PEPTIDYL-TRNA .7. SUBSTRATE SPECIFICITY OF PEPTIDYL-TRNA HYDROLASE

被引:28
作者
DEGROOT, N
GRONER, Y
LAPIDOT, Y
机构
[1] Department of Biological Chemistry, The Hebrew University of Jerusalen, Jerusalem
关键词
D O I
10.1016/0005-2787(69)90006-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. © 1969.
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页码:286 / &
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