Glycerol-3-phosphate dehydrogenase (NAD⁺)

In enzymology, a glycerol-3-phosphate dehydrogenase (NAD⁺) (EC 1.1.1.8) is an enzyme that catalyzes the chemical reaction

sn-glycerol 3-phosphate + NAD⁺ ${\displaystyle \rightleftharpoons }$ glycerone phosphate + NADH + H⁺

The two substrates of this enzyme are sn-glycerol 3-phosphate and NAD⁺, whereas its 3 products are glycerone phosphate, NADH, 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-3-phosphate:NAD⁺ 2-oxidoreductase. Other names in common use include alpha-glycerol phosphate dehydrogenase (NAD⁺), alpha-glycerophosphate dehydrogenase (NAD⁺), glycerol 1-phosphate dehydrogenase, glycerol phosphate dehydrogenase (NAD⁺), glycerophosphate dehydrogenase (NAD⁺), hydroglycerophosphate dehydrogenase, L-alpha-glycerol phosphate dehydrogenase, L-alpha-glycerophosphate dehydrogenase, L-glycerol phosphate dehydrogenase, L-glycerophosphate dehydrogenase, NAD⁺-alpha-glycerophosphate dehydrogenase, NAD⁺-dependent glycerol phosphate dehydrogenase, NAD⁺-dependent glycerol-3-phosphate dehydrogenase, NAD⁺-L-glycerol-3-phosphate dehydrogenase, NAD⁺-linked glycerol 3-phosphate dehydrogenase, NADH-dihydroxyacetone phosphate reductase, and glycerol-3-phosphate dehydrogenase (NAD⁺). This enzyme participates in glycerophospholipid metabolism.

Structural studies[]

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1EVY, 1EVZ, 1JDJ, 1M66, 1M67, 1N1E, 1N1G, 1WPQ, 1X0V, 1X0X, 1YJ8, and 1Z82.

References[]

• Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 85-96.
• Brosemer RW, Kuhn RW (1969). "Comparative structural properties of honeybee and rabbit alpha-glycerophosphate dehydrogenases". Biochemistry. 8 (5): 2095–105. doi:10.1021/bi00833a047. PMID 4307630.
• O'Brien SJ, MacIntyre RJ (1972). "The -glycerophosphate cycle in Drosophila melanogaster. I Biochemical and developmental aspects". Biochem. Genet. 7 (2): 141–61. doi:10.1007/BF00486085. PMID 4340553. S2CID 22009695.
• Warkentin DL, Fondy TP (1973). "Isolation and characterization of cytoplasmic L-glycerol-3-phosphate dehydrogenase from rabbit-renal-adipose tissue and its comparison with the skeletal-muscle enzyme". Eur. J. Biochem. 36 (1): 97–109. doi:10.1111/j.1432-1033.1973.tb02889.x. PMID 4200180.
• Albertyn J, van Tonder A, Prior BA (1992). "Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae". FEBS Lett. 308 (2): 130–2. doi:10.1016/0014-5793(92)81259-O. PMID 1499720. S2CID 39643279.
• Koekemoer TC, Litthauer D, Oelofsen W (1995). "Isolation and characterization of adipose tissue glycerol-3-phosphate dehydrogenase". Int. J. Biochem. Cell Biol. 27 (6): 625–32. doi:10.1016/1357-2725(95)00012-E. PMID 7671141.