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Entry
EC 1.4.3.22                 Enzyme                                 

Name
diamine oxidase;
amine oxidase (ambiguous);
amine oxidase (copper-containing) (ambiguous);
CAO (ambiguous);
Cu-containing amine oxidase (ambiguous);
copper amine oxidase (ambiguous);
diamine oxidase (ambiguous);
diamino oxhydrase (ambiguous);
histaminase;
histamine deaminase (incorrect);
semicarbazide-sensitive amine oxidase (incorrect);
SSAO (incorrect)
Class
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
histamine:oxygen oxidoreductase (deaminating)
Reaction(IUBMB)
histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2 [RN:R02150]
Reaction(KEGG)
Substrate
histamine [CPD:C00388];
H2O [CPD:C00001];
O2 [CPD:C00007]
Product
(imidazol-4-yl)acetaldehyde;
NH3 [CPD:C00014];
H2O2 [CPD:C00027]
Comment
A group of enzymes that oxidize diamines, such as histamine, and also some primary monoamines but have little or no activity towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, like EC 1.4.3.21 (primary-amine oxidase) but unlike EC 1.4.3.4 (monoamine oxidase), they are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide.
History
EC 1.4.3.22 created 2007 (EC 1.4.3.6 created 1961, part-incorporated 2008)
Pathway
ec00330  Arginine and proline metabolism
ec00340  Histidine metabolism
ec00380  Tryptophan metabolism
ec01100  Metabolic pathways
Orthology
K11182  diamine oxidase
Genes
HSA: 26(AOC1)
PTR: 107975990(AOC1)
PPS: 100973977(AOC1)
GGO: 101145709(AOC1)
PON: 100173768(AOC1)
NLE: 100598250(AOC1)
MCC: 714112(AOC1)
MCF: 102141942(AOC1)
CSAB: 103227226(AOC1)
RRO: 104675391(AOC1)
RBB: 108531161(AOC1)
CJC: 100414302(AOC1)
SBQ: 101033597(AOC1)
MMU: 76507(Aoc1)
RNO: 65029(Aoc1)
HGL: 101712557(Aoc1)
CCAN: 109694449(Aoc1)
OCU: 100347103(AOC1)
TUP: 102495583(AOC1)
CFA: 475536(AOC1)
AML: 100484243(AOC1)
UMR: 103660997(AOC1)
ORO: 101381594(AOC1)
FCA: 101096221(AOC1)
PTG: 102955637(AOC1)
AJU: 106974449(AOC1)
BTA: 509751(AOC1)
BOM: 102275498(AOC1)
BIU: 109557791(AOC1)
PHD: 102330697(AOC1)
CHX: 102177774(AOC1)
OAS: 101106065 101112561(AOC1)
SSC: 100517436(AOC1)
CFR: 102522082(AOC1)
CDK: 105105709(AOC1)
BACU: 103017288(AOC1)
LVE: 103087882(AOC1)
OOR: 101279845(AOC1)
ECB: 100063930(AOC1)
EPZ: 103544966(AOC1)
EAI: 106823380(AOC1)
MYB: 102245958 102256259(AOC1)
HAI: 109389675(AOC1)
RSS: 109435152(AOC1)
PALE: 102880369(AOC1)
LAV: 100668068 100668351(AOC1)
TMU: 101356291
MDO: 100017902(AOC1)
SHR: 100915360(AOC1)
GGA: 100858159(AOC1)
CJO: 107308680(AOC1)
APLA: 106019416(AOC1)
FAB: 101814988
PHI: 102101625(AOC1)
PMAJ: 107214654(AOC1)
FPG: 101917962(AOC1)
FCH: 102057016(AOC1)
CLV: 102084607(AOC1)
AAM: 106500478
ASN: 102380706(AOC1)
AMJ: 102569229(AOC1)
CPIC: 101932586(AOC1)
ACS: 100557987(aoc1)
PVT: 110082530(AOC1)
PBI: 103060423(AOC1)
GJA: 107108215(AOC1)
XLA: 108695581(aoc1.S) 108705560
XTR: 100486601(aoc1)
NPR: 108803230(AOC1)
DRE: 555401(aoc1)
CCAR: 109050071(aoc1) 109066974
IPU: 108276865(aoc1)
AMEX: 103033242(aoc1)
TRU: 101078662(aoc1)
LCO: 104927590(aoc1)
NCC: 104965259(aoc1)
MZE: 101467347(aoc1)
OLA: 101163530(aoc1)
XMA: 102236337(aoc1)
PRET: 103482350(aoc1)
NFU: 107382765(aoc1)
KMR: 108246408(aoc1)
CSEM: 103376876(aoc1)
LCF: 108881560(aoc1)
SDU: 111228279(aoc1)
HCQ: 109518117(aoc1)
BPEC: 110165585(aoc1)
MALB: 109953334(aoc1)
SASA: 106590278
ELS: 105019484(aoc1)
SFM: 108935426(aoc1)
LCM: 102354448(AOC1)
SHX: MS3_05030
EGL: EGR_03941
CRE: CHLREDRAFT_206147(AMX3)
MNG: MNEG_1864
 » show all
Taxonomy
Reference
1
  Authors
Zeller, E.A.
  Title
Diamine oxidases.
  Journal
In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 313-335.
Reference
2  [PMID:182134]
  Authors
Crabbe MJ, Waight RD, Bardsley WG, Barker RW, Kelly ID, Knowles PF.
  Title
Human placental diamine oxidase. Improved purification and characterization of a copper- and manganese-containing amine oxidase with novel substrate specificity.
  Journal
Biochem J 155:679-87 (1976)
Reference
3  [PMID:8182053]
  Authors
Chassande O, Renard S, Barbry P, Lazdunski M.
  Title
The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter.
  Journal
J Biol Chem 269:14484-9 (1994)
  Sequence
[hsa:26]
Reference
4  [PMID:10668504]
  Authors
Houen G.
  Title
Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions.
  Journal
APMIS Suppl 96:1-46 (1999)
Reference
5  [PMID:12072962]
  Authors
Elmore BO, Bollinger JA, Dooley DM.
  Title
Human kidney diamine oxidase: heterologous expression, purification, and characterization.
  Journal
J Biol Inorg Chem 7:565-79 (2002)
DOI:10.1007/s00775-001-0331-1
Other DBs
ExplorEnz - The Enzyme Database: 1.4.3.22
IUBMB Enzyme Nomenclature: 1.4.3.22
ExPASy - ENZYME nomenclature database: 1.4.3.22
BRENDA, the Enzyme Database: 1.4.3.22

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