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- W2063543271 abstract "The enzyme discadenine synthase, which transfers the 3-amino-3-carboxypropyl residue of S-adenosylmethionine to an acceptor, N6-isopentenyladenine, from the fruiting body of the cellular slime mold Dictyostelium discoideum, was purified 420-fold. Its apparent molecular mass was 82 000 Da and the isoelectric point was pH 5.8. The Km value for S-adenosylmethionine was 1.85 · 10−5 M and for benzyladenine was 7.0 · 10−7 M. In contrast to theenzyme which catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine in tRNAs, the present enzyme did not require Mg2+ and was not stimulated by ATP. Some other metal ions (Zn2+, Mn2+, Ca2+) showed inhibition at 10–100 mM." @default.
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- W2063543271 date "1986-03-01" @default.
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- W2063543271 title "Purification and some properties of discadenine synthase from Dictyostelium discoideum" @default.
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- W2063543271 doi "https://doi.org/10.1016/0304-4165(86)90106-6" @default.
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