Izvorni kod stranice Primarni-amin oksidaza

{{Infobox Enzim
| Name = Primarni-amin oksidaza
| EC_number = 1.4.3.21
| CAS_number = 
| IUBMB_EC_number = 1/4/3/21
| GO_code = 
| image = 2c10.jpg
| width = 270
| caption = Dimer amin oksidaze (čovjek)
}}
'''Primarni-amin oksidaza''' ({{EC broj|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)''.<ref>{{cite journal | title = 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 |author = Haywood, G.W. and Large, P.J. |journal = Biochem. J. |date = 1981 |volume = 199 |pages = 187-201 |pmid = 7337701}}</ref><ref>{{cite journal | title = Cloning and molecular analysis of the pea seedling copper amine oxidase |author = Tipping, A.J. and McPherson, M.J. |journal = J. Biol. Chem. |date = 1995 |volume = 270 |pages = 16939-16946 |pmid = 7622512}}</ref><ref>{{cite journal | title = Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects | url = https://archive.org/details/sim_international-journal-of-biochemistry-cell-biology_1996-03_28_3/page/259 |author = Lyles, G.A. |journal = Int. J. Biochem. Cell Biol. |date = 1996 |volume = 28 |pages = 259-274 |pmid = 8920635}}</ref><ref>{{cite journal | title = Crystal structures of the copper-containing amine oxidase from ''Arthrobacter globiformis'' in the holo and apo forms: implications for the  biogenesis of topaquinone |author = 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. |journal = Biochemistry |date = 1997 |volume = 36 |pages = 16116-16133 |pmid = 9405045}}</ref><ref>{{cite journal | title = Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini |author = Lee, Y. and Sayre, L.M. |journal = J. Biol. Chem. |date = 1998 |volume = 273 |pages = 19490-19494 |pmid = 9677370}}</ref><ref>{{cite journal | title = Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions |author = Houen, G. |journal = APMIS Suppl. |date = 1999 |volume = 96 |pages = 1-46 |pmid = 10668504}}</ref><ref>{{cite journal | title = Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase |author = Andr&eacute;s, N., Lizcano, J.M., Rodr&iacute;guez, M.J., Romera, M., Unzeta, M. and Mahy, N. |journal = J. Histochem. Cytochem. |date = 2001 |volume = 49 |pages = 209-217 |pmid = 11156689}}</ref><ref>{{cite journal | title = Probing the catalytic mechanism of ''Escherichia coli'' amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue | url = https://archive.org/details/sim_biochemical-journal_2002-08-01_365/page/n260 |author = Saysell, C.G., Tambyrajah, W.S., Murray, J.M., Wilmot, C.M., Phillips, S.E., McPherson, M.J. and Knowles, P.F. |journal = Biochem. J. |date = 2002 |volume = 365 |pages = 809-816 |pmid = 11985492}}</ref><ref>{{cite journal | title = Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do |author = O'Sullivan, J., Unzeta, M., Healy, J., O'Sullivan, M.I., Davey, G. and Tipton, K.F. |journal = Neurotoxicology |date = 2004 |volume = 25 |pages = 303-315 |pmid = 14697905}}</ref><ref>{{cite journal | title = Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications |author = Airenne, T.T., Nymalm, Y., Kidron, H., Smith, D.J., Pihlavisto, M., Salmi, M., Jalkanen, S., Johnson, M.S. and Salminen, T.A. |journal = Protein Sci. |date = 2005 |volume = 14 |pages = 1964-1974 |pmid = 16046623}}</ref> Ovaj enzim [[Kataliza|katalizuje]] sledeću [[hemijska reakcija|hemijsku reakciju]]

: RCH<sub>2</sub>NH<sub>2</sub> + H<sub>2</sub>O + O<sub>2</sub> <math>\rightleftharpoons</math> RCHO + NH<sub>3</sub> + H<sub>2</sub>O<sub>2</sub>

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

== Reference ==
{{reflist}}

== Literatura ==
{{refbegin|2}}
* {{PriceEnzymology3rd}}
* {{TooneAdvancesInEnzymology}}
* {{Branden ProteinStructure2nd}}
* {{SegelEnzymeKinetics}}
* {{CopelandEvaluationOfEnzymeInhibitors2nd}}
* {{MichalBiochemicalPathways}}
{{refend}}

== Vanjske veze ==
* {{MeshName|Primary-amine+oxidase}}

{{Enzimi}}

[[Kategorija:EC 1.4.3]]