Allosteric Regulatory Enzymes

2008
ISBN: 978-0-387-72888-9
Verlag: Springer US

Buch, Englisch, 250 Seiten, Format (B × H): 160 mm x 241 mm, Gewicht: 1220 g

All enzymes are remarkable since they have the ability to increase the rate of a chemical reaction, often by more than a billion-fold. Allosteric enzymes are even more amazing because the have the additional ability to change their rate in response to cellular activators or inhibitors. This enables them to control the pathway in which they are the regulatory enzyme. Since the effector molecules represent the current status of the cell for a given metabolic pathway, this results in very responsive and balanced metabolic states, and makes it possible for cells and organisms to be appropriately dynamic, and responsive, in a changing environment. This book provides a logical introduction to the limits for enzyme function as dictated by the factors that are limits for life. This book presents a complete description of all the mechanisms used for changing enzyme acticity. Eight enzymes are used as model systems after extensive study of their mechanisms. Wherever possible, the human form of the enzyme is used to illustrate the regulatory features.

Zielgruppe

Research

Autoren/Hrsg.

Traut, Thomas W.

Fachgebiete

• Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)
• Naturwissenschaften Biowissenschaften Enzymologie

Inhaltsverzeichnis

Overview Of Enzymes.- To Enzymes.- The Limits For Life Define The Limits For Enzymes.- Enzyme Kinetics.- Properties And Evolution Of Allosteric Enzymes.- Kinetics Of Allosteric Enzymes.- K-Type Enzymes.- Hemoglobin.- Glycogen Phosphorylase.- Phosphofructokinase.- Ribonucleotide Reductase.- Hexokinase.- V-Type Enzymes.- To V-Type Enzymes.- G Proteins.- Protein Kinases.

Über Autor(innen)

Thomas Traut has a PhD in molecular biology and has studied enzymes since 1974.  As a professor at the University of North Carolina at Chapel Hill, he has focused on enzyme regulation and taught advanced enzymology to graduate students.  Important findings from his research helped to define the mechanism of allosteric control for dissociating enzymes.