Biology:Primary-amine oxidase
| Primary-amine oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 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 | ||||||||
| |||||||||
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 [math]\displaystyle{ \rightleftharpoons }[/math] RCHO + NH3 + H2O2
These enzymes are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone).
Like monoamine oxidase (MAO), SSAO can deaminate short-chain primary amines, but is insensitive to MAO inhibitors. Semicarbazide inhibits the enzyme, in addition to other hydrazines, hydroxylamine and propargylamine. However, hydrazines are weak inhibitors and stronger inhibitors have been developed.
SSAO is found in the smooth muscle of blood vessels and various other tissues. The physiological function of SSAO is not well understood. Development of blood vessels, lipolysis regulation, and detoxication are suggested. It may function as a scavenger enzyme to assist MAO. However, the oxidation process generates harmful products that may be involved in causing atherosclerosis and vascular damage in diabetes. Elevation of SSAO activity is observed in atherosclerosis, diabetes mellitus, obesity, carotid plaque cases and varicosities.
There are SSAO inhibitors in development.[13][14]
Human proteins containing this domain
Bacterial proteins containing this domain
- Tyramine oxidase (tynA) in Escherichia coli[15][16]
References
- ↑ "Primary-amine oxidase". International Union of Biochemistry and Molecular Biology. http://www.enzyme-database.org/query.php?ec=1.4.3.21.
- ↑ "Vascular cell lines expressing SSAO/VAP-1: a new experimental tool to study its involvement in vascular diseases". Biology of the Cell 103 (11): 543–57. Nov 2011. doi:10.1042/BC20110049. PMID 21819380.
- ↑ "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. Oct 1981. doi:10.1042/bj1990187. PMID 7337701.
- ↑ "Cloning and molecular analysis of the pea seedling copper amine oxidase". The Journal of Biological Chemistry 270 (28): 16939–46. Jul 1995. doi:10.1074/jbc.270.28.16939. PMID 7622512.
- ↑ "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. Mar 1996. doi:10.1016/1357-2725(95)00130-1. PMID 8920635.
- ↑ "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. Dec 1997. doi:10.1021/bi971797i. PMID 9405045.
- ↑ "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. Jul 1998. doi:10.1074/jbc.273.31.19490. PMID 9677370.
- ↑ "Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions". APMIS 107 (S96): 1–46. 1999. doi:10.1111/apm.1999.107.s96.5. PMID 10668504.
- ↑ "Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase". The Journal of Histochemistry and Cytochemistry 49 (2): 209–17. Feb 2001. doi:10.1177/002215540104900208. PMID 11156689.
- ↑ "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. Aug 2002. doi:10.1042/BJ20011435. PMID 11985492.
- ↑ "Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do". Neurotoxicology 25 (1–2): 303–15. Jan 2004. doi:10.1016/S0161-813X(03)00117-7. PMID 14697905.
- ↑ "Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications". Protein Science 14 (8): 1964–74. Aug 2005. doi:10.1110/ps.051438105. PMID 16046623.
- ↑ "Anti-inflammatory effects of LJP 1586 [Z-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride], an amine-based inhibitor of semicarbazide-sensitive amine oxidase activity". The Journal of Pharmacology and Experimental Therapeutics 324 (2): 867–75. 2008. doi:10.1124/jpet.107.131672. PMID 17993604.
- ↑ "Design, synthesis, and biological evaluation of semicarbazide-sensitive amine oxidase (SSAO) inhibitors with anti-inflammatory activity". Journal of Medicinal Chemistry 49 (7): 2166–73. 2006. doi:10.1021/jm050538l. PMID 16570912.
- ↑ "EC 1.4.3.21 – primary-amine oxidase and Organism(s) Escherichia coli, Escherichia coli K-12". Technische Universität Braunschweig. https://www.brenda-enzymes.org/enzyme.php?ecno=1.4.3.21&Suchword=&reference=&UniProtAcc=&organism%5B%5D=Escherichia+coli&organism%5B%5D=Escherichia+coli+K-12.
- ↑ "Primary Amine Oxidase of Escherichia coli Is a Metabolic Enzyme that Can Use a Human Leukocyte Molecule as a Substrate". PLOS ONE 10 (11): e0142367. 2015. doi:10.1371/journal.pone.0142367. PMID 26556595. Bibcode: 2015PLoSO..1042367E.
External links
- Primary-amine+oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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