4-phosphoerythronate dehydrogenase

In enzymology, 4-phosphoerythronate dehydogenase (EC 1.1.1.290) is an enzyme that catalyzes the chemical reaction

4-phospho-D-erythronic acid

+ NAD⁺

 

 

 

H⁺

 

H⁺

 

(R)-3-hydroxy-2-oxo-4-phosphonooxybutanoic acid

+ NADH

 

4-phosphoerythronate dehydrogenase
Identifiers
EC no.	1.1.1.290
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

The two substrates of this enzyme are 4-phospho-D-erythronic acid and oxidised nicotinamide adenine dinucleotide (NAD⁺). Its products are (R)-3-hydroxy-2-oxo-4-phosphonooxybutanoic acid, reduced NADH, and a proton.^{[1][2][3][4][5]}

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD⁺ or NADP⁺ as acceptor. The systematic name of this enzyme class is 4-phospho-D-erythronate:NAD⁺ 2-oxidoreductase. Other names in common use include PdxB, PdxB 4PE dehydrogenase, and 4-O-phosphoerythronate dehydrogenase. This enzyme participates in vitamin B₆ metabolism.^[6]

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2O4C.