Erythrose-4-phosphate dehydrogenase

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In enzymology, an erythrose-4-phosphate dehydrogenase (EC 1.2.1.72) is an enzyme that catalyzes the chemical reaction

D-erythrose 4-phosphate + NAD⁺ + H₂O $\rightleftharpoons$ 4-phosphoerythronat + NADH + 2 H⁺

The 3 substrates of this enzyme are D-erythrose 4-phosphate, NAD⁺, and H₂O, whereas its 3 products are 4-phosphoerythronat, NADH, and H⁺.

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.

[edit] References

IUBMB entry for 1.2.1.72
BRENDA references for 1.2.1.72 (Recommended.)
PubMed references for 1.2.1.72
PubMed Central references for 1.2.1.72
Google Scholar references for 1.2.1.72
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: 2804–12. PMID 7751290.
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: 15106–12. doi:10.1074/jbc.272.24.15106. PMID 9182530.
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: 4294–9. PMID 9696782.