This book compiles detailed information concerning a dozen of the best known allosteric enzymes, and so allows the comparison of their regulatory mechanisms and the confrontation of these mechanisms with the theoretical models. Stimulating and unexpected ideas emerge from these comparisons and emphasize the importance of developing various methods of investigation such as crystallography, X-ray solution scattering, and the study of fast movements in proteins and site-directed mutagenesis. This book is addressed to students and researchers interested in structure-function relationship in proteins, enzymology and metabolic regulation. It is also a basis for teaching.
Table of Contents
Concepts and Models of Enzyme Cooperativity. Structure and Function of Hemoglobin: The Cooperative Mechanism. Aspartate Transcarbamylase from Escherichia coli. Glycogen Phosphorylase b. Regulation of Bacterial Glutamine Phosphoribosyl-Pyrophosphate Amidotransferase. Mammalian Glyceraldehyde-3-Phosphate Dehydrogenase and Its Use to Elucidate Molecular Mechanisms of Cooperativity. Citrate Synthase. Ribonucleotide Reductase. Allosteric Interactions in Deoxycytidylate Aminohydrolase. Rabbit Muscle Phosphofructokinase. Yeast Phosphofructokinase. Concluding Remarks. Index.