Phenylalanyl‐tRNA synthetase from Thermus thermophilus HB8 Purification and properties of the crystallizing enzyme

FEBS Letters

Lavrik, O.I.¹  Chernaya, M.M.²  Reshetnikova, L.S.²  Ankilova, V.N.¹ 

[1] Institute of Bioorganic Chemistry, Siberian Division of the USSR Academy of Sciences, Novosibirsk 630090, USSR;Institute of Molecular Biology, the USSR Academy qf Sciences, Moscow 117986, USSR

关键词: Phenylalanyl-tRNA synthetase;    tRNAPhe;    Thermodynamic parameter;    Crystallization;    (Thermus thermophilus);    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(88)81403-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phenylalanyl-tRNA synthetase from Thermus thermophilus HB8 was isolated, characterized and crystallized. The enzyme is a tetramer of α₂β₂-type structure, its molecular mass being 264 kDa. Molecular masses of the enzyme subunits are 40 (α) and 92 (β) kDa. The optimal temperature conditions of the tRNA^Phe aminoacylation, catalyzed by this enzyme, are close to 80°C. K _M values for tRNA^Phe from E.coli, for tRNA^Phe from T. thermophilus HB8, for phenylalanine and ATP, as well as their temperature dependencies were determined. The enzyme crystals were grown by the hanging drop technique at 4°C in the presence of ammonium sulfate.

【 授权许可】

Unknown