Primary-amine oxidase

Primary-amine oxidase

Amine oxidase (semicarbazide-sensitive) dimer, Human
Identifiers
EC number 1.4.3.21
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Primary-amine oxidase, also known as semicarbazide-sensitive amine oxidase (SSAO),[1][2] is an enzyme (EC 1.4.3.21) with the systematic name primary-amine:oxygen oxidoreductase (deaminating).[3][4][5][6][7][8][9][10][11][12] This enzyme catalyses the following chemical reaction

RCH2NH2 + H2O + O2 RCHO + NH3 + H2O2

These enzymes are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone).

Human proteins containing this domain

References

  1. ↑ Andrew McDonald. "Primary-amine oxidase". ExplorEnz – The Enzyme Database. International Union of Biochemistry and Molecular Biology. Retrieved 30 December 2015.
  2. ↑ Solé M, Unzeta M (Nov 2011). "Vascular cell lines expressing SSAO/VAP-1: a new experimental tool to study its involvement in vascular diseases". Biology of the Cell / Under the Auspices of the European Cell Biology Organization. 103 (11): 543–57. PMID 21819380. doi:10.1042/BC20110049.
  3. ↑ Haywood GW, Large PJ (Oct 1981). "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". The Biochemical Journal. 199 (1): 187–201. PMC 1163349 Freely accessible. PMID 7337701. doi:10.1042/bj1990187.
  4. ↑ Tipping AJ, McPherson MJ (Jul 1995). "Cloning and molecular analysis of the pea seedling copper amine oxidase". The Journal of Biological Chemistry. 270 (28): 16939–46. PMID 7622512. doi:10.1074/jbc.270.28.16939.
  5. ↑ Lyles GA (Mar 1996). "Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects". The International Journal of Biochemistry & Cell Biology. 28 (3): 259–74. PMID 8920635. doi:10.1016/1357-2725(95)00130-1.
  6. ↑ Wilce MC, Dooley DM, Freeman HC, Guss JM, Matsunami H, McIntire WS, Ruggiero CE, Tanizawa K, Yamaguchi H (Dec 1997). "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 (51): 16116–33. PMID 9405045. doi:10.1021/bi971797i.
  7. ↑ Lee Y, Sayre LM (Jul 1998). "Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini". The Journal of Biological Chemistry. 273 (31): 19490–4. PMID 9677370. doi:10.1074/jbc.273.31.19490.
  8. ↑ Houen G (1999). "Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions". APMIS. Supplementum. 96: 1–46. PMID 10668504.
  9. ↑ Andrés N, Lizcano JM, Rodríguez MJ, Romera M, Unzeta M, Mahy N (Feb 2001). "Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase". The Journal of Histochemistry and Cytochemistry. 49 (2): 209–17. PMID 11156689. doi:10.1177/002215540104900208.
  10. ↑ Saysell CG, Tambyrajah WS, Murray JM, Wilmot CM, Phillips SE, McPherson MJ, Knowles PF (Aug 2002). "Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue". The Biochemical Journal. 365 (Pt 3): 809–16. PMC 1222726 Freely accessible. PMID 11985492. doi:10.1042/BJ20011435.
  11. ↑ O'Sullivan J, Unzeta M, Healy J, O'Sullivan MI, Davey G, Tipton KF (Jan 2004). "Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do". Neurotoxicology. 25 (1-2): 303–15. PMID 14697905. doi:10.1016/S0161-813X(03)00117-7.
  12. ↑ Airenne TT, Nymalm Y, Kidron H, Smith DJ, Pihlavisto M, Salmi M, Jalkanen S, Johnson MS, Salminen TA (Aug 2005). "Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications". Protein Science. 14 (8): 1964–74. PMC 2279308 Freely accessible. PMID 16046623. doi:10.1110/ps.051438105.
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