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pubmed-article:6553233pubmed:abstractTextCan a queuine-specific tRNA function normally without replacement of G by Q in its structure? To answer this, kinetics of aspartate queuine-containing tRNA (Q-tRNA) is compared with its queuine-deficient counterpart (G-tRNA). The results indicate that Asp Q-tRNA is a more effective substrate than the Asp G-tRNA. The Asp Q-tRNA exhibits a higher reaction velocity (Vmax greater than 30%) and a higher reaction rate (Km less than 55%) than its counterpart. The Asp tRNAs derived from human tumor lines and grown in athymic mice contain a full complement of queuine. This tumor tRNA exhibits aminoacylation kinetics similar to a normal liver tRNA. Reasons for observing the lack of a G-to-Q modification in cancer tRNAs by others are hypothesized. Two purified Asp isoacceptors from liver are compared for the aminoacylation reaction; small differences are noted in the Vmax, but none in the Km values.lld:pubmed
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pubmed-article:6553233pubmed:authorpubmed-author:SinghalR PRPlld:pubmed
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pubmed-article:6553233pubmed:articleTitleThe role of queuine in the aminoacylation of mammalian aspartate transfer RNAs.lld:pubmed
pubmed-article:6553233pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:6553233pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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