Erythrose-4-phosphate dehydrogenase

Erythrose-4-phosphate dehydrogenase
Identifiers
EC number	1.2.1.72
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
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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-phosphoerythronate + 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 (see DXP-dependent biosynthesis of pyridoxal phosphate).

References

• 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. PMC 176952. 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 (24): 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 (16): 4294–9. PMC 107430. PMID 9696782.