Substrate Specificity of Escherichia coli Peptidyl‐Transferase

Amos Panet*, Nathan de Groot, Yehuda Lapidot

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

The kinetics of the puromycin interaction with different ribosomal bound peptidyl‐tRNAs were studied. The rates of the puromycin reaction with AA‐Phe‐tRNA and AA2‐Phe‐tRNA using three different amino acids (AA) were compared. At 4° all the three dipeptidyl‐tRNAsPhe reacted considerably slower than the three tripeptidyl‐tRNAsPhe. Acetyl‐Phe‐tRNA reacted faster than the dipeptidyl‐tRNA, but slower than the tripeptidyl‐tRNA. Glyn‐Phe‐tRNA (n= 3, 6 and 9) reacted with puromyein much faster than Gly‐Phe‐tRNA and at a rate similar to that of Gly2‐Phe‐tRNA. Lauroyl‐Phe‐tRNA reacted with puromyein much slower than acetyl‐and octanoyl‐Phe‐tRNA both at 4° and 30°

Original languageEnglish
Pages (from-to)222-225
Number of pages4
JournalEuropean Journal of Biochemistry
Volume15
Issue number2
DOIs
StatePublished - Aug 1970

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