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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.

Technical section:

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

GAPDH, PS00071; Glyceraldehyde 3-phosphate dehydrogenase active site  (PATTERN)
Consensus pattern: [ASV]-S-C-[NT]-T-{S}-x-[LIM]
C is the active site residue
Sequences known to belong to this class detected by the pattern: ALL, except for Bacillus megaterium GAPDH which has Pro instead of Ser in position 2 of the pattern
Other sequence(s) detected in Swiss-Prot: 5
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• Scan Swiss-Prot/TrEMBL entries against PS00071
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Matching PDB structures: 1A7K 1B7G 1CER 1CF2 ... [ALL]

References:

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