Propylamine transferase, which catalyzes the biosynthesis of spermidine from 1,4-diaminobutane (putrescine) and decarboxylated adenosylmethionine, has been purified to homogeneity (approximately 2,000-fold) from Escherichia coli W. The enzyme has a molecular weight of approximately 73,000 and is composed of 2 subunits of equal size. 1,5-Diaminopentane and spermidine can replace 1,4-diaminobutane as the propylamine acceptor, but the reaction takes place at a reduced rate.
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Bowman et al. (1973) studied this question.
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