Erythrose-4-phosphate dehydrogenase

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Erythrose-4-phosphate dehydrogenase
Identifiers
EC no. 1.2.1.72
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In enzymology, erythrose-4-phosphate dehydrogenase (EC 1.2.1.72) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
H2O
H+
Erythrose-4-phosphate dehydrogenase
H2O
H+
 
+ NADH
 

The three substrates of this enzyme are D-erythrose 4-phosphate, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are 4-phospho-D-erythronic acid, reduced NADH, and a proton. [1] [2] [3] [4]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-erythrose 4-phosphate:NAD+ oxidoreductase. Other names in common use include erythrose 4-phosphate dehydrogenase, E4PDH, GapB, Epd dehydrogenase, and E4P dehydrogenase. This enzyme participates in vitamin B6 metabolism (see DXP-dependent biosynthesis of pyridoxal phosphate).

References

  1. Enzyme 1.2.1.72 at KEGG Pathway Database.
  2. Zhao G, Pease AJ, Bharani N, Winkler ME (1995). "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 (10): 2804–12. doi:10.1128/jb.177.10.2804-2812.1995. PMC   176952 . PMID   7751290.
  3. Boschi-Muller S, Azza S, Pollastro D, Corbier C, Branlant G (1997). "Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase". J. Biol. Chem. 272 (24): 15106–12. doi: 10.1074/jbc.272.24.15106 . PMID   9182530.
  4. Yang Y, Zhao G, Man TK, Winkler ME (1998). "Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12". J. Bacteriol. 180 (16): 4294–9. doi:10.1128/JB.180.16.4294-4299.1998. PMC   107430 . PMID   9696782.