Primarni-amin oksidaza

Primarni-amin oksidaza (EC, aminska oksidaza (nespecifična), aminska oksidaza (sadrži bakar), aminska oksidaza (sadrži piridoksal), CAO (nespecifična), bakarna aminska oksidaza (nespecifična), Cu-aminska oksidaza (nespecifična), aminska oksidaza sa Cu (nespecifična), histamin deaminaza (nespecifična), histaminska oksidaza (nespecifična), monoaminska oksidaza (nespecifična), monoaminska oksidaza plasme (nespecifična), poliaminska oksidaza (nespecifična), semikarbazid-sensitivna aminska oksidaza (nespecifična), SSAO (nespecifična)) je enzim sa sistematskim imenom primarni-amin:kiseonik oksidoreduktaza (deaminacija).[1][2][3][4][5][6][7][8][9][10] Ovaj enzim katalizuje sledeću hemijsku reakciju

Primarni-amin oksidaza
Dimer amin oksidaze (čovjek)
EC broj
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
RCH2NH2 + H2O + O2 RCHO + NH3 + H2O2

Ova grupa enzima oksiduje primarne monoamine, i ima malo ili nije aktivna na diaminima.


  1. Haywood, G.W. and Large, P.J. (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”. Biochem. J. 199: 187-201. PMID 7337701. 
  2. Tipping, A.J. and McPherson, M.J. (1995). „Cloning and molecular analysis of the pea seedling copper amine oxidase”. J. Biol. Chem. 270: 16939-16946. PMID 7622512. 
  3. Lyles, G.A. (1996). „Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects”. Int. J. Biochem. Cell Biol. 28: 259-274. PMID 8920635. 
  4. Wilce, M.C., Dooley, D.M., Freeman, H.C., Guss, J.M., Matsunami, H., McIntire, W.S., Ruggiero, C.E., Tanizawa, K. and Yamaguchi, H. (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: 16116-16133. PMID 9405045. 
  5. Lee, Y. and Sayre, L.M. (1998). „Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini”. J. Biol. Chem. 273: 19490-19494. PMID 9677370. 
  6. Houen, G. (1999). „Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions”. APMIS Suppl. 96: 1-46. PMID 10668504. 
  7. Andrés, N., Lizcano, J.M., Rodríguez, M.J., Romera, M., Unzeta, M. and Mahy, N. (2001). „Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase”. J. Histochem. Cytochem. 49: 209-217. PMID 11156689. 
  8. Saysell, C.G., Tambyrajah, W.S., Murray, J.M., Wilmot, C.M., Phillips, S.E., McPherson, M.J. and Knowles, P.F. (2002). „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. PMID 11985492. 
  9. O'Sullivan, J., Unzeta, M., Healy, J., O'Sullivan, M.I., Davey, G. and Tipton, K.F. (2004). „Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do”. Neurotoxicology 25: 303-315. 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. (2005). „Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications”. Protein Sci. 14: 1964-1974. PMID 16046623. 


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