{PDOC00069}
{PS00071; GAPDH}
{BEGIN}
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* Glyceraldehyde 3-phosphate dehydrogenase active site *
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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].

-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.
-Last update: December 2004 / Pattern and text revised.

[ 1] Harris J.I., Waters M.
     (In) The Enzymes (3rd edition) 13:1-50(1976).
[ 2] Fabry S., Lang J., Niermann T., Vingron M., Hensel R.
     "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."
     Eur. J. Biochem. 179:405-413(1989).
     PubMed=2492940
[ 3] Zhao G., Pease A.J., Bharani N., Winkler M.E.
     "Biochemical characterization of gapB-encoded erythrose 4-phosphate
     dehydrogenase of Escherichia coli K-12 and its possible role in
     pyridoxal 5'-phosphate biosynthesis."
     J. Bacteriol. 177:2804-2812(1995).
     PubMed=7751290

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