期刊论文详细信息
FEBS Letters | |
Nicking of the tryptophan synthase β2‐subunit at Glu‐296 prevents the conformational change undergone on binding the α‐subunit | |
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
【 预 览 】
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