Limit search to available items
Book Cover
Author Seidler, Norbert W

Title GAPDH : biological properties and diversity / Norbert W. Seidler
Published Dordrecht ; New York : Springer, ©2013


Description 1 online resource
Series Advances in experimental medicine and biology, 0065-2598 ; 985
Advances in experimental medicine and biology ; 985.
Contents Basic Biology of GAPDH -- GAPDH and Intermediary Metabolism -- Compartmentation of GAPDH -- Functional Diversity -- GAPDH, as a Virulence Factor -- Target for Diverse Chemical Modifications -- Dynamic Oligomeric Properties -- Multiple Binding Partners -- GAPDH in Anesthesia
Summary GAPDH (glyceraldehyde 3-phosphate dehydrogenase) is more than just a glycolytic enzyme. An unprecedented amount of literature demonstrates that GAPDH has an astounding multiplicity of function. This diversity is not simply due to cell compartmentation (i.e. redistributing glycolytic energy to where it is needed), although this feature is undoubtedly important and discussed in the book. GAPDH integrates glycolysis with other cellular processes. This concept of integration cannot be understated. But, there is more. GAPDH actively participates in numerous non-glycolytic cellular events that fall into very broad categories including the cell infrastructure and the transmission of genetic information. Some of GAPDH's biological properties are completely non-intuitive given the current undergraduate textbook understanding of this glycolytic enzyme. For example, GAPDH binds to select phospholipids and catalyzes organelle biogenesis. It has fusogenic properties, enabling it to be actively involved in nuclear envelop reassembly, autophagy and membrane trafficking. Human macrophages exhibit surface-localized GAPDH with receptor function. As scientists, we are trained to consider GAPDH as a soluble cytosolic dehydrogenase enzyme. The literature observations - as described in this book - tell us something quite different. Besides oxidoreductase activity, GAPDH exhibits peroxidase, uracil DNA glycosylase, nitrosylase, mono-ADP-ribosylase, esterase and phosphotransferase activity. GAPDH binds membrane transport proteins, G-proteins, poly-nucleotides, adenines, specific lipids, select carbohydrates, cytoskeletal proteins, nuclear import and export proteins, diverse ATPases, molecular chaperones and other molecules
Analysis Medicine
Chemistry/Food Science, general
Bibliography Includes bibliographical references and index
In Springer eBooks
Subject Aldehyde dehydrogenase.
Enzymes -- Synthesis.
Cell physiology.
Cell Physiological Phenomena
Cells -- enzymology
Gene Expression Regulation, Enzymologic
Glyceraldehyde-3-Phosphate Dehydrogenases
MEDICAL -- Biochemistry.
Cell physiology
Aldehyde dehydrogenase
Enzymes -- Synthesis
Form Electronic book
LC no. 2012944710
ISBN 9789400747166