Journal Article

Action of Polyamine Aminotransferase on Norspermidine

Takamitsu Yorifuji, Shinya Kondo, Takashi Naka, Tohru Ishihara and Eiichi Shimizu

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 122, issue 3, pages 544-549
Published in print September 1997 | ISSN: 0021-924X
Published online September 1997 | e-ISSN: 1756-2651 | DOI:
Action of Polyamine Aminotransferase on Norspermidine

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The norspermidine-pyruvate reaction catalyzed by polyamine aminotransferase from Arthrobacter sp. TMP-1 formed N-3-aminopropyl-3-aminopropionaldehyde (APAPAL), L-alanine, 1,3-diaminopropane (DAP), allylamine, and acrolein, and the relative rates of formation of the latter four products were 24, 3.3, 2.3, and 1.2%, respectively, of the rate of the DAP-pyruvate transamination. The identification of APAPAL was done by 13C-NMR after it had been enzymatically oxidized to N-3-aminopropyl-β-alanine followed by isolation of the oxidized product. The DAP was also isolated and identified by 13C-NMR. The allylamine and acrolein were identified by HPLC and a specific color reaction with m-aminophenol, respectively. In the absence of pyruvate, the enzyme catalyzed the elimination of DAP from norspermidine to yield allylamine, and the addition of DAP to allylamine to yield norspermidine with relative rates of 0.007 and 0.095%, respectively. When allylamine was incubated with the enzyme as the sole substrate, it was converted to N-allyl- 1,3-diaminopropane and an unidentified product.

Keywords: acrolein; 1,3-diaminopropane; elimination and addition; norspermidine; polyamine aminotransferase

Journal Article.  0 words. 

Subjects: Biochemistry

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