Primary-amine oxidase
| Primary-amine oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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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 | ||||||||
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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
- ↑ Andrew McDonald. "Primary-amine oxidase". ExplorEnz – The Enzyme Database. International Union of Biochemistry and Molecular Biology. Retrieved 30 December 2015.
- ↑ 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.
- ↑ 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. - ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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
- Primary-amine oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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