Primary-amine oxidase

Primary-amine oxidase
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 \rightleftharpoons 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. doi:10.1042/BC20110049. PMID 21819380.
  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. doi:10.1042/bj1990187. PMC 1163349. PMID 7337701.
  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. doi:10.1074/jbc.270.28.16939. PMID 7622512.
  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. doi:10.1016/1357-2725(95)00130-1. PMID 8920635.
  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. doi:10.1021/bi971797i. PMID 9405045.
  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. doi:10.1074/jbc.273.31.19490. PMID 9677370.
  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. doi:10.1177/002215540104900208. PMID 11156689.
  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. doi:10.1042/BJ20011435. PMC 1222726. PMID 11985492.
  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. doi:10.1016/S0161-813X(03)00117-7. PMID 14697905.
  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. doi:10.1110/ps.051438105. PMC 2279308. PMID 16046623.

External links

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