Interaction of Glycyl-L-phenylalanine with Escherichia coli Phenylalanyl-tRNA Synthetase

Sidney M. Hecht; S. D. Hawrelak

doi:10.1021/bi00721a015

Interaction of Glycyl-L-phenylalanine with Escherichia coli Phenylalanyl-tRNA Synthetase

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Abstract

The interaction of glycyl-L-phenylalanine with the phenylalanyl-tRNA synthetase from Escherichia coli has been studied by the attempted enzymatic acylation of tRNA with the dipeptide and with the dipeptidyl-AMP anhydride. Also measured were inhibition of the formation of phenylalanyl-tRNA^phe in the presence of glycyl-L-phenylalanine and the dipeptidyl-AMP analog, glycyl-L-phenylalaninol-AMP, as well as the inhibition of ATP-PP; exchange in the presence of certain amino alcohol-AMP analogs of aminoacyl adenylates. The results, which indicated specific recognition of the dipeptide and dipeptidyl-AMP anhydride by the phenylalanyl-tRNA synthetase, are of interest in terms of the mechanism by which preexisting proteins are excluded from incorporation onto tRNA.

Original language	English (US)
Pages (from-to)	4967-4975
Number of pages	9
Journal	Biochemistry
Volume	13
Issue number	24
DOIs	https://doi.org/10.1021/bi00721a015
State	Published - Nov 1 1974
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

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title = "Interaction of Glycyl-L-phenylalanine with Escherichia coli Phenylalanyl-tRNA Synthetase",

abstract = "The interaction of glycyl-L-phenylalanine with the phenylalanyl-tRNA synthetase from Escherichia coli has been studied by the attempted enzymatic acylation of tRNA with the dipeptide and with the dipeptidyl-AMP anhydride. Also measured were inhibition of the formation of phenylalanyl-tRNAphe in the presence of glycyl-L-phenylalanine and the dipeptidyl-AMP analog, glycyl-L-phenylalaninol-AMP, as well as the inhibition of ATP-PP; exchange in the presence of certain amino alcohol-AMP analogs of aminoacyl adenylates. The results, which indicated specific recognition of the dipeptide and dipeptidyl-AMP anhydride by the phenylalanyl-tRNA synthetase, are of interest in terms of the mechanism by which preexisting proteins are excluded from incorporation onto tRNA.",

author = "Hecht, {Sidney M.} and Hawrelak, {S. D.}",

year = "1974",

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doi = "10.1021/bi00721a015",

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volume = "13",

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T1 - Interaction of Glycyl-L-phenylalanine with Escherichia coli Phenylalanyl-tRNA Synthetase

AU - Hecht, Sidney M.

AU - Hawrelak, S. D.

PY - 1974/11/1

Y1 - 1974/11/1

N2 - The interaction of glycyl-L-phenylalanine with the phenylalanyl-tRNA synthetase from Escherichia coli has been studied by the attempted enzymatic acylation of tRNA with the dipeptide and with the dipeptidyl-AMP anhydride. Also measured were inhibition of the formation of phenylalanyl-tRNAphe in the presence of glycyl-L-phenylalanine and the dipeptidyl-AMP analog, glycyl-L-phenylalaninol-AMP, as well as the inhibition of ATP-PP; exchange in the presence of certain amino alcohol-AMP analogs of aminoacyl adenylates. The results, which indicated specific recognition of the dipeptide and dipeptidyl-AMP anhydride by the phenylalanyl-tRNA synthetase, are of interest in terms of the mechanism by which preexisting proteins are excluded from incorporation onto tRNA.

AB - The interaction of glycyl-L-phenylalanine with the phenylalanyl-tRNA synthetase from Escherichia coli has been studied by the attempted enzymatic acylation of tRNA with the dipeptide and with the dipeptidyl-AMP anhydride. Also measured were inhibition of the formation of phenylalanyl-tRNAphe in the presence of glycyl-L-phenylalanine and the dipeptidyl-AMP analog, glycyl-L-phenylalaninol-AMP, as well as the inhibition of ATP-PP; exchange in the presence of certain amino alcohol-AMP analogs of aminoacyl adenylates. The results, which indicated specific recognition of the dipeptide and dipeptidyl-AMP anhydride by the phenylalanyl-tRNA synthetase, are of interest in terms of the mechanism by which preexisting proteins are excluded from incorporation onto tRNA.

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JO - Biochemistry

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Interaction of Glycyl-L-phenylalanine with Escherichia coli Phenylalanyl-tRNA Synthetase

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