Substrate specificity of Escherichiacoli peptidyltransferase at the donor site
作者： James C.-H. Mao
DOI: 10.1016/0006-291X(73)90754-7
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摘要: Abstract The substrate specificity of E. coli peptidyltransferase at the donor site was investigated by “50S reaction”. Seventeen N-acetylated or unacetylated aminoacyl-tRNAs and dipeptidyl-tRNAs were used as substrates puromycin acceptor. Results indicated that nature amino acid side chain tRNA has a predominant effect on reaction rate peptidyltransferase. Amino acids dipeptides with high hydrophobicity transferred faster than those low hydrophobicity. alkyl chains are better donors aromatic chains. Substrates C-terminal proline extremely slowly which can probably be attributed to its unusual α-imino structure in addition
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