SPECIFICITY OF LINCOMYCIN ACTION ON PEPTIDYL TRANSFERASE-ACTIVITY

被引：7

作者：

CAMPBELL, JM

REUSSER, F

CASKEY, CT

机构：

[1] UPJOHN CO, RES LABS, KALAMAZOO, MI 49001 USA

[2] BAYLOR UNIV, COLL MED, DEPT MED, HOUSTON, TX 77030 USA

[3] BAYLOR UNIV, COLL MED, HOWARD HUGHES MED INST LAB, DEPT BIOCHEM, HOUSTON, TX 77030 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 90卷 / 03期

关键词：

D O I：

10.1016/0006-291X(79)91930-2

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 antibiotic lincomycin and 12 of its analogs were analyzed for their effects on 3 [Escherichia coli] peptidyl transferase reactions, peptide bond formation, esterification and hydrolysis of formylmethionyl-tRNA. Only lincomycin stimulated hydrolysis while having inhibitory effects on the other 2 reactions. The effects of the analogs were variable. Modifications at the C7 position or loss of the carbonyl group caused dramatic alterations in lincomycin activity. Most of the analogs inhibited all 3 reactions indicating that interaction with the ribosome is not sufficient to elicit the unique specificity of action observed with lincomycin.

引用

页码：1032 / 1038

页数：7

共 19 条

[11] SEPARATION OF 3 MICROBIAL AMINO ACID POLYMERIZATION FACTORS [J].