Non-participation of aminoacyl adenylates in the spermine catalyzed aminoacylation of transfer-RNA

Igarashi et., al. (1) have reported that spermine catalyzes the overall reaction of aminoacylation of tRNA without catalyzing ATP:PPi exchange. Quantitation now shows that the rate of spermine catalyzed ATP:PPi exchange is only one twentieth that of spermine catalyzed esterification (and one ten tho...

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Veröffentlicht in:Biochemical and biophysical research communications 1972-05, Vol.47 (4), p.775-783
Hauptverfasser: Pastuszyn, Andrzej, Loftfield, Robert B.
Format: Artikel
Sprache:eng
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Zusammenfassung:Igarashi et., al. (1) have reported that spermine catalyzes the overall reaction of aminoacylation of tRNA without catalyzing ATP:PPi exchange. Quantitation now shows that the rate of spermine catalyzed ATP:PPi exchange is only one twentieth that of spermine catalyzed esterification (and one ten thousandths of the Mg 2+ catalyzed ATP:PPi exchange). This evidence is incompatible with the obligatory intermediate formation of Enz·(AA∼AMP) and PPi in the biosynthesis of AA-tRNA and is compatible with a concerted reaction of the three substrates and the enzyme to form three products including AA-tRNA.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(72)90559-1