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

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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
Volume35
Issue number2-3
DOIs
Publication statusPublished - Jul 1986

Keywords

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

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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