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Spermidine Biosynthesis

PURIFICATION AND PROPERTIES OF PROPYLAMINE TRANSFERASE FROM ESCHERICHIA COLI

William H. Bowman 1, Celia White Tabor 1, and Herbert Tabor 1

From the 1 From the Laboratory of Biochemical Pharmacology, National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20014

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.

Submitted on October 2, 1972


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