PROSITE documentation PDOC00069Glyceraldehyde 3-phosphate dehydrogenase active site
Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) (GAPDH) [1] 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 [2].
Escherichia coli D-erythrose 4-phosphate dehydrogenase (E4PDH) (gene epd or gapB) is an enzyme highly related to GAPDH [3].
Last update:December 2004 / Pattern and text revised.
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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). | |
PubMed ID | 2492940 |
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). | |
PubMed ID | 7751290 |
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