Nicking of the tryptophan synthase β2‐subunit at Glu‐296 prevents the conformational change undergone on binding the α‐subunit

FEBS Letters

Djavadi-Ohaniance, Lisa¹  Goldberg, Michel E.¹  Linkens, Hans-Josef¹ 

[1] Unité de Biochimie Cellulaire, Institut Pasteur, 28, rue du Dr. Roux, 75724 Paris Cedex 15, France

关键词: Conformational change;    Tryptophan synthase;    Monoclonal antibody: Proteolytic cleavage: Ligand binding;    α;    β2;    α;    or β2 subunit of Escherichia coli tryptophan synthase;    reduced β2;    NaBH4;    reduced holo β2;    Ig;    immunoglobulin;    mAb;    monoclonal antibody;    SDS;    sodium dodecyl sulfate;    PEG 6000;    polyethyleneglycol with M r = 6;    000;    Pyridoxal-P;    pyridoxal 5'-phosphate: Tryptophan synthase;   

DOI  :  10.1016/0014-5793(93)80591-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Using a monoclonal antibody as conformational probe it has been shown that the weakly active nicked-β2 dimer of tryptophan synthase generated by proteolytic cleavage at Glu-296, does not undergo on association with α subunit a conformational change known to occur in intact β2 subunit. This α induced conformational change is also prevented in intact β2 by the coenzyme pyridoxal-5'-phosphate when the substrate l-serine is absent.

【 授权许可】

Unknown