Primarni-amin oksidaza

Primarni-amin oksidaza
Amin oksidaza dimer, Human
Identifikatori
EC broj1.4.3.21
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum

Primarni-amin oksidaza (EC 1.4.3.21, 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

RCH2NH2 + H2O + O2 RCHO + NH3 + H2O2

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

Reference

  1. ^ Haywood, G.W. & 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. & 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. & 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. 

Literatura

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