Utilization of Selenocysteine by a Cysteinyl-tRNA Synthetase from Phaseolus aureus1
AUTOR(ES)
Shrift, Alex
RESUMO
An l-cysteinyl-tRNA synthetase (EC 6.1.1.16) from Phaseolus aureus has been purified approximately 200-fold. The enzyme uses selenocysteine as substrate in the ATP-PPi exchange assay; other cysteine analogs were inactive. The molecular weight 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 two identical monomers of molecular weight 30,000. A method for the preparation of selenocysteine from selenocystine is described.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=542225Documentos Relacionados
- Cysteinyl-tRNA Synthetase from Phaseolus aureus: Purification and Properties 1
- Cysteinyl-tRNA Synthetase from Astragalus Species 1
- Cysteinyl-tRNA Synthetase from Astragalus Species
- Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase
- Cysteine Activation in Cultured Cystinotic Cells THE SPECIFIC ACTIVITY OF CYSTEINYL-tRNA SYNTHETASE AND tRNACys AND THE DETERMINATION OF THE MICHAELISMENTEN CONSTANTS FOR CYSTEINYL-tRNA SYNTHETASE
