Identification of N1-acetylnorspermidine in Vibrio parahaemolyticus and an enzyme activity responsible for its formation

Shigeo Yamamoto, Hiroshi Nakao, Yasuyoshi Koumoto, Sumio Shinoda

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

N1-Acetylnorspermidine [CH3CONH(CH2)3NH(CH2)3NH3] was identified in Vibrio parahaemolyticus, which contains norspermidine as a major polyamine. This is the first example for the natural occurence of monoacetylated unusual polyamine. The N1-acetylnorspermidine content was the highest 4 h after inoculation. Incubation of norspermidine and acetyl CoA with a cell extract from V. parahaemolyticus produced N1-acetylnorspermidine. A remarkable increase in specific activity of the acetyltransferase was observed at the exponential phase of growth. Spermidine also served as a substrate for the enzyme, with the formation of two isomers of the acetylspermidines (N1-acetylspermidine was predominant), but the reaction rate was less than 50% of that with norspermidine. These results suggest that norspermidine in V. parahaemolyticus may be associated with the cell growth and its role may be controlled through acetylation, as reported for spermidine in Escherichia coli.

Original languageEnglish
Pages (from-to)225-230
Number of pages6
JournalFEMS Microbiology Letters
Volume61
Issue number1-2
DOIs
Publication statusPublished - Oct 1 1989
Externally publishedYes

Keywords

  • Acetyltransferase
  • Norspermidine
  • Polyamine acetylation

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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