Peptidyl transferase substrate activity and inhibition of protein biosynthesis by a hydrophilic-aminoacyl analogue of puromycin

A puromycin analogue possessing a hydrophilic amino acid, 3′-N-[S-(6-hydroxyhexyl)- L -cysteinyl]puromycin aminonucleoside, has been prepared and examined as a substrate for ribosomal peptidyl transferase. Kinetic studies indicate that this non-aromatic aminoacyl analogue is 95.6% as efficient as th...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 81; no. 2; pp. 559 - 564
Main Authors Vince, Robert, Fong, Kei-Lai L.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 30.03.1978
Subjects
Acyltransferases - metabolism
Escherichia coli - metabolism
Kinetics
Peptidyl Transferases - metabolism
Protein Biosynthesis - drug effects
Puromycin - analogs & derivatives
Puromycin - pharmacology
Ribosomes - metabolism
RNA, Transfer - metabolism
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Summary:A puromycin analogue possessing a hydrophilic amino acid, 3′-N-[S-(6-hydroxyhexyl)- L -cysteinyl]puromycin aminonucleoside, has been prepared and examined as a substrate for ribosomal peptidyl transferase. Kinetic studies indicate that this non-aromatic aminoacyl analogue is 95.6% as efficient as the parent antibiotic in the transpeptidation reaction. In addition, the analogue is an effective inhibitor of poly (U) and poly (U,C) directed protein synthesis in an Escherichia coli cell free system.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(78)91571-1