ACTION OF POLYAMINE AMINOTRANSFERASE ON NORSPERMIDINE

The norspermidine-pyruvate reaction catalyzed by polyamine aminotransf erase from Arthrobacter sp, TMP-1 formed N-3-aminopropyl-3-aminopropio naldehyde (APAPAL), L-alanine, 1,3-diaminopropane (DAP), allylamine, a nd acrolein, and the relative rates of formation of the latter four pr oducts were 24, 3.3, 2.3, and 1.2%, respectively, of the rate of the D AP-pyruvate transamination. The identification of APAPAL was done by C -13-NMR after it had been enzymatically oxidized to N-3-aminopropyl-be ta-alanine followed by isolation of the oxidized product, The DAP was also isolated and identified by C-13-NMR, The allylamine and acrolein were identified by HPLC and a specific color reaction with m-aminophen ol, respectively. In the absence of pyruvate, the enzyme catalyzed the elimination of DAP from norspermidine to yield allylamine, and the ad dition 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-dia minopropane and an unidentified product.