Purification and some properties of a novel L-2,4-diaminobutyric acid decarboxylase from Vibrio alginolyticus

H. Nakao, M. Ishii, S. Shinoda, S. Yamamoto

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Previous investigations have shown that members of the genus Vibrio possess a novel enzyme activity decarboxylating L-2,4-diaminobutyric acid (DABA) to 1,3-diaminopropane (DAP). In this paper we describe the purification, by about 3600-fold, of the enzyme from V. alginolyticus. The purified enzyme was apparently homogeneous, and had a specific activity of 4200 nmol DAP min-1 (mg protein)-1. The enzyme protein has an M(r) of 450000 ± 20000 and is apparently comprised of four identical subunits (M(r) 109000 ± 1000). Neither 2,3-dimainopropionic acid, ornithine, lysine nor arginine served as substrates. Some properties of the enzyme were determined. Cultivation of this bacterium in the presence of added DABA brought about increased production of norspermidine (NSPD), characteristically present in this species as well as DAP, suggesting that the enzyme may be functionally implicated in the formation of DAP, a biosynthetic precursor of NSPD.

Original languageEnglish
Pages (from-to)345-351
Number of pages7
JournalJournal of General Microbiology
Volume135
Issue number2
Publication statusPublished - 1989

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Vibrio alginolyticus
Enzymes
Acids
Ornithine
Vibrio
Lysine
Arginine
2,4-diaminobutyric acid decarboxylase
2,4-diaminobutyric acid
Proteins
Bacteria

ASJC Scopus subject areas

  • Microbiology

Cite this

Purification and some properties of a novel L-2,4-diaminobutyric acid decarboxylase from Vibrio alginolyticus. / Nakao, H.; Ishii, M.; Shinoda, S.; Yamamoto, S.

In: Journal of General Microbiology, Vol. 135, No. 2, 1989, p. 345-351.

Research output: Contribution to journalArticle

Nakao, H. ; Ishii, M. ; Shinoda, S. ; Yamamoto, S. / Purification and some properties of a novel L-2,4-diaminobutyric acid decarboxylase from Vibrio alginolyticus. In: Journal of General Microbiology. 1989 ; Vol. 135, No. 2. pp. 345-351.
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