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- W2004507462 abstract "A prolyl RNA synthetase isolated from sonic extracts of Escherichia coli 9723 has been purified approximately 20-fold using conventional enzyme purification techniques. The purified enzyme catalyzes both an l-proline-dependent adenosine triphosphate-inorganic pyrophosphate exchange and a transfer of l-proline-C14 to soluble ribonucleic acid (sRNA). dl-3,4-Dehydroproline competitively inhibits the transfer of proline-C14 to sRNA, but does not inhibit the proline-dependent ATP-PPi exchange. Rather, a 3,4-dehydroproline-dependent ATP-PPi exchange catalyzed by the prolyl RNA synthetase can be demonstrated. A 4-hydroxy-l-proline-dependent ATP-PPi exchange is also catalyzed by the enzyme when high concentrations of this imino acid are employed. Hydroxyproline at relatively high concentrations is not an effective inhibitor of the transfer of proline-C14 to sRNA. Some of the properties and conditions for optimal activity of the purified enzyme are reported." @default.
- W2004507462 created "2016-06-24" @default.
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- W2004507462 date "1964-01-01" @default.
- W2004507462 modified "2023-10-11" @default.
- W2004507462 title "Purification and properties of the prolyl RNA synthetase of Escherichia coli" @default.
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- W2004507462 doi "https://doi.org/10.1016/0003-9861(64)90167-5" @default.
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