Erythrose-4-phosphate dehydrogenase

Erythrose-4-phosphate dehydrogenase
Identifiers
EC no.	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
Search PMC articles PubMed articles NCBI proteins

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 ${\displaystyle \rightleftharpoons }$ 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^+. [explainpolicedepartment]

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.