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PROSITE documentation PDOC00069

Glyceraldehyde 3-phosphate dehydrogenase active site





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

GAPDH, PS00071; Glyceraldehyde 3-phosphate dehydrogenase active site  (PATTERN)


References

1AuthorsHarris J.I. Waters M.
Source(In) The Enzymes (3rd edition) 13:1-50(1976).

2AuthorsFabry S. Lang J. Niermann T. Vingron M. Hensel R.
TitleNucleotide 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.
SourceEur. J. Biochem. 179:405-413(1989).
PubMed ID2492940

3AuthorsZhao G. Pease A.J. Bharani N. Winkler M.E.
TitleBiochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis.
SourceJ. Bacteriol. 177:2804-2812(1995).
PubMed ID7751290



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