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

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 186卷 / 02期

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.

引用

页码：286 / &

共 18 条

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