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Glycerol-3-phosphate dehydrogenase (NAD(P)+)

From Wikipedia, the free encyclopedia

In enzymology, a glycerol-3-phosphate dehydrogenase [NAD(P)+] (EC 1.1.1.94) is an enzyme that catalyzes the chemical reaction

sn-glycerol 3-phosphate + NAD(P)+ glycerone phosphate + NAD(P)H + H+

The 3 substrates of this enzyme are sn-glycerol 3-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-3-phosphate:NAD(P)+ 2-oxidoreductase. Other names in common use include L-glycerol-3-phosphate:NAD(P)+ oxidoreductase, glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide, (phosphate)), glycerol 3-phosphate dehydrogenase (NADP+), and glycerol-3-phosphate dehydrogenase [NAD(P)+]. This enzyme participates in glycerophospholipid metabolism.

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Transcription

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1TXG.

References

  • Kito M, Pizer LI (1969). "Purification and regulatory properties of the biosynthetic L-glycerol 3-phosphate dehydrogenase from Escherichia coli". J. Biol. Chem. 244 (12): 3316–23. PMID 4389388.
  • Edgar JR, Bell RM (1978). "Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid". J. Biol. Chem. 253 (18): 6348–53. PMID 355254.
  • Edgar JR, Bell RM (1978). "Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. Kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase". J. Biol. Chem. 253 (18): 6354–63. PMID 28326.
  • Edgar JR, Bell RM (1980). "Biosynthesis in Escherichia coli of sn-glycerol-3-phosphate, a precursor of phospholipid. Further kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase". J. Biol. Chem. 255 (8): 3492–7. PMID 6767719.


This page was last edited on 26 August 2023, at 14:20
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