|PROSITE documentation PDOC00069 [for PROSITE entry PS00071]|
Glyceraldehyde 3-phosphate dehydrogenase (EC 188.8.131.52) (GAPDH)  is a tetrameric NAD-binding enzyme common to both the glycolytic and gluconeogenic pathways. A cysteine in the middle of the molecule is involved in forming a covalent phosphoglycerol thioester intermediate. The sequence around this cysteine is totally conserved in eubacterial and eukaryotic GAPDHs and is also present, albeit in a variant form, in the otherwise highly divergent archaebacterial GAPDH .
Escherichia coli D-erythrose 4-phosphate dehydrogenase (E4PDH) (gene epd or gapB) is an enzyme highly related to GAPDH .Last update:
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Harris J.I. Waters M.|
|Source||(In) The Enzymes (3rd edition) 13:1-50(1976).|
|2||Authors||Fabry S. Lang J. Niermann T. Vingron M. Hensel R.|
|Title||Nucleotide sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from the mesophilic methanogenic archaebacteria Methanobacterium bryantii and Methanobacterium formicicum. Comparison with the respective gene structure of the closely related extreme thermophile Methanothermus fervidus.|
|Source||Eur. J. Biochem. 179:405-413(1989).|
|3||Authors||Zhao G. Pease A.J. Bharani N. Winkler M.E.|
|Title||Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis.|
|Source||J. Bacteriol. 177:2804-2812(1995).|