sn-glycerol-1-phosphate dehydrogenase

In enzymology, a sn-glycerol-1-phosphate dehydrogenase (EC 1.1.1.261) is an enzyme that catalyzes the chemical reaction

sn-glycerol 1-phosphate + NAD(P)⁺ ${\displaystyle \rightleftharpoons }$ glycerone phosphate + NAD(P)H + H⁺

The 3 substrates of this enzyme are sn-glycerol 1-phosphate, NAD⁺, and NADP⁺, whereas its 4 products are glycerone phosphate, NADH, NADPH, and H⁺.

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 sn-glycerol-1-phosphate:NAD(P)⁺ 2-oxidoreductase. This enzyme is also called glycerol-1-phosphate dehydrogenase [NAD(P)⁺].

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).

References

• Koga Y, Kyuragi T, Nishihara M, Sone N (1998). "Did archaeal and bacterial cells arise independently from noncellular precursors? A hypothesis stating that the advent of membrane phospholipid with enantiomeric glycerophosphate backbones caused the separation of the two lines of descent". J. Mol. Evol. 46 (1): 54–63. doi:10.1007/PL00006283. PMID 9419225.

This page was last edited on 8 April 2024, at 22:14