Cysteinyl-tRNA Synthetase from Phaseolus aureus: Purification and Properties

Plant Physiol. 1977 Nov;60(5):670-4. doi: 10.1104/pp.60.5.670.

Abstract

l-Cysteinyl-tRNA synthetase (EC 6.1.1.16) from Phaseolus aureus was purified approximately 300-fold and was free of contaminating aminoacyl-tRNA synthetases. Optimum assay conditions were determined and substrate specificity and inhibitor properties were investigated using the ATP-PPi exchange reaction. The Km values for l-cysteine, ATP, and PPi were 6.20 x 10(-5)m, 1.15 x 10(-3)m, and 1 x 10(-3)m, respectively. Both l-selenocysteine (Km = 5 x 10(-5)m) and alpha-l-aminobutyric acid (Km = 1 x 10(-2)m) acted as alternative substrates of the purified cysteinyl-tRNA synthetase. The enzyme was sensitive to sulfhydryl group reagents; it was inhibited by sulfide, 0-acetylserine, and reduced glutathione.