The effect of phosphate on the unfolding‐refolding of phosphoglycerate kinase induced by guanidine hydrochloride

FEBS Letters

Betton, J.M.¹  Chardot, T.¹  Yon, J.M.¹  Mitraki, A.¹  Amigues, Y.¹  Desmadril, M.¹ 

[1]Laboratoire d'Enzymologie Physico-Chimique et Moléculaire, GR-CNRS associté à l'Université de Paris-Sud, 91 405 Orsay, France

关键词: Protein folding;    Phosphoglycerate kinase;    Phosphate effect;    Equilibrium;    Kinetics;    Structural domain;   

DOI  :  10.1016/0014-5793(88)80586-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphate ions were found to stabilize the native structure of phosphoglycerate kinase without modifying the folding pathway. The transition curves obtained from different signals: enzyme activity, ellipticity at 220 nm and fluorescence intensity at 336 nm (excitation at 292 nm) are shifted to smaller guanidine hydrochloride c _m values in the absence of phosphate. The kinetic characteristics are qualitatively similar, unfolding rate constants being slightly smaller in the presence of phosphate. The mechanism by which the native structure of phosphoglycerate kinase is stabilized by phosphate probably occurs upon specific phosphate binding to the nucleotide β- or γ-phosphate binding site of nucleotides.

【 授权许可】

Unknown