000 03309nam a22004575i 4500
001 978-94-007-4716-6
003 DE-He213
005 20140220082934.0
007 cr nn 008mamaa
008 120731s2013 ne | s |||| 0|eng d
020 _a9789400747166
_9978-94-007-4716-6
024 7 _a10.1007/978-94-007-4716-6
_2doi
050 4 _aR-RZ
072 7 _aMBGR
_2bicssc
072 7 _aMED000000
_2bisacsh
082 0 4 _a610
_223
100 1 _aSeidler, Norbert W.
_eauthor.
245 1 0 _aGAPDH: Biological Properties and Diversity
_h[electronic resource] /
_cby Norbert W. Seidler.
264 1 _aDordrecht :
_bSpringer Netherlands :
_bImprint: Springer,
_c2013.
300 _aXIV, 295 p. 96 illus., 8 illus. in color.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
347 _atext file
_bPDF
_2rda
490 1 _aAdvances in Experimental Medicine and Biology,
_x0065-2598 ;
_v985
520 _aGAPDH (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 _aMedicine.
650 0 _aChemistry.
650 0 _aBiochemistry.
650 1 4 _aBiomedicine.
650 2 4 _aBiomedicine general.
650 2 4 _aBiochemistry, general.
650 2 4 _aChemistry/Food Science, general.
710 2 _aSpringerLink (Online service)
773 0 _tSpringer eBooks
776 0 8 _iPrinted edition:
_z9789400747159
830 0 _aAdvances in Experimental Medicine and Biology,
_x0065-2598 ;
_v985
856 4 0 _uhttp://dx.doi.org/10.1007/978-94-007-4716-6
912 _aZDB-2-SBL
999 _c99456
_d99456