Extended substrate specificity of serum amine oxidase: Possible involvement in protein posttranslational modification

Xintao Wang, Paola Pietrangeli, Mircea Alexandru Mateescu, Bruno Mondovi

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

The capacity of bovine serum amineoxidase (SAG) to oxidize free amino groups of nonconventional substrates, such as polylysine (up to 50 kDa) and some proteins as lysozyme and ribonuclease A, is described. The oxidation was quantified from the amount of H2O2, and NH3 enzymatically produced by SAG. Kinetic analysis indicated a stereospecific preference for L-configuration. Maximal oxidation rate was obtained with poly-L-lysine (9.6 kDa). After 10 h of incubation at 37°C, the poly-l-lysine was partially oxidized generating 1.5 moles of H2O2 by one mole of polylysine. Denatured SAO presented very low oxidation rates with the mentioned substrates.

Original languageEnglish (US)
Pages (from-to)91-97
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume223
Issue number1
DOIs
StatePublished - Jun 5 1996

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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