KEGG   ENZYME: 1.14.17.1Help
Entry
EC 1.14.17.1                Enzyme                                 

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 + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O [RN:R02535]
Reaction(KEGG)
Substrate
dopamine [CPD:C03758];
ascorbate [CPD:C00072];
O2 [CPD:C00007]
Product
noradrenaline [CPD:C00547];
dehydroascorbate [CPD:C05422];
H2O [CPD:C00001]
Comment
A copper protein. 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
Pathway
ec00350  Tyrosine metabolism
ec01100  Metabolic pathways
Orthology
K00503  dopamine beta-monooxygenase
Genes
HSA: 1621(DBH)
PTR: 464827(DBH)
PPS: 100985587(DBH)
GGO: 101154486(DBH)
PON: 100461514(DBH)
NLE: 100597609(DBH)
MCC: 574105(DBH)
MCF: 102139527(DBH)
CSAB: 103239676(DBH)
RRO: 104669786(DBH)
RBB: 108513277(DBH)
CJC: 100406041(DBH)
SBQ: 101046079(DBH)
MMU: 13166(Dbh)
RNO: 25699(Dbh)
CGE: 100761411(Dbh)
NGI: 103742818(Dbh)
HGL: 101724312(Dbh)
CCAN: 109677868(Dbh)
OCU: 103347199(DBH)
TUP: 102468703(DBH)
CFA: 448806(DBH)
AML: 100480347(DBH)
UMR: 103679922(DBH)
ORO: 101362871(DBH)
FCA: 101082957(DBH)
PTG: 102961078(DBH)
AJU: 106988258(DBH)
BTA: 280758(DBH)
BOM: 102286194(DBH)
BIU: 109566610(DBH)
PHD: 102327132(DBH)
CHX: 102176244(DBH)
SSC: 733609(DBH)
CFR: 102523816(DBH)
CDK: 105106327(DBH)
BACU: 103001548(DBH)
LVE: 103082302(DBH)
OOR: 101269198(DBH)
ECB: 791247(DBH)
EPZ: 103564043(DBH)
EAI: 106845350(DBH)
MYB: 102264141(DBH)
MYD: 102763656(DBH)
HAI: 109381156(DBH)
RSS: 109445985(DBH)
PALE: 102882740(DBH)
LAV: 100675803(DBH)
TMU: 101344432
MDO: 100018814(DBH)
SHR: 100925655(DBH)
OAA: 100073905(DBH)
GGA: 395549(DBH)
MGP: 100544779(DBH)
CJO: 107321868(DBH)
APLA: 101793381(DBH)
ACYG: 106044068(DBH)
TGU: 100224356(DBH)
GFR: 102038113(DBH)
FAB: 101810825(DBH)
PHI: 102100810(DBH)
PMAJ: 107211985(DBH)
CCW: 104688340(DBH)
FPG: 101923335(DBH)
FCH: 102048380(DBH)
CLV: 102097674(DBH)
EGZ: 104129357(DBH)
AAM: 106484479(DBH)
ASN: 102377750(DBH)
AMJ: 102562465(DBH)
PSS: 102455557(DBH)
CMY: 102935981(DBH)
CPIC: 101944381(DBH)
ACS: 100566843(dbh)
PVT: 110089291(DBH)
PBI: 103050577(DBH)
GJA: 107106563(DBH)
XLA: 108698178(dbh.L) 108699900(dbh.S)
XTR: 100492247(dbh)
NPR: 108792841(DBH)
DRE: 30505(dbh)
SGH: 107595570(dbh) 107597665
IPU: 108276829(dbh)
AMEX: 103038160(dbh)
TRU: 101066621(dbh)
LCO: 104923914(dbh) 109141567
NCC: 104968179(dbh)
MZE: 101464817(dbh)
OLA: 101157870(dbh)
XMA: 102218690(dbh)
PRET: 103473626(dbh)
NFU: 107372400(dbh)
CSEM: 103389065(dbh)
LCF: 108879254(dbh)
HCQ: 109517071(dbh)
BPEC: 110174164(dbh)
SASA: 106568424(dbh)
ELS: 105014776(dbh)
SFM: 108934136(dbh)
LCM: 102359119(DBH)
CMK: 103182970(dbh)
CIN: 100176680
SPU: 586320
APLC: 110976390
SKO: 102804261
DME: Dmel_CG1543(Tbh)
DSI: Dsimw501_GD16874(Dsim_Tbh)
MDE: 101897009
AAG: 5574019
AME: 751102(Tbh)
BIM: 100743458
BTER: 100649446
SOC: 105201088
AEC: 105145835
ACEP: 105618961
PBAR: 105434118
HST: 105182135
CFO: 105258572
LHU: 105668349
PGC: 109857916
NVI: 100119029
TCA: 663011(TcTBH)
NVL: 108563606
BMOR: 100862766(Tbh)
PRAP: 110994553
API: 100166363
DNX: 107169334
ZNE: 110838985
FCD: 110851639
TUT: 107360804
CEL: CELE_H13N06.6(tbh-1)
CBR: CBG07714(Cbr-tbh-1)
OBI: 106875923
 » show all
Taxonomy
Reference
1  [PMID:5846992]
  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
2  [PMID:14416204]
  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)
Other DBs
ExplorEnz - The Enzyme Database: 1.14.17.1
IUBMB Enzyme Nomenclature: 1.14.17.1
ExPASy - ENZYME nomenclature database: 1.14.17.1
BRENDA, the Enzyme Database: 1.14.17.1
CAS: 9013-38-1

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