Ribozyme-Catalyzed Amirloacylation from CoA Thioesters
Chemistry and Biochemistry
Coenzyme A (CoA) thioesters play essential roles in modern metabolism. To demonstrate plausible biochemical functions of thioesters in the RNA world, we have isolated a new class of ribozymes (ACT) that catalyze self-aminoacylation from a number of CoA thioesters with catalytic efficiencies ranging from 7000 to 24 000 M-1·min-1. Active thioester substrates are required to contain both a free α-amino group in the acyl moiety and a CoA as the thiol component. We hypothesize ribozyme-based aminoacylation systems using aminoacyl thioesters of CoA as the ancestors of modern aminoacyl tRNA synthetases. On the basis of our previous results [Huang et al. (2000) Biochemistry 39, 15548−15555; Coleman and Huang (2002) Chem. Biol. 9, 1227−1236], an extensive RNA-catalyzed “metabolic pathway” involving CoA and its thioesters is proposed. Complex contemporary metabolic systems could have evolved from the proposed ribozyme pathways.
(2005). Ribozyme-Catalyzed Amirloacylation from CoA Thioesters. Biochemistry, 44(11), 4582-4590.
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