Peptidyl-tRNA VII. Substrate specificity of peptidyl-tRNA hydrolase

N. De Groot*, Y. Groner, Y. Lapidot

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

The enzymatic hydrolysis of peptidyl-tRNA is described. The hydrolysis rates of peptidyl-tRNA with different peptide chain lengths containing free and blocked α-amino groups are compared to the hydrolysis rates of N-acylaminoacyl-tRNA. It is shown that the hydrolysis rate of peptidyl-tRNA containing two peptide bonds is considerably higher than that of N-acylaminoacyl-tRNA. Moreover, the hydrolysis rate of different peptidyl-tRNA's depends on the peptide chain length. Thus, Gly2-Phe-tRNA is hydrolyzed faster than GlyPhe-tRNA, and Gly4Phe-tRNA is hydrolyzed faster than Gly2Phe-tRNA. The apparent Km and vmax values for Ac-Leu-tRNA are compared to those of Ala2Leu-tRNA.

Original languageEnglish
Pages (from-to)286-296
Number of pages11
JournalBBA Section Nucleic Acids And Protein Synthesis
Volume186
Issue number2
DOIs
StatePublished - 20 Aug 1969

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