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- W1985397746 abstract "Cysteinyl- and methionyl-tRNA synthetases (EC 6.1.1.-) were purified 1200and 1000-fold, respectively, from sonic extracts of Paracoccus denitrificans strain 8944, and kinetics, substrate specificity and regulatory properties were determined using the ATP-PPi exchange reaction. Both enzymes had pH optima of approx. 8 and were inhibited by sulphydryl-group reagents.Cysteinyl-tRNA synthetase catalysed l-selenocysteine- and α-aminobutyric acid-dependent ATP-PPi exchange and methionyl-tRNA synthetase catalysed l-homocysteine-, l-selenomethionine- and norleucine-dependent ATP-PPg exchange. Both enzymes were inhibited by O-acetylserine. Cysteinyl-tRNA synthetase activity was stimulated by methionine and methionyl-tRNA synthetase activity was stimulated by sulphide, cysteine, and cysteic acid." @default.
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- W1985397746 date "1967-07-01" @default.
- W1985397746 modified "2023-10-02" @default.
- W1985397746 title "Evidence for a methionyl residue in the active site of isocitrate dehydrogenase" @default.
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- W1985397746 doi "https://doi.org/10.1016/0006-291x(67)90433-0" @default.
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