Ribozyme-Catalyzed Amirloacylation from CoA Thioesters

Document Type

Article

Publication Date

3-22-2005

Department

Chemistry and Biochemistry

School

Mathematics and Natural Sciences

Abstract

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.

Publication Title

Biochemistry

Volume

44

Issue

11

First Page

4582

Last Page

4590

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