Substrates: substrates mimic the entire acceptor stems of tRNAAla and tRNAGlu. Ala-miHxAla-7 is as good a substrate as Ala-tRNAAla at the first binding site. Glu-miHxGlu-7 is at least as good a substrate as Glu-tRNAGlu Products: -
Substrates: substrates mimic the entire acceptor stems of tRNAAla and tRNAGlu. Ala-miHxAla-7 is as good a substrate as Ala-tRNAAla at the first binding site. Glu-miHxGlu-7 is at least as good a substrate as Glu-tRNAGlu Products: -
Substrates: the acceptor arms of the two substrates are the only parts of the tRNAs required for CDPS activity. The enzyme shows strong preference for Glu-tRNAGlu as the second substrate Products: -
Substrates: the acceptor arms of the two substrates are the only parts of the tRNAs required for CDPS activity. The enzyme shows strong preference for Glu-tRNAGlu as the second substrate Products: -
synthesis and purification of shortened amino acid-tRNA analogues (AA-minitRNAs), by using flexizymes to aminoacylate a diversity of minitRNAs. Aminoacylated molecules mimicking the entire acceptor arms of tRNAs are as effective a substrate as entire AA-tRNAs
synthesis and purification of shortened amino acid-tRNA analogues (AA-minitRNAs), by using flexizymes to aminoacylate a diversity of minitRNAs. Aminoacylated molecules mimicking the entire acceptor arms of tRNAs are as effective a substrate as entire AA-tRNAs
Canu, N.; Tellier, C.; Babin, M.; Thai, R.; Ajel, I.; Seguin, J.; Cinquin, O.; Vinck, R.; Moutiez, M.; Belin, P.; Cintrat, J.C.; Gondry, M.
Flexizyme-aminoacylated shortened tRNAs demonstrate that only the aminoacylated acceptor arms of the two tRNA substrates are required for cyclodipeptide synthase activity
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