GAPDH: Biological Properties and Diversity

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...

Full description

Bibliographic Details
Main Author: Seidler, Norbert W. (Author)
Corporate Author: SpringerLink (Online service)
Format: Electronic
Language:English
Published: Dordrecht : Springer Netherlands : Imprint: Springer, 2013.
Series:Advances in Experimental Medicine and Biology, 985
Subjects:
Online Access:https://ezaccess.library.uitm.edu.my/login?url=http://dx.doi.org/10.1007/978-94-007-4716-6
LEADER 03328nam a22004575i 4500
001 16992
003 DE-He213
005 20130727031520.0
007 cr nn 008mamaa
008 120731s2013 ne | s |||| 0|eng d
020 # # |a 9789400747166  |9 978-94-007-4716-6 
024 7 # |a 10.1007/978-94-007-4716-6  |2 doi 
050 # 4 |a R-RZ 
072 # 7 |a MBGR  |2 bicssc 
072 # 7 |a MED000000  |2 bisacsh 
082 0 4 |a 610  |2 23 
100 1 # |a Seidler, Norbert W.  |e author. 
245 1 0 |a GAPDH: Biological Properties and Diversity  |c by Norbert W. Seidler.  |h [electronic resource] / 
264 # 1 |a Dordrecht :  |b Springer Netherlands :  |b Imprint: Springer,  |c 2013. 
300 # # |a XIV, 295 p. 96 illus., 8 illus. in color.  |b online resource. 
336 # # |a text  |b txt  |2 rdacontent 
337 # # |a computer  |b c  |2 rdamedia 
338 # # |a online resource  |b cr  |2 rdacarrier 
347 # # |a text file  |b PDF  |2 rda 
490 1 # |a Advances in Experimental Medicine and Biology,  |v 985  |x 0065-2598 ; 
520 # # |a 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. 
650 # 0 |a Medicine. 
650 # 0 |a Chemistry. 
650 # 0 |a Biochemistry. 
650 1 4 |a Biomedicine. 
650 2 4 |a Biomedicine general. 
650 2 4 |a Biochemistry, general. 
650 2 4 |a Chemistry/Food Science, general. 
710 2 # |a SpringerLink (Online service) 
773 0 # |t Springer eBooks 
776 0 8 |i Printed edition:  |z 9789400747159 
830 # 0 |a Advances in Experimental Medicine and Biology,  |v 985  |x 0065-2598 ; 
856 4 0 |u https://ezaccess.library.uitm.edu.my/login?url=http://dx.doi.org/10.1007/978-94-007-4716-6 
912 # # |a ZDB-2-SBL 
950 # # |a Biomedical and Life Sciences (Springer-11642)