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: 
463895(AOC1)
PPS: 
100973977(AOC1)
GGO: 
101145709(ABP1)
PON: 
100173768(AOC1)
NLE: 
100598250(AOC1)
MCC: 
714112(AOC1)
MCF: 
102141942(AOC1)
RRO: 
104675391(AOC1)
CJC: 
100414302(AOC1)
MMU: 
76507(Aoc1)
RNO: 
65029(Aoc1)
CGE: 
NGI: 
HGL: 
101712557(Aoc1)
OCU: 
100347103(AOC1)
TUP: 
102495583(AOC1)
CFA: 
475536(AOC1)
AML: 
100484243(AOC1)
UMR: 
103660997(AOC1)
FCA: 
101096221(AOC1)
PTG: 
102955637(AOC1)
BTA: 
509751(AOC1)
BOM: 
102275498(AOC1)
PHD: 
102330697(AOC1)
CHX: 
102177774(AOC1)
OAS: 
SSC: 
100517436(AOC1)
CFR: 
102522082(AOC1)
BACU: 
103017288(AOC1)
LVE: 
103087882(AOC1)
ECB: 
100063930(AOC1)
MYB: 
MYD: 
PALE: 
102880369(AOC1)
MDO: 
100017902(AOC1)
SHR: 
100915360(AOC1)
OAA: 
GGA: 
100858159(AOC1)
CJO: 
107308680(AOC1)
APLA: 
106019416(AOC1)
FAB: 
PHI: 
102101625(AOC1)
FPG: 
101917962(AOC1)
FCH: 
102057016(AOC1)
CLV: 
102084607(AOC1)
AAM: 
ASN: 
102380706(AOC1)
AMJ: 
102569229(AOC1)
ACS: 
100557987(aoc1)
PBI: 
103060423(AOC1)
GJA: 
107108215(AOC1)
XTR: 
100486601(aoc1)
DRE: 
555401(aoc1)
TRU: 
101078662(aoc1)
MZE: 
101467347(aoc1)
OLA: 
XMA: 
102236337(aoc1)
LCM: 
102354448(AOC1)
BFO: 
LGI: 
CRG: 
OBI: 
SMM: 
NVE: 
CRE: 
CSL: 
ACAN: 
 » 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: 

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