Renaturation of the allosteric phosphofructokinase from Escherichia coli.
作者： A Martel , J R Garel
DOI: 10.1016/S0021-9258(17)42933-4
关键词: Enzyme 、 Biochemistry 、 Chemistry 、 Guanidine 、 Allosteric regulation 、 Phosphofructokinase 、 Monomer 、 Escherichia coli 、 Kinetics 、 Reaction rate constant
摘要: Abstract The allosteric phosphofructokinase from Escherichia coli has been renatured after complete unfolding in concentrated guanidine hydrochloride. enzyme regains both its catalytic and regulatory abilities quantitatively. kinetics of reactivation are biphasic consistent with a two-step mechanism which monomolecular reaction precedes bimolecular one. presence ATP during increases the rate at is renatured; second order constant step about 10(4) M-1 S-1 absence to 2 X 10(5) 1 mM ATP. other ligands have no effect on reactivation. It tentatively proposed that folded monomer intermediate species already possesses functional ATP-binding site rate-limiting association formation dimeric species. This interpretation compatible known three-dimensional structure another bacterial phosphofructokinase, Bacillus stearothermophilus.
sci-hub.st 参考文章(14)
D. Kotlarz, H. Buc, Two Escherichia coli fructose-6-phosphate kinases Biochimica et Biophysica Acta (BBA) - Enzymology. ,vol. 484, pp. 35- 48 ,(1977) , 10.1016/0005-2744(77)90111-5
D. Blangy, H. Buc, J. Monod, Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli. Journal of Molecular Biology. ,vol. 31, pp. 13- 35 ,(1968) , 10.1016/0022-2836(68)90051-X
Daniel Blangy, Phosphofructokinase from E. Coli
: Evidence for a tetrameric structure of the enzyme FEBS Letters. ,vol. 2, pp. 109- 111 ,(1968) , 10.1016/0014-5793(68)80115-2
Jacque Monod, Jeffries Wyman, Jean-Pierre Changeux, On the Nature of Allosteric Transitions: A Plausible Model Journal of Molecular Biology. ,vol. 12, pp. 88- 118 ,(1965) , 10.1016/S0022-2836(65)80285-6
R. Jaenicke, Folding and association of proteins Biophysics of Structure and Mechanism. ,vol. 8, pp. 231- 256 ,(1982) , 10.1007/BF00537204
J. R. Garel, A. Dautry-Varsat, Sequential folding of a bifunctional allosteric protein. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 77, pp. 3379- 3383 ,(1980) , 10.1073/PNAS.77.6.3379
Gisele Le Bras, Jean Renaud Garel, A proteolyzed derivative of Escherichia coli phosphofructokinase is no longer sensitive to allosteric effectors and still shows cooperativity in substrate binding. Biochemistry. ,vol. 21, pp. 6656- 6660 ,(1982) , 10.1021/BI00269A007
D. Blangy, Propriétés allostériques de la phosphofructokinase d'E. coli. Étude de la fixation des ligands par dialyse à l'équilibre Biochimie. ,vol. 53, pp. 135- 144 ,(1971) , 10.1016/S0300-9084(71)80044-5
Edith KOLB, Peter J. HUDSON, J. Ieuan HARRIS, Phosphofructokinase: complete amino-acid sequence of the enzyme from Bacillus stearothermophilus. FEBS Journal. ,vol. 108, pp. 587- 597 ,(1980) , 10.1111/J.1432-1033.1980.TB04754.X
D. Kotlarz, H. Garreau, H. Buc, Regulation of the amount and of the activity of phosphofructokinases and pyruvate kinases in Escherichia coli. Biochimica et Biophysica Acta. ,vol. 381, pp. 257- 268 ,(1975) , 10.1016/0304-4165(75)90232-9