S-adenosylmethionine (SAM) synthetase was purified to homogeneity from soybean (Glycine max) axes. The enzyme was purified 216-fold with a 1.5% yield by ammonium sulfate fractionation, acetone fractionation, ion exchange chromatography with DEAE-sephacel, gel filtration with Sephacryl S-300, and afffinity chromatography with ATP-agarose. The enzyme activity reached a maximum 3 days after germination. SAM synthetase had a subunit molecular weight of 57,000 daltons from a silver stained single band on SDS-PAGE. The molecular weight of the enzyme was 110,000 daltons from Sephacryl S-300 gel filtration. The enzyme was composed of two identical subunits. The $K_m$ values of the enzyme for L-methionine and ATP were 1.81 and 1.53 mM, respectively. The enzymatic activity was not affected by polyamines, agmatine, or SAM analogues, but was inhibited by SAM. The inhibition pattern was showed non-competitive for L-methionine and uncompetitive for ATP. The activity of SAM synthetase was inhibited by thiol-blocking reagents. The enzyme was induced by treatment with $10^{-3}$ M putrescine at germination. Experimental data revealed a possible novel regulation mechanism of polyamine biosynthesis through several endogenous intermediates.