Open AccessSubstrate Specificity of Escherichia coli Peptidyl‐Transferase
Author(s) -
Panet Amos,
Groot Nathan,
Lapidot Yehuda
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb00998.x
Subject(s) - puromycin , transfer rna , peptidyl transferase , substrate (aquarium) , chemistry , amino acid , escherichia coli , aminoacyl trna , biochemistry , ribosomal rna , stereochemistry , biology , ribosome , protein biosynthesis , rna , ecology , gene
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 AA 2 ‐Phe‐tRNA using three different amino acids (AA) were compared. At 4° all the three dipeptidyl‐tRNAs Phe reacted considerably slower than the three tripeptidyl‐tRNAs Phe . Acetyl‐Phe‐tRNA reacted faster than the dipeptidyl‐tRNA, but slower than the tripeptidyl‐tRNA. Gly n ‐Phe‐tRNA ( n = 3, 6 and 9) reacted with puromyein much faster than Gly‐Phe‐tRNA and at a rate similar to that of Gly 2 ‐Phe‐tRNA. Lauroyl‐Phe‐tRNA reacted with puromyein much slower than acetyl‐and octanoyl‐Phe‐tRNA both at 4° and 30°