Spermine oxidase: an amine oxidase with specificity for spermine and spermidine.

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  • Author(s): HIRSCH JG
  • Source:
    The Journal of experimental medicine [J Exp Med] 1953 Mar; Vol. 97 (3), pp. 345-55.
  • Publication Type:
    Journal Article
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Rockefeller University Press Country of Publication: United States NLM ID: 2985109R Publication Model: Print Cited Medium: Print ISSN: 0022-1007 (Print) Linking ISSN: 00221007 NLM ISO Abbreviation: J Exp Med Subsets: OLDMEDLINE
    • Publication Information:
      Original Publication: New York, NY : Rockefeller University Press
    • Subject Terms:
      Amine Oxidase (Copper-Containing)* ; Oxidation-Reduction* ; Oxidoreductases* ; Oxidoreductases Acting on CH-NH Group Donors* ; Spermidine* ; Spermine*; Animals ; Cattle ; Deamination ; Kinetics ; Sheep ; Substrate Specificity ; Polyamine Oxidase
    • Abstract:
      Sheep serum and bovine serum contain an enzyme which brings about a rapid oxidative deamination of certain biological amines. This enzyme differs from previously described amine oxidases in several regards and especially in its substrate specificity. Studies thus far indicate that only spermine and the closely related compound spermidine serve as substrates for the enzyme in sheep serum. For this reason, the enzyme has been named spermine oxidase. Spermine oxidase is active in a variety of fluids of various ionic strength and buffer composition. The reaction takes place between pH 6.0 and pH 8.0 with an optimal rate in the vicinity of neutrality. Under certain conditions, the rate of oxygen consumption during the initial phase of the reaction is independent of the concentration of substrate. The diminution in rate observed during the latter phase of the enzymatic attack appears to be due to an alteration in the kinetics at low concentrations of substrate, or to competitive inhibition by a product of the reaction. Carbonyl reagents almost completely block the action of spermine oxidase, while certain amines and the cyanide ion bring about partial inhibition. Thiol reagents and sequestering compounds do not alter the course of the oxidative process. In the presence of low concentrations of mercuric chloride, the sheep serum-spermine system consumes approximately twice as much oxygen as controls containing no mercuric ion. The mechanism by which the mercuric ion stimulates additional oxygen uptake is obscure.
    • References:
      Biochem J. 1945;39(5):478-81. (PMID: 16747942)
      J Exp Med. 1952 Feb;95(2):191-208. (PMID: 14907970)
      Biochem J. 1925;19(6):1034-6. (PMID: 16743594)
    • Contributed Indexing:
      Indexing Agency: CLML Local ID #: 5324:23362:465.
      Non-Mesh Headings: OXIDASES*
    • Accession Number:
      2FZ7Y3VOQX (Spermine)
      EC 1.- (Oxidoreductases)
      EC 1.4.3.21 (Amine Oxidase (Copper-Containing))
      EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors)
      U87FK77H25 (Spermidine)
    • Publication Date:
      Date Created: 19530301 Date Completed: 20030501 Latest Revision: 20231213
    • Publication Date:
      20231215
    • Accession Number:
      PMC2136271
    • Accession Number:
      10.1084/jem.97.3.345
    • Accession Number:
      13052805