Surf Wiki
Save to docs
general/ec-1-4-3

From Surf Wiki (app.surf) — the open knowledge base

Primary-amine oxidase

Class of enzymes

Class of enzymes

FieldValue
NamePrimary-amine oxidase
EC_number1.4.3.21
image2c10.jpg
width270
captionAmine oxidase (semicarbazide-sensitive) dimer, Human

Primary-amine oxidase, also known as semicarbazide-sensitive amine oxidase (SSAO), is an enzyme () with the systematic name primary-amine:oxygen oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction

: RCH2NH2 + H2O + O2 \rightleftharpoons 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.

Human proteins containing this domain

  • AOC2
  • AOC3

Bacterial proteins containing this domain

  • Tyramine oxidase (tynA) in Escherichia coli

References

References

  1. "Primary-amine oxidase". International Union of Biochemistry and Molecular Biology.
  2. (Nov 2011). "Vascular cell lines expressing SSAO/VAP-1: a new experimental tool to study its involvement in vascular diseases". Biology of the Cell.
  3. (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.
  4. (Jul 1995). "Cloning and molecular analysis of the pea seedling copper amine oxidase". The Journal of Biological Chemistry.
  5. (Mar 1996). "Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects". The International Journal of Biochemistry & Cell Biology.
  6. (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.
  7. (Jul 1998). "Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini". The Journal of Biological Chemistry.
  8. (1999). "Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions". [[APMIS]].
  9. (Feb 2001). "Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase". The Journal of Histochemistry and Cytochemistry.
  10. (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.
  11. (Jan 2004). "Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do". Neurotoxicology.
  12. (Aug 2005). "Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications". Protein Science.
  13. (2008). "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.
  14. (2006). "Design, synthesis, and biological evaluation of semicarbazide-sensitive amine oxidase (SSAO) inhibitors with anti-inflammatory activity". Journal of Medicinal Chemistry.
  15. "EC 1.4.3.21 – primary-amine oxidase and Organism(s) Escherichia coli, Escherichia coli K-12". Technische Universität Braunschweig.
  16. (2015). "Primary Amine Oxidase of Escherichia coli Is a Metabolic Enzyme that Can Use a Human Leukocyte Molecule as a Substrate". PLOS ONE.
Info: Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

ec-1.4.3
Want to explore this topic further?

Ask Mako anything about Primary-amine oxidase — get instant answers, deeper analysis, and related topics.

Research with Mako

Free with your Surf account

Content sourced from Wikipedia, available under CC BY-SA 4.0.

This content may have been generated or modified by AI. CloudSurf Software LLC is not responsible for the accuracy, completeness, or reliability of AI-generated content. Always verify important information from primary sources.

Report