Erythrose-4-phosphate dehydrogenase

Erythrose-4-phosphate dehydrogenase
Identifiers
EC no.1.2.1.72
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

In enzymology, erythrose-4-phosphate dehydrogenase (EC 1.2.1.72) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
H2O
H+
H2O
H+
 
4-phospho-D-erythronic acid
 

The three substrates of this enzyme are D-erythrose 4-phosphate, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are 4-phospho-D-erythronic acid, reduced NADH, and a proton.

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).