Competitive inhibition of nitric oxide synthase by p-aminobenzamidine, a serine proteinase inhibitor

Giorgio Venturini, Enea Menegatti, Paolo Ascenzi

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

p-Aminobenzamidine competitively inhibits bovine trypsin, human and bovine thrombin, and human plasmin, all of which act on substrates containing preferentially the L-arginyl side chain at their P 1 position. Considering the structural and functional similarity between p-aminobenzamidine and the L-arginyl side chain in trypsin-like serine proteinases, we investigated the interaction of p-aminobenzamidine with mouse brain nitric oxide synthase (NOS), which uses L-arginine as the substrate for generating NO and L-citrulline. p-Aminobenzamidine is a competitive NOS inhibitor (K(i) = 1.2 x 10 -4 M, at pH 7.5 and 37.0°C), but not an NO precursor. Therefore, p-aminobenzamidine affects the NO production and the trypsin-like serine proteinase action.

Original languageEnglish
Pages (from-to)88-90
Number of pages3
JournalBiochemical and Biophysical Research Communications
Volume232
Issue number1
DOIs
Publication statusPublished - Mar 6 1997

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Serine Proteinase Inhibitors
Nitric Oxide Synthase
Trypsin
Serine Proteases
Citrulline
Fibrinolysin
Substrates
Thrombin
Arginine
Brain
4-aminobenzamidine

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Competitive inhibition of nitric oxide synthase by p-aminobenzamidine, a serine proteinase inhibitor. / Venturini, Giorgio; Menegatti, Enea; Ascenzi, Paolo.

In: Biochemical and Biophysical Research Communications, Vol. 232, No. 1, 06.03.1997, p. 88-90.

Research output: Contribution to journalArticle

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