Glycerol-3-Phosphate Dehydrogenase
From Proteopedia
(Difference between revisions)
| Line 17: | Line 17: | ||
===Function=== | ===Function=== | ||
| - | GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the . The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs. | + | GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs. |
Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway. | Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway. | ||
Revision as of 04:59, 1 April 2010
Template:STRUCTURE 2r4e Glycