Utilization of Selenocysteine by a Cysteinyl-tRNA Synthetase from Phaseolus aureus

Abstract
An L-cysteinyl-tRNA synthetase (EC 6.1.1.16) from P. aureus was purified approximately 200-fold. The enzyme uses selenocysteine as substrate in the ATP-PPi exchange assay; other cysteine analogs were inactive. The MW as determined by Sephadex G-200 column chromatography is about 61,000; sodium dodecyl sulfate and 8 M urea acrylamide gel electrophoresis indicate that the enzyme is a dimer consisting of 2 identical monomers of MW 30,000. A method for the preparation of selenocysteine from selenocystine is described.

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