2

2 entries

1.14.17.1

2 entries

1.14.18.1

23 entries

1.16.3.1

0.00285

-

-

438006

1.4.3.21

0.099

-

at pH 7.4, 37°C

726290

1.4.3.21

0.1

-

isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.21

2 entries

1.4.3.22

0.6

-

-

391951

1.4.3.4

0.088

-

at 25°C in 50 mM potassium phosphate, pH 7.4

724786

1.4.3.4

0.111

-

-

394560

1.4.3.4

0.405

-

-

394562

1.4.3.4

1.36

-

11°C

394552

1.4.3.4

4.3

-

at pH 7.4 and 25°C

742990

1.4.3.4

4.71

-

at pH 7.4 and 25°C

742989

1.4.9.2

0.13

-

-

396594

1.4.9.2

0.292

-

-

396594

1.4.3.4

6 entries

1.4.9.2

2 entries

2.1.1.336

0.0073

-

at pH 8.8 and 37°C

741290

2.1.1.6

0.0005

-

-

441532

2.1.1.6

0.0033

-

-

441524

2.1.1.6

0.0033

-

membrane-bound enzyme form, brain

686194

2.1.1.6

0.015

-

recombinant enzyme expressed in Sf9 cells, membrane-bound enzyme form

686194

2.1.1.6

0.017

-

MB-COMT, 0.1 mM S-adenosyl-L-methionine

686075

2.1.1.6

0.207

-

recombinant enzyme expressed in Sf9 cells, soluble enzyme form

686194

2.1.1.6

0.2632

-

S-COMT, 0.1 mM S-adenosyl-L-methionine

686075

2.1.1.6

0.28

-

soluble enzyme form, brain

686194

2.1.1.6

0.44

-

-

441544

2.3.1.110

0.078

-

-

486134

2.3.1.110

0.202

-

-

486132

2.3.1.110

0.34

-

with feruloyl-CoA as acceptor

486130

2.3.1.110

0.721

-

pH 8.5, 30°C

660244

2.3.1.110

0.779

-

30°C, pH 8.5, recombinant enzyme

676598

2.1.1.6

9 entries

2.3.1.110

5 entries

2.3.1.5

0.71

0.72

-

487116

2.3.1.87

0.11

-

pH not specified in the publication, temperature not specified in the publication

756913

2.3.1.87

0.17

-

wild-type, pH 8.0, 22°C

735681

2.3.1.87

0.19

-

pH 7.3, 22°C, recombinant aaNAT1

719595

2.3.1.87

0.27

-

pH 7.3, 22°C, recombinant aaNAT2

719595

2.3.1.87

0.33

-

-

672840

2.3.1.87

0.48

-

-

672840

2.3.1.87

1.76

-

pH 6.8, 37°C

660441

2.3.1.87

11

-

cosubstrate acetyl-CoA, pH 7.0, 25°C

758432

2.4.1.17

1.89

-

formation of dopamine-4-O-glucuronide, mutant F90A

703419

2.4.1.17

1.95

-

formation of dopamine-4-O-glucuronide, wild-type

703419

2.4.1.17

1.99

-

formation of dopamine-3-O-glucuronide, mutant F90A

703419

2.4.1.17

2.19

-

formation of dopamine-3-O-glucuronide, wild-type

703419

2.4.1.17

2.31

-

formation of dopamine-3-O-glucuronide, mutant F90L

703419

2.4.1.17

2.59

-

formation of dopamine-4-O-glucuronide, mutant F90L

703419

2.4.1.17

2.63

-

formation of dopamine-4-O-glucuronide, mutant F93A

703419

2.4.1.17

2.67

-

formation of dopamine-3-O-glucuronide, mutant F93L

703419

2.4.1.17

2.91

-

formation of dopamine-3-O-glucuronide, mutant F93A

703419

2.4.1.17

3.11

-

formation of dopamine-4-O-glucuronide, mutant F93L

703419

2.8.2.1

0.00065

-

wild-type SULT1A3: purified recombinant enzyme from Escherichia coli, pH 7.4, 37°C

645670

2.8.2.1

0.00094

-

wild-type SULT1A3: recombinant from V79 cells, pH 7.4, 37°C

645670

2.8.2.1

0.001

-

wild-type SULT1A3: native enzyme, and recombinant from COS-7 cells, Escherichia coli, Saccharomyces cerevisiae, pH 7.4, 37°C

