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).
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SYSTEMATIC NAME
IUBMB Comments
D-erythrose 4-phosphate:NAD+ oxidoreductase
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).
production of E4P can be coupled to the NADH generating E4PD activity which enables measurement of the transketolase reaction involving F6P as donor substrate
the chemical mechanism of erythrose 4-phosphate oxidation by gap-encoded protein proceeds through a two-step mechanism involving covalent intermediates with Cys149, with rates associated to the acylation and deacylation process of 280 per s and 20 per s, respectively. No isotopic solvent effect is observed, suggesting that the rate-limiting step is not hydrolysis
epd expression is very low in Escherichia coli. In presence of glucose, the 3 epd, pgk and fba ORFs are efficiently cotranscribed from promoter epd P0. Translational limitation of the epd expression in Escherichia coli
epd expression is very low in Escherichia coli. In presence of glucose, the 3 epd, pgk and fba ORFs are efficiently cotranscribed from promoter epd P0. Translational limitation of the epd expression in Escherichia coli
mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 5.7fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+
mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 33.3fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+
mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 2.7fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+
turnover number of phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity is decreased by the factor 40. 95.2fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+
mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 5fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+
coupling of a transketolase reaction (using Leishmania mexicana transketolase) that converts D-fructose 6-phosphate to D-erythrose 4-phosphate, which can then be converted to 4-phosphate D-erythronate using E4PD, whereby D-ribose 5-phosphate and D-glyceraldehyde 3-phosphate can both be used as ketol acceptor substrates in the reaction
Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis
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
Bardey, V.; Vallet, C.; Robas, N.; Charpentier, B.; Thouvenot, B.; Mougin, A.; Hajnsdorf, E.; Regnier, P.; Springer, M.; Branlant, C.
Characterization of the molecular mechanisms involved in the differential production of erythrose-4-phosphate dehydrogenase, 3-phosphoglycerate kinase and class II fructose-1,6-bisphosphate aldolase in Escherichia coli