EC Tree |
1. Oxidoreductases |
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 1.14.17.1 |
BRENDA Enzyme Link: | BRENDA 1.14.17.1 |
KEGG Enzyme Link: | KEGG1.14.17.1 |
BioCyc Enzyme Link: | BioCyc 1.14.17.1 |
ExPASy Enzyme Link: | ExPASy1.14.17.1 |
EC2PDB Enzyme Link: | EC2PDB 1.14.17.1 |
ExplorEnz Enzyme Link: | ExplorEnz 1.14.17.1 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.14.17.1 |
IntEnz Enzyme Link: | IntEnz 1.14.17.1 |
MEDLINE Enzyme Link: | MEDLINE 1.14.17.1 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:19117 | dopamine + L-ascorbate + O2 = (R)-noradrenaline + H2O + L-dehydroascorbate |
RULE(radius=1) | [*:1]-[C;H0;+0:2](-[OH;+0:3])=[C;H0;+0:4](-[*:5])-[OH;+0:6].[*:7]-[CH2;+0:8]-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[C;H0;+0:4](-[*:5])=[O;H0;+0:6].[*:7]-[CH;+0:8](-[*:9])-[OH;+0:10].[OH2;+0:11] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Direct spectrophotometric detection of ascorbate free radical formed by dopamine beta-monooxygenase and by ascorbate oxidase. | Skotland T, Ljones T | 1980 Jun 5 | 7388045 |
Evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase. Implications for the reactive oxygen species. | Evans JP, Ahn K, Klinman JP | 2003 Dec 12 | 12966104 |
Reduction of dopamine beta-monooxygenase. A unified model for apparent negative cooperativity and fumarate activation. | Wimalasena K, Dharmasena S, Wimalasena DS, Hughbanks-Wheaton DK | 1996 Oct 18 | 8824243 |
Purification and characterization of avian dopamine beta-hydroxylase. | Long RA, Weppelman RM, Taylor JE, Tolman RL, Olson G | 1981 Dec 22 | 7326235 |
Dopamine beta-hydroxylase: activity and inhibition in the presence of beta-substituted phenethylamines. | Klinman JP, Krueger M | 1982 Jan 5 | 7059582 |
3,4-dihydroxyphenylethylamine beta-hydroxylase. Physical properties, copper content, and role of copper in the catalytic acttivity. | Friedman S, Kaufman S | 1965 Dec | 5846992 |
Bovine adrenal medullary dopamine beta-hydroxylase: purification by affinity chromatography, kinetic studies and presence of essential histidyl residues. | Aunis D, Miras-Portugal MT, Mandel P | 1973 Dec 19 | 4778938 |
Mechanism-based inhibition of dopamine beta-monooxygenase by aldehydes and amides. | Bossard MJ, Klinman JP | 1986 Dec 15 | 3782127 |
Inactivation of dopamine beta-hydroxylase by beta-ethynyltyramine: kinetic characterization and covalent modification of an active site peptide. | DeWolf WE Jr, Chambers PA, Southan C, Saunders D, Kruse LI | 1989 May 2 | 2751998 |
Inhibition of dopamine beta-hydroxylase by bidentate chelating agents. | Townes S, Titone C, Rosenberg RC | 1990 Feb 9 | 2306475 |