Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy

D-erythrose 4-phosphate:NAD+ oxidoreductase

D-erythrose 4-phosphate + NAD+ + H2O = 4-phosphoerythronat + NADH + 2 H+ [RN:R01825]

R01825
Reaction

D-erythrose 4-phosphate [CPD:C00279];
NAD+ [CPD:C00003];
H2O [CPD:C00001]

This enzyme was originally thought to be a glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), but this has since been disproved, as glyceraldehyde 3-phosphate is not a substrate [1,2]. Forms part of the pyridoxal-5'-phosphate coenzyme biosynthesis pathway in Escherichia coli, along with EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (pyridoxamine-phosphate oxidase).

EC 1.2.1.72 created 2006

1  [PMID:7751290]

Zhao G, Pease AJ, Bharani N, Winkler ME

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 (1995)
DOI:10.1128/JB.177.10.2804-2812.1995

[eco:b2927]

2  [PMID:9182530]

Boschi-Muller S, Azza S, Pollastro D, Corbier C, Branlant G.

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 (1997)
DOI:10.1074/jbc.272.24.15106

[eco:b2927]

3  [PMID:9696782]

Yang Y, Zhao G, Man TK, Winkler ME.

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 (1998)
DOI:10.1128/JB.180.16.4294-4299.1998

[eco:b2927]