645670

2.8.2.1

0.0014

-

recombinant wild-type M-PST, pH 7.0, 37°C

645669

2.8.2.1

0.0022

-

dopamine 4-O-sulfate formation, recombinant SULT1A3

671928

2.8.2.1

0.0022

-

wild-type SULT1A3, pH 7.4, 37°C

645668

2.8.2.1

0.0026

-

dopamine 3-O-sulfate formation, recombinant SULT1A3

671928

2.8.2.1

0.0029

-

M-PST, pH 7.0, 37°C

645658

2.8.2.1

0.0036

-

wild-type enzyme, enzyme form SULT1D1

660962

2.8.2.1

0.0053

-

isoform SULT1A3, 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

702138

2.8.2.1

0.0056

-

SULT1A3 mutant H143Y, pH 7.4, 37°C

645668

2.8.2.1

0.0062

-

isoenzyme B, pH 9.5, 37°C

645641

2.8.2.1

0.0065

-

SULT1A3, pH 7.0, 37°C

671885

2.8.2.1

0.0068

-

at pH 7.0 and 37°C

723935

2.8.2.1

0.007

-

pH 7.0, 37°C, SULT1A3

675515

2.8.2.1

0.0071

-

SULT1A3, pH 6.5, 37°C

645678

2.8.2.1

0.0097

-

recombinant isozyme M-PST, i.e. HAST3

645655

2.8.2.1

0.011

-

-

645662

2.8.2.1

0.014

-

ST1A5, pH 7.4, 37°C

645680

2.8.2.1

0.0177

-

isoenzyme A, pH 6.0, 37°C

645641

2.8.2.1

0.02

-

pH 9.0, 37°C

645654

2.8.2.1

0.031

-

mutant enzyme D247L, enzyme form SULT1D1

660962

2.8.2.1

0.0316

-

SULT1A3, pH 11.0, 37°C

671885

2.8.2.1

0.037

-

mutant enzyme O86D, enzyme form SULT1D1

660962

2.8.2.1

0.0381

-

SULT1A3, pH 9.0, 37°C

671885

2.8.2.1

0.087

-

SULT1A3 double mutant H143Y/E146A, pH 7.4, 37°C

645668

2.8.2.1

0.0875

-

recombinant wild-type P-PST, pH 7.0, 37°C

645669

2.8.2.1

0.098

-

ST1a4, pH 7.4, 37°C

645680

2.8.2.1

0.109

-

wild-type SULT1A1, pH 7.4, 37°C

645668

2.8.2.1

0.127

-

SULT1A3 mutant E146A, pH 7.4, 37°C

645668

2.8.2.1

0.13

-

pH 7.4, 37°C

645680

2.8.2.1

0.13

-

ST1A1

645680

2.8.2.1

0.13

-

ST1A3

645680

2.8.2.1

0.175

-

SULT1A1, pH 7.0

645682

2.8.2.1

0.18

-

SULT1A1, pH 7.3-7.4

645682

2.8.2.1

0.24

-

pH 9.3, 37°C

645663

2.8.2.1

0.5

-

ST1A8, pH 7.4, 37°C

645680

2.8.2.1

2.2

-

recombinant isozyme P-PST, i.e. HAST1

645655

2.8.2.1

11.3

-

enzyme form SULT1A3

662515

2.3.1.87

8 entries

2.4.1.17

10 entries

2.8.2.1

39 entries

2.8.2.22

0.0111

-

recombinant protein

645841

2.8.2.4

0.2407

-

pH 7.0, 37°C, SULT1E1-V145E

645902

2.8.2.4

32.22

-

pH 7.0, 37°C, SULT1E1-wild-type

645902

2.8.2.4

79.35

-

pH 7.0, 37°C, SULT1E1-K85A

645902

2.8.2.9

0.16

-

pH 5.5, 37°C

644817

2.8.2.9

0.41

-

pH 9, 25°C

644826

4.1.1.28

0.00083

-

mutant enzyme K303A, in 50 mM HEPES, pH 7.5, at 25°C

701921

4.1.1.28

0.0505

-

wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C

701921

4.2.1.78

0.347

-

pH 7.3, 37°C

749327

4.2.1.78

0.502

-

pH 7.3, 37°C

749327

4.2.1.78

1.5

-

-

5895

4.2.1.78

5

-

-

5894

2.8.2.4

3 entries

2.8.2.9

2 entries

4.1.1.28

2 entries

4.2.1.78

4 entries

4.3.3.4

0.7

-

with fixed concentration of secologanin of 5 mM

247118