In enzymology, sn-glycerol-1-phosphate dehydrogenase () is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are (S)-glyceryl 1-phosphate and oxidised nicotinamide adenine dinucleotide (NAD<sup>+</sup>). Its products are glycerone phosphate, reduced NADH, and a proton. The enzyme can also use the alternative cofactor, nicotinamide adenine dinucleotide phosphate.
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 sn-glycerol-1-phosphate:NAD(P)<sup>+</sup> 2-oxidoreductase. This enzyme is also called glycerol-1-phosphate dehydrogenase [NAD(P)<sup>+</sup>].
G-1-P dehydrogenase is responsible for the formation of sn-glycerol 1-phosphate, the backbone of the membrane phospholipids of Archaea. The gene encoding glycerol-1-phosphate dehydrogenase has been detected in all the archaeal species and has not been found in any bacterial or eukaryal species. sn-glycerol 1-phosphate produced by this enzyme is the most fundamental difference by which Archaea and bacteria are discriminated.
The enzyme sn-glycerol-1-phosphate dehydrogenase, usually having 394 amino acids, was also identified in bacteria. More than 5700 sequences have been published in GenBank (September 2023) in a different bacteria, including such well-known ones as Bacillus subtilis (GenBank: AOR99168.1).