Literature DB >> 16668008

Oxidation of spermine by an amine oxidase from lentil seedlings.

A Cogoni1, A Padiglia, R Medda, P Segni, G Floris.   

Abstract

Spermine is a substrate of lentil (Lens culinaris) seedling amine oxidase and the oxidation products are reversible inactivators of the enzyme. The spermine is oxidized at the terminal amino groups to a dialdehyde: 2 moles of hydrogen peroxide and 2 moles of ammonia per mole of spermine are formed. The pH optimum of the enzyme with spermine is 7.9 in TI-HCI buffer; the K(m) value is 4.4.10(-4) molar, similar to that found with other substrates (putrescine and spermidine).

Entities:  

Year:  1991        PMID： 16668008      PMCID： PMC1077555          DOI： 10.1104/pp.95.2.477

Source DB:  PubMed          Journal:  Plant Physiol        ISSN： 0032-0889            Impact factor:   8.340


  10 in total

1.  IDENTIFICATION OF THE AMINOALDEHYDES PRODUCED BY THE OXIDATION OF SPERMINE AND SPERMIDINE WITH PURIFIED PLASMA AMINE OXIDASE.

Authors:  C W TABOR; H TABOR; U BACHRACH
Journal:  J Biol Chem       Date:  1964-07       Impact factor: 5.157

2.  Further studies of a spectrophotometric method for the determination of diamine oxidase activity.

Authors:  B HOLMSTEDT; L LARSSON; R THAM
Journal:  Biochim Biophys Acta       Date:  1961-03-18

3.  Acrolein. IV. Evidence for the formation of the cytotoxic aldehyde acrolein from enzymatically oxidized spermine or spermidine.

Authors:  R A Alarcon
Journal:  Arch Biochem Biophys       Date:  1970-04       Impact factor: 4.013

4.  Enzymic assay for spermine and spermidine.

Authors:  U Bachrach; B Reches
Journal:  Anal Biochem       Date:  1966-10       Impact factor: 3.365

5.  Preparation and stability of oxidized polyamines.

Authors:  B W Kimes; D R Morris
Journal:  Biochim Biophys Acta       Date:  1971-01-01

6.  A rapid and sensitive colorimetric assay of amine oxidase.

Authors:  B I Naik; R G Goswami; S K Srivastava
Journal:  Anal Biochem       Date:  1981-02       Impact factor: 3.365

7.  A simple routine method for mono and diamine oxidase estimation in human serum.

Authors:  G B Leyton
Journal:  Pathology       Date:  1981-04       Impact factor: 5.306

8.  Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase.

Authors:  E Hölttä
Journal:  Biochemistry       Date:  1977-01-11       Impact factor: 3.162

9.  Mechanism of action of plasma amine oxidase products released under anaerobic conditions.

Authors:  K A Berg; R H Abeles
Journal:  Biochemistry       Date:  1980-07-08       Impact factor: 3.162

10.  Transient kinetics of copper-containing lentil (Lens culinaris) seedling amine oxidase.

Authors:  A Bellelli; M Brunori; A Finazzi-Agró; G Floris; A Giartosi; A Rinaldi
Journal:  Biochem J       Date:  1985-12-15       Impact factor: 3.857
  10 in total
  2 in total

1.  Insights into polyamine metabolism: homospermidine is double-oxidized in two discrete steps by a single copper-containing amine oxidase in pyrrolizidine alkaloid biosynthesis.

Authors:  Mahmoud M Zakaria; Thomas Stegemann; Christian Sievert; Lars H Kruse; Elisabeth Kaltenegger; Ulrich Girreser; Serhat S Çiçek; Manfred Nimtz; Dietrich Ober
Journal:  Plant Cell       Date:  2022-05-24       Impact factor: 12.085

2.  Accumulation of Agmatine, Spermidine, and Spermine in Sprouts and Microgreens of Alfalfa, Fenugreek, Lentil, and Daikon Radish.

Authors:  Irena Kralj Cigić; Sašo Rupnik; Tjaša Rijavec; Nataša Poklar Ulrih; Blaž Cigić
Journal:  Foods       Date:  2020-05-01
  2 in total

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