Characterization of a novel spermidine/spermine acetyltransferase, BltD, from Bacillus subtilis

Dale P. Woolridge, Jesse D. Martinez, David E. Stringer, Eugene W. Gerner

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


Overexpression of the BltD gene in Bacillus subtilis causes acetylation of the polyamines spermidine and spermine. BltD is co-regulated with another gene, Blt, which encodes a multidrug export protein whose overexpression facilitates spermidine export. Here we show that BltD acetylates both spermidine and spermine at primary propyl amine moieties, with spermine being the preferred substrate. In the presence of saturating concentrations of acetyl CoA, BltD rapidly acetylates spermine at both the N1 and N12 positions. The K(m) (app) values for spermine, spermidine and N1-acetylspermine are ≤ 67, 200 and 1200 μM, respectively. Diamines ranging from 1,3-diaminopropane to 1,12-diaminododecane, monoacetylputrescine and N8-acetylspermidine were not substrates for BltD. Putrescine (1,4-diaminobutane) and N8-acetylspermidine were competitive inhibitors of spermidine acetylation by BltD, with K(i) values of 0.25 and 5.76 mM, respectively. CoA competitively inhibited both spermidine and acetyl-CoA interactions with BltD. These data and other results indicate that the mechanism of spermidine and spermine acetylation by BltD is a random-order mechanism of bi-molecular kinetics.

Original languageEnglish (US)
Pages (from-to)753-758
Number of pages6
JournalBiochemical Journal
Issue number3
StatePublished - Jun 15 1999


  • Bacteria
  • Enzyme kinetics
  • Polyamine

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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