Since selenomethionine appears to be a better precursor of ethylene in senescing flower tissue of Ipomoe tricolor and in indole acetic acid-treated pea stem sections than is methionine (Konze JR, N Schilling, H Kende 1978 Plant Physiol 62: 397-401), we compared the effectiveness of selenomethionine and methioine to participate in reactions which may be connected to ethylne biosynthesis. Evidence is presented that selenomethionine is also a better substrate of methionine adenosyltransferase (ATP: methionine S-adenosyltransferase, EC 2.5.1.6) from L trolor, the V,"for selenomethionine being twice as high as that for methionine. The affinity of the enzyme is higher for methionine than for selnomthionine, however. Methionine added to flower tissue together with sekeomethionine inhibits the enhancement of ethylene synthesis by the seleno analog. Likewise, methioine reduces the high, selenomethionine-dependent reaction rates of methioine adenosyltransferase from L tricolor flower tissue. On the other hand, selenomethionine is less effective as an ethylene precursor than is methionine in model systems involving oxidation by free radicals. It was concluded that activation of methionine by methionine adenosyltransferase and formation of S-adenosylmethionine are more likely to be involved in ethylene biosynthesis than is oxidation ofmethionine by free radicals.In all plant tissues investigated thus far, methionine was found to be the precursor of ethylene (for reviews see refs. 13 and 22). Since methionine can be converted to ethylene in vitro via methional (14,20)