Phenylalanyl‐tRNA synthetase from <i>escherichia coli</i> MRE‐600

Lavrik, Olga I.; Nevinsky, G.A.

doi:10.1016/0014-5793(80)81300-7

Cited by 3 publications

(1 citation statement)

References 8 publications

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“…Attempts have been made to use analogs of aminoacyl adenylates for affinity modification of the synthetases. ATP Y-(p-azidobenzyl)-methylanilidate was shown to be a reversible competitive inhibitor of E. coli MRE-600 phenylalanyl-tRNA synthetase with respect to ATP and amino acid; UV-irradiation of the synthetase in the presence of this compound resulted in complete inactivation of the enzyme [8]. For methionyl-tRNA synthetase, despite the high affinity of methioninyl-8-azido-adenosine St-phosphate for the enzyme, only 5 -15% of the photoreactive analog was bound covalently [6].…”

Section: Introductionmentioning

confidence: 99%

Affinity labelling of tryptophanyl‐tRNA synthetase with mesitoyl‐AMP

Madoyan¹,

Фаворова²,

Kovaleva³

et al. 1981

FEBS Letters

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Section: Introductionmentioning

confidence: 99%

Affinity labelling of tryptophanyl‐tRNA synthetase with mesitoyl‐AMP

Madoyan¹,

Фаворова²,

Kovaleva³

et al. 1981

FEBS Letters

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Phenylalanyl-tRNA synthetase from E. coli MRE-600: analysis of the active site distribution on the enzyme subunits by affinity labelling

Ходырева

Moor

Ankilova

et al. 1985

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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Interaction of fluorescent ATP and tRNA analogs with phenylalanyl-tRNA synthetase

et al. 1988

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Введение. Этенопроизводные нуклеотидов широко используются для изучения структурно-функциональной топографии ферментов, зависимых от нуклеотидов [1]. Получены производные тРНК различной специфичности, содержащие остатки этеноаденозипа [2, 3]. Особый интерес представляет применение такого типа соединений в качестве аффинных реагентов для модификации белков. В работе [4] впервые обнаружена возможность ковалентного присоединения 1 ,Ы 6-этеиоадепозин-5 /-трифосфата (εΑΤΡ) к фенил аланил-тРНК синтетазе (КФ 6.1.1.20). Настоящая работа посвящена более детальному исследованию аффинной модификации фенил алан ил-тРН К синтетазы с помощью εΑΤΡ. Получены флюоресцентные аналоги τΡΗΚ ρί1β и исследовано их взаимодействие с сиптетазой.

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Phenylalanyl‐tRNA synthetase from escherichia coli MRE‐600

Cited by 3 publications

References 8 publications

Affinity labelling of tryptophanyl‐tRNA synthetase with mesitoyl‐AMP

Affinity labelling of tryptophanyl‐tRNA synthetase with mesitoyl‐AMP

Phenylalanyl-tRNA synthetase from E. coli MRE-600: analysis of the active site distribution on the enzyme subunits by affinity labelling

Interaction of fluorescent ATP and tRNA analogs with phenylalanyl-tRNA synthetase

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