In enzymology, L-threonine 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-threonine and oxidised nicotinamide adenine dinucleotide (NAD<sup>+</sup>). Its products are (S)-2-amino-3-ketobutyric acid, 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<sup>+</sup> or NADP<sup>+</sup> as acceptor. The systematic name of this enzyme class is L-threonine:NAD<sup>+</sup> oxidoreductase. Other names in common use include L-threonine dehydrogenase, threonine 3-dehydrogenase, and threonine dehydrogenase. This enzyme participates in glycine, serine and threonine metabolism.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .