Inhibitory effect of arginine-derivatives from ginseng extract and basic amino acids on protein-arginine N-methyltransferase

B. C. Yoo, Gil-Hong Park, H. Okuda, T. Takaku, S. Kim, Woo Ik Hwang

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Protein-arginine N-methyltransferase (protein methylase I) catalyzes methylation of arginyl residues on substrate protein posttranslationally utilizing S-adenosyl-L-methionine as the methyl donor and yields N(G)-methylarginine residues. Arginyl-fructose and arginyl-fructosyl-glucose from Korean red ginseng were found to inhibit protein methylase I activity in vitro. This inhibitory activity was shown to be due to arginyl moiety in the molecules, rather than that of carbohydrates. Several basic amino acids as well as polyamines were also found to inhibit protein methylase I activity. Interestingly, the intensity of the inhibitory activity was correlated with the number of amino-group in polyamines, thus, in the order of spermine > spermidine > putrescine > agmatine-sulfate, with IC50 at approximately 15 mM, 25 mM, 35 mM, and 50 mM, respectively. On the other hand, neutral amino acids or NaCl did not inhibit the enzyme activity. Lineweaver-Burk plot analysis of the protein methylase I activity in the presence of arginine and spermidine indicated that the inhibition was competitive in nature in respect to protein substrate, with the K(i) values of 24.8 mM and 11.5 mM, respectively.

Original languageEnglish
Pages (from-to)391-400
Number of pages10
JournalAmino Acids
Volume17
Issue number4
Publication statusPublished - 1999 Dec 1

Keywords

  • Amino acids
  • Arginine derivatives
  • Basic amino acids
  • Ginseng extract
  • Inhibitors
  • Polyamines
  • Protein-arginine methyltransferase

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Inhibitory effect of arginine-derivatives from ginseng extract and basic amino acids on protein-arginine N-methyltransferase'. Together they form a unique fingerprint.

  • Cite this