Purification and properties of carboxynorspermidine decarboxylase, a novel enzyme involved in norspermidine biosynthesis, from Vibrio alginolyticus

H. Nakao, S. Shinoda, S. Yamamoto

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A novel enzyme which catalyses the decarboxylation of carboxynorspermidine [H2N(CH2)3NHCH2CH2CH(NH2)COOH] to yield norspermidine [H2N(CH2)3NH(CH2)3NH2], one of the unusual polyamines, was purified to apparent homogeneity (3100-fold) from cells of Vibrio alginolyticus. The enzyme has an apparent M(r) of 86000, with a pI of 4.25, and is a dimer composed of identical subunits with an apparent M(r) of 43500. The K(m) for carboxynorspermidine was 175 μM and for pyridoxal 5'-phosphate, 4.8 μM. The purified preparation had a specific activity of 24.1 μmol norspermidine produced min-1 (mg protein)-1. Carboxyspermidine, a structural homologue, was able fully to replace carboxynorspermidine as a substrate, to produce spermidine, but neither 2,3-diaminopropionic acid, 2,4-diaminobutyric acid, ornithine nor lysine showed detectable substrate activity. The optimum pH was 8.25. Dithiothreitol greatly stimulated the enzyme activity, maximum stimulation being observed at more than 5 mM-dithiothreitol.

Original languageEnglish
Pages (from-to)1699-1704
Number of pages6
JournalJournal of General Microbiology
Volume136
Issue number9
Publication statusPublished - 1990

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Vibrio alginolyticus
Dithiothreitol
Enzymes
Decarboxylation
Pyridoxal Phosphate
Ornithine
Spermidine
Polyamines
Lysine
carboxynorspermidine decarboxylase
norspermidine
Proteins

ASJC Scopus subject areas

  • Microbiology

Cite this

Purification and properties of carboxynorspermidine decarboxylase, a novel enzyme involved in norspermidine biosynthesis, from Vibrio alginolyticus. / Nakao, H.; Shinoda, S.; Yamamoto, S.

In: Journal of General Microbiology, Vol. 136, No. 9, 1990, p. 1699-1704.

Research output: Contribution to journalArticle

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abstract = "A novel enzyme which catalyses the decarboxylation of carboxynorspermidine [H2N(CH2)3NHCH2CH2CH(NH2)COOH] to yield norspermidine [H2N(CH2)3NH(CH2)3NH2], one of the unusual polyamines, was purified to apparent homogeneity (3100-fold) from cells of Vibrio alginolyticus. The enzyme has an apparent M(r) of 86000, with a pI of 4.25, and is a dimer composed of identical subunits with an apparent M(r) of 43500. The K(m) for carboxynorspermidine was 175 μM and for pyridoxal 5'-phosphate, 4.8 μM. The purified preparation had a specific activity of 24.1 μmol norspermidine produced min-1 (mg protein)-1. Carboxyspermidine, a structural homologue, was able fully to replace carboxynorspermidine as a substrate, to produce spermidine, but neither 2,3-diaminopropionic acid, 2,4-diaminobutyric acid, ornithine nor lysine showed detectable substrate activity. The optimum pH was 8.25. Dithiothreitol greatly stimulated the enzyme activity, maximum stimulation being observed at more than 5 mM-dithiothreitol.",
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