EC 1.4.3.21 - Primary-amine oxidase

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IntEnz Enzyme Nomenclature
EC 1.4.3.21

Names

Accepted name:
primary-amine oxidase
Other names:
amine oxidase [ambiguous]
amine oxidase (copper-containing)
amine oxidase (pyridoxal containing) [incorrect]
benzylamine oxidase [incorrect]
CAO [ambiguous]
copper amine oxidase [ambiguous]
Cu-amine oxidase [ambiguous]
Cu-containing amine oxidase [ambiguous]
diamine oxidase [incorrect]
diamino oxhydrase [incorrect]
histamine deaminase [ambiguous]
histamine oxidase [ambiguous]
monoamine oxidase [ambiguous]
plasma monoamine oxidase [ambiguous]
polyamine oxidase [ambiguous]
semicarbazide-sensitive amine oxidase [ambiguous]
SSAO [ambiguous]
Systematic name:
primary-amine:oxygen oxidoreductase (deaminating)

Reactions

Comments:

A group of enzymes that oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, monoamine oxidase, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0052595 , GO:0052594 , GO:0052596 , GO:0008131 , GO:0052593
UniProtKB/Swiss-Prot: (21) [show] [UniProt]

References

  1. Haywood, G.W. and Large, P.J.
    Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source.
    Biochem. J. 199: 187-201 (1981). [PMID: 7337701]
  2. Tipping, A.J. AND McPherson, M.J.
    Cloning and molecular analysis of the pea seedling copper amine oxidase.
    J. Biol. Chem. 270: 16939-16946 (1995). [PMID: 7622512]
  3. Lyles, G.A.
    Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects.
    Int. J. Biochem. Cell Biol. 28: 259-274 (1996). [PMID: 8920635]
  4. Wilce, M.C.J., Dooley, D.M., Freeman, H.C., Guss, J.M., Matsunami, H., McIntire, W.S., Ruggiero, C.E., Tanizawa, K. and Yamaguchi, H.
    Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone.
    Biochemistry 36: 16116-16133 (1997). [PMID: 9405045]
  5. Lee, Y. and Sayre, L.M.
    Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini.
    J. Biol. Chem. 273: 19490-19494 (1998). [PMID: 9677370]
  6. Houen, G.
    Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions.
    APMIS Suppl. 96: 1-46 (1999). [PMID: 10668504]
  7. Andrés, N., Lizcano, J.M., Rodríguez, M. J., Romera, M., Unzeta, M. and Mahy, N.
    Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase.
    J. Histochem. Cytochem. 49: 209-217 (2001). [PMID: 11156689]
  8. Saysell, C.G., Tambyrajah, W.S., Murray, J.M., Wilmot, C.M., Phillips, S.E.V., McPherson, M.J. and Knowles, P.F.
    Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue.
    Biochem. J. 365: 809-816 (2002). [PMID: 11985492]
  9. O'Sullivan, J., Unzeta, M., Healy, J., O'Sullivan, M.I., Davey, G. and Tipton, K.F.
    Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do.
    Neurotoxicology 25: 303-315 (2004). [PMID: 14697905]
  10. Airenne, T.T., Nymalm, Y., Kidron, H., Smith, D.J., Pihlavisto, M., Salmi, M., Jalkanen, S., Johnson, M.S. and Salminen, T.A.
    Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications.
    Protein Sci. 14: 1964-1974 (2005). [PMID: 16046623]

[EC 1.4.3.21 created 2008]