4-hydroxythreonine-4-phosphate dehydrogenase

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

The two substrates of this enzyme are 4-phosphonooxy-L-threonine and oxidised nicotinamide adenine dinucleotide (NAD⁺). Its products are (2S)-2-amino-3-oxo-4-phosphonooxybutanoate, reduced NADH, and a proton.

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-phosphonooxy-L-threonine:NAD⁺ oxidoreductase. Other names in common use include NAD⁺-dependent threonine 4-phosphate dehydrogenase, L-threonine 4-phosphate dehydrogenase, 4-(phosphohydroxy)-L-threonine dehydrogenase, PdxA, and 4-(phosphonooxy)-L-threonine:NAD⁺ oxidoreductase. This enzyme participates in vitamin B₆ metabolism.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .

References