TY - JOUR
T1 - Peptidyl-tRNA VII. Substrate specificity of peptidyl-tRNA hydrolase
AU - De Groot, N.
AU - Groner, Y.
AU - Lapidot, Y.
PY - 1969/8/20
Y1 - 1969/8/20
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0014459302&partnerID=8YFLogxK
U2 - 10.1016/0005-2787(69)90006-9
DO - 10.1016/0005-2787(69)90006-9
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C2 - 4898482
AN - SCOPUS:0014459302
SN - 0005-2787
VL - 186
SP - 286
EP - 296
JO - BBA Section Nucleic Acids And Protein Synthesis
JF - BBA Section Nucleic Acids And Protein Synthesis
IS - 2
ER -