The presence of l-2,4-diaminobutyric acid decarboxylase activity in Vibrio species: A new biosynthetic pathway for 1,3-diaminopropane

Shigeo Yamamoto, Yasuo Suemoto, Yumiko Seito, Hiroshi Nakao, Sumio Shinoda

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8 Citations (Scopus)


A new enzyme activity, which catalyzes decarboxylation of l-2,4-diaminobutyric acid (DABA) to yield 1,3-diaminopropane (DAP), has been found in dialyzed crude extracts prepared from Vibrio alginolyticus. The pH optimum for the activity was 8.0-8.5, and the enzyme showed a pyridoxal 5′-phosphate (PLP) requirement. Mg2+ caused about 30% stimulation in activity. The enzyme was active to only l-DABA among the diamino acids examined, and the Km value for l-DABA was 0.13 mM. Ammonium sulfate fractionation of a dialyzed crude extract followed by HPLC separation allowed us to conclude that this enzyme differed from the decarboxylase which occurs in Vibrio spp. to produce norspermidine (Nspd) for carboxynorspermidine (C-Nspd) having a moiety similar in structure to DABA. The same enzyme activity was detected in several other Vibrio species.

Original languageEnglish
Pages (from-to)289-293
Number of pages5
JournalFEMS Microbiology Letters
Issue number2-3
Publication statusPublished - 1986



  • polyamine
  • precursor of norspermidine
  • Pyridoxal 5′-phosphate-dependent enzyme

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Microbiology

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