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 |
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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. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(72)90559-1 |