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

Robert Vince; Kei Lai L. Fong

doi:10.1016/0006-291X(78)91571-1

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

Robert Vince, Kei Lai L. Fong

Center for Drug Design

Research output: Contribution to journal › Article › peer-review

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Abstract

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.

Original language	English (US)
Pages (from-to)	559-564
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	81
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(78)91571-1
State	Published - Mar 30 1978

Bibliographical note

Funding Information:
We thank Jay Brownell investigation was supported Research Career Development Cancer Institute, DHEW.

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abstract = "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.",

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AB - 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.

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

Abstract

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