High-performance liquid chromatography on an ion exchanger column was successfully used for a rapid biochemical analysis of crystals of yeast tRNAAsp and aspartyl-tRNA synthetase as well as cocrystals formed by the synthetase and the tRNA.
Interaction of aminoacyl-tRNA synthetases and tRNA: Positive and negative cooperativity of their active centres
โ Scribed by E. G. Malygin; V. V. Zinoviev; F. Fasiolo; L. L. Kisselev; L. L. Kochkina; V. Z. Achverdyan
- Publisher
- Springer
- Year
- 1976
- Tongue
- English
- Weight
- 420 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0301-4851
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โฆ Synopsis
The influence of tRNA on the kinetics of PP-ATP exchange and aminoacyl-tRNA formation catalysed by leucyl-, phenylalanyl-, and tryptophanyl-tRNA synthetases has been investigated. These enzymes were chosen because they belong to three main classes of quaternary structure t~l, ot2/32 and a2, respectively. The present paper shows that the investigated synthetases manifest kinetic cooperativity of the active centres which is negative in the case of AAA formation and positive in the case of leucyl-and tryptophanyl-tRNA synthesis. The obtained data were interpreted with the aid of the trigger model of the enzyme.
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Two nonhydrolyzable prolyl adenylate analogs, 5ะ-O-[N-(L-prolyl)-sulfamoyl]adenosine (L-PSA) and 5ะ-O-[N-(D-prolyl)-sulfamoyl]adenosine (D-PSA), were prepared in three steps from 2ะ,3ะ-di-O-isopropylideneadenosine. Both of these compounds inhibited the in vitro activity of Escherichia coli and human