• Source: Erythrose-4-phosphate dehydrogenase

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



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{\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.

Kata Kunci Pencarian:

• Erythrose 4-phosphate
• Erythrose-4-phosphate dehydrogenase
• Pentose phosphate pathway
• EPD
• Calvin cycle
• Fructose-bisphosphate aldolase
• Pyridoxal phosphate
• Tetrose
• Shikimate pathway
• Quinic acid