Conformational dynamics and enzyme activity.
Conformational flexibility and structural fluctuations play an important role in enzyme activity. A great variety of internal motions ranging over different time scales and of different amplitudes are involved in the catalytic cycle. These different types of motions and their functional consequences are considered in the light of experimental data and theoretical analyses. The conformational changes upon substrate binding, and particularly the hinge-bending motion which occurs in enzymes made of two domains, are analyzed from several well documented examples. The conformational events accompanying the different steps of the catalytic cycle are discussed. The last section concerns the motions involved in the allosteric transition which regulates the enzyme activity.
Yon
J M
JM
Laboratoire de Modélisation et d'Ingénérie des Protéines, Unité Associée du CNRS, Université de Paris-Sud, Orsay, France.
Perahia
D
D
Ghélis
C
C
D000494:Allosteric Regulation; D002384:Catalysis; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D004798:Enzymes