Entry
Name
dopamine beta-monooxygenase;
dopamine beta-hydroxylase;
MDBH (membrane-associated dopamine beta-monooxygenase);
SDBH (soluble dopamine beta-monooxygenase);
dopamine-B-hydroxylase;
3,4-dihydroxyphenethylamine beta-oxidase;
4-(2-aminoethyl)pyrocatechol beta-oxidase;
dopa beta-hydroxylase;
dopamine beta-oxidase;
dopamine hydroxylase;
phenylamine beta-hydroxylase;
(3,4-dihydroxyphenethylamine)beta-mono-oxygenase;
DbetaM (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
dopamine,ascorbate:oxygen oxidoreductase (beta-hydroxylating)
Reaction(IUBMB)
dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O [RN:
R02535 ]
Reaction(KEGG)
Substrate
Product
Comment
A copper protein. The enzyme, found in animals, binds two copper ions with distinct roles during catalysis. Stimulated by fumarate.
History
EC 1.14.17.1 created 1965 as EC 1.14.2.1, transferred 1972 to EC 1.14.17.1, modified 2020
Pathway
Orthology
K00503 dopamine beta-monooxygenase
Genes
XLA : 108698178(dbh.L) 108699900(dbh.S)
SANH : 107658656 107685164
SGH : 107595570(dbh) 107597665
CCAR : 109052532 109080215
CAUA : 113109649 113109662
IFU : 128620171 128620707(dbh)
MSAM : 119882201 119914708(dbh)
NWH : 119424449(dbh) 119429221
PSPA : 121303526 121307068
SCLV : 120339920 120342663
LPIC : 129278135 129278136
DSI : Dsimw501_GD16874(Dsim_Tbh)
AALB : 109427529 115256503
ASUA : 134204518 134207195
CFEL : 113385824 113385829
CEL : CELE_H13N06.6(tbh-1)
CBR : CBG_07714(Cbr-tbh-1)
LGI : LOTGIDRAFT_120180 LOTGIDRAFT_162200 LOTGIDRAFT_191156 LOTGIDRAFT_233457 LOTGIDRAFT_234237
PVUL : 126812196 126832242
PCAN : 112557427 112561909 112563147 112570230 112570414 112575465 112576338
BGT : 106066921 106077242 106078772
HRF : 124114394 124138380 124142782 124142798 124148606 124151079
HRJ : 124253288 124257823 124266189 124270276 124275898 124284219 124284488 124289238
CRG : 105321753 105329831 105337151 105344230
CVN : 111125361 111127321 111133921
MYI : 110442054 110447535 110447536 110450515 110452901 110454243 110454251 110455641 110456098 110456174 110467057 110467403
PMAX : 117316542 117316561 117316569 117316585 117319629 117321720 117321721 117321920 117321941 117334297 117334351 117334793 117335029
MMER : 123533077 123533930 123538847 123545778 123546293 123555574 123561327
LAK : 106150741 106165088 106173926 106180620 106181793
» show all
Taxonomy
Reference
Authors
LEVIN EY, LEVENBERG B, KAUFMAN S.
Title
The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine.
Journal
J Biol Chem 235:2080-6 (1960)
Reference
Authors
Friedman S, Kaufman S.
Title
3,4-dihydroxyphenylethylamine beta-hydroxylase. Physical properties, copper content, and role of copper in the catalytic acttivity.
Journal
J Biol Chem 240:4763-73 (1965)
Reference
Authors
Skotland T, Ljones T
Title
Direct spectrophotometric detection of ascorbate free radical formed by dopamine beta-monooxygenase and by ascorbate oxidase.
Journal
Reference
Authors
Evans JP, Ahn K, Klinman JP
Title
Evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase. Implications for the reactive oxygen species.
Journal
Other DBs
ExPASy - ENZYME nomenclature database: 1.14.17.1
LinkDB
All DBs