Arginine aminopeptidase activity of phytopathogenic spiroplasmas

Isr J Med Sci. 1984 Oct;20(10):1022-4.

Abstract

The arginine aminopeptidase activity of arginine-utilizing phytopathogenic spiroplasmas was investigated with arginine beta-naphthylamide substrate using the fluorometric method. Hydrolysis of this substrate was demonstrated with broth cultures, washed concentrated whole cells, and cell-free extracts of corn stunt spiroplasma (CSS) and Spiroplasma citri. Growing CSS and S. citri in the presence of 47 mM arginine resulted in a reduction in aminopeptidase activity, indicating that synthesis of the enzyme might be subject to control by catabolic repression. Results of these experiments suggest a possible biochemical basis for pathogenicity of phytopathogenic spiroplasmas in vivo.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aminopeptidases / biosynthesis
  • Aminopeptidases / metabolism*
  • Arginine / metabolism
  • Enzyme Repression
  • Plants / microbiology
  • Spiroplasma / enzymology*

Substances

  • Arginine
  • Aminopeptidases
  • aminopeptidase B