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

[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.

[学科分类] 生物化学/生物物理

[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