KEGG   ENZYME: 1.4.3.22Help
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
Arginine and proline metabolism
Histidine metabolism
Tryptophan metabolism
Metabolic pathways
Orthology
K11182  
diamine oxidase
Genes
HSA: 
26(AOC1)
PTR: 
PPS: 
100973977(AOC1)
GGO: 
101145709(AOC1)
PON: 
100173768(AOC1)
NLE: 
100598250(AOC1)
MCC: 
714112(AOC1)
MCF: 
102141942(AOC1)
CSAB: 
103227226(AOC1)
RRO: 
104675391(AOC1)
CJC: 
100414302(AOC1)
SBQ: 
101033597(AOC1)
MMU: 
76507(Aoc1)
RNO: 
65029(Aoc1)
CGE: 
100763954 100771382
NGI: 
103745300 103745301 103745358 103745360 103745361
HGL: 
101712557(Aoc1)
CCAN: 
109694449(Aoc1)
OCU: 
100347103(AOC1)
TUP: 
102495583(AOC1)
CFA: 
475536(AOC1)
AML: 
100484243(AOC1)
UMR: 
103660997(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)
BACU: 
103017288(AOC1)
LVE: 
103087882(AOC1)
ECB: 
100063930(AOC1)
MYB: 
102245958 102256259(AOC1)
MYD: 
102751704 102773146 107184081
HAI: 
109389675(AOC1)
RSS: 
109435152(AOC1)
PALE: 
102880369(AOC1)
LAV: 
100668068 100668351(AOC1)
MDO: 
100017902(AOC1)
SHR: 
100915360(AOC1)
OAA: 
100075142 100077877
GGA: 
100858159(AOC1)
CJO: 
107308680(AOC1)
APLA: 
106019416(AOC1)
FAB: 
101814988
PHI: 
102101625(AOC1)
FPG: 
101917962(AOC1)
FCH: 
102057016(AOC1)
CLV: 
102084607(AOC1)
AAM: 
106500478
ASN: 
102380706(AOC1)
AMJ: 
102569229(AOC1)
CPIC: 
101932586(AOC1)
ACS: 
100557987(aoc1)
PBI: 
103060423(AOC1)
GJA: 
107108215(AOC1)
XLA: 
108695581(aoc1.S) 108705560
XTR: 
100486601(aoc1)
DRE: 
555401(aoc1)
IPU: 
108276865(aoc1)
TRU: 
101078662(aoc1)
TNG: 
GSTEN00016699G001 GSTEN00016700G001
LCO: 
104927590(aoc1)
MZE: 
101467347(aoc1)
OLA: 
101163530
XMA: 
102236337(aoc1)
CSEM: 
103376876(aoc1)
SASA: 
106590278
LCM: 
102354448(AOC1)
BFO: 
BRAFLDRAFT_124922 BRAFLDRAFT_217424 BRAFLDRAFT_217434 BRAFLDRAFT_217436 BRAFLDRAFT_279774 BRAFLDRAFT_279777 BRAFLDRAFT_77414
LGI: 
LOTGIDRAFT_118163 LOTGIDRAFT_118238 LOTGIDRAFT_120790 LOTGIDRAFT_133255 LOTGIDRAFT_137098 LOTGIDRAFT_159693 LOTGIDRAFT_159859 LOTGIDRAFT_224288
CRG: 
105317731 105319659 105333031 105336069 105338020 105340107 105344412
OBI: 
106869685 106870602 106880971
SMM: 
Smp_017610
NVE: 
NEMVE_v1g230529 NEMVE_v1g243223
ADF: 
107333816 107333827 107337677 107352948
CRE: 
CHLREDRAFT_206147(AMX3)
CSL: 
COCSUDRAFT_46300
ACAN: 
ACA1_076120
FCY: 
FRACYDRAFT_244491
 » 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 (1976) 679-87.
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 (1994) 14484-9.
  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 (1999) 1-46.
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 (2002) 565-79.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
DBGET integrated database retrieval system