Conformational modification of muscle phosphofructokinase from Jaculus orientalis upon ligand binding

FEBS Letters

El Hachimi, Z.²  Tijane, M.²  Yon, J.M.¹  Benjouad, A.²  Desmadril, M.¹ 

[1] Laboratoire d'Enzymologie Physico-chimique et Moléculaire, Groupe de Recherche du Centre National de la Recherche Scientifique associé à l'Université de Paris-Sud, 91405F Orsay, France;Laboratoire de Biochimie, Faculté des Sciences, Rabat, Morocco

关键词: Phosphofructokinase;    6-;    Allostery;    Conformational change;    PFK;    phosphofructokinase (EC 2.7.1.11);    Fru-6-P;    fructose 6-phosphate;    DTT;    dithiothreitol;    NbS2;    dithiobisnitrobenzoate;    NbS;    thionitrobenzoate;    Mal-NEt;    N-ethylmaleimide;   

DOI  :  10.1016/0014-5793(89)80185-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphofructokinase from Jaculus orientalis muscle is an allosteric enzyme regulated by substrates and nucleotide effectors. The conformational modifications upon ligand binding were probed by UV difference spectra and reactivities of thiol groups towards dithiobisnitrobenzoate and N-ethylmaleimide. The binding of Fru-6-P induced significant perturbations in the environment of the aromatic residues and buried the most reactive on the three accessible cysteines per protomer. The same effect on thiol reactivity was observed upon binding of the activator AMP. Various perturbations of both difference spectra and thiol reactivity were detected in the presence of either MG-ATP, an allosteric inhibitor, or MG-ITP which is not an effector.

【 授权许可】

Unknown