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Enzyme Activity Measurement for Primary-Amine Oxidase

Creative Enzymes develops exclusive and unique enzyme activity assays to stand out in the marketplace. Our products are the most trusted, accurate, and proven, resulting in a high rate of repeat sales. Thus Creative Enzymes has enough confidence to provide most precise activity measurement for primary-amine oxidase to the customers.

Primary-amine oxidase (EC 1.4.3.21) is an enzyme that catalyzes the oxidation of primary amines to produce corresponding aldehydes with concomitant reduction of molecular oxygen and water to ammonia and hydrogen peroxide, which can be concluded as following reaction formula (in which R represents aromatic or aliphatic moieties):

R-CH2-NH2 + H2O + O2 → R-CHO + NH3 + H2O2

Primary-amine oxidase oxidizes primary monoamines but has little or even no activity towards diamines, such as histamine, or towards secondary and tertiary amines. Primary-amine oxidase is ubiquitous which can be found in plants, bacteria and mammals, and it is a homodimeric enzyme with each monomer containing a copper ion and a covalently bound redox factor, topaquinone (TPQ). This enzyme belongs to the oxidoreductase family, and the systematic name of this enzyme class is amine:oxygen oxidoreductase (deaminating) (copper-containing). In addition, other names in common use include:

  • amine oxidase (ambiguous);
  • amine oxidase (copper-containing);
  • amine oxidase (pyridoxal containing) (incorrect);
  • benzylamine oxidase (incorrect);
  • CAO (ambiguous);
  • copper amine oxidase (ambiguous);
  • Cu-amine oxidase (ambiguous);
  • Cu-containing amine oxidase (ambiguous);
  • diamine oxidase (incorrect);
  • diamino oxhydrase (incorrect);
  • histamine deaminase (ambiguous);
  • histamine oxidase (ambiguous);
  • monoamine oxidase (ambiguous);
  • plasma monoamine oxidase (ambiguous);
  • polyamine oxidase (ambiguous);
  • semicarbazide-sensitive amine oxidase (ambiguous);
  • SSAO (ambiguous)

The crystal structure of copper-containing amine oxidase from Escherichia coli. Figure: The crystal structure of copper-containing amine oxidase from Escherichia coli.
PDB: 1LVN

Note that primary-amine oxidase also plays a pivotal role in seven pathways: glycine, serine and threonine metabolism; tyrosine metabolism; phenylalanine metabolism; beta-alanine metabolism; isoquinoline alkaloid biosynthesis; tropane, piperidine and pyridine alkaloid biosynthesis; and biosynthesis of secondary metabolites. Additionally, primary-amine oxidases from bacteria have a role in the utilization of primary amines as a source of nitrogen or carbon; primary-amine oxidases from eukaryotes have multiple functions including cell adhesion, cell signaling, cell growth, wound healing and detoxification. In human, three types of primary-amine oxidases have been identified, which are closely related with chronic vascular and neurobiological disorders, such as diabetic complications, atherosclerosis, and neurodegenerative disease. At this point, it can be concluded that primary-amine oxidase is an important enzyme in the biological, medical and pharmaceutical industries. However, the activity assay of primary-amine oxidase has not been well established by using spectrophotometric assays even though it has so many great values. Fortunately, Creative Enzymes is proud to make the most accurate activity assay available for primary-amine oxidase, based on years of extensive experiences in testing the enzymes and optimizing the methods. Over years, Creative Enzymes has continued growing with the same entrepreneurial and innovative spirit, and we are absolutely your best choice during development of products involving primary-amine oxidase.

Our Products Cannot Be Used As Medicines Directly For Personal Use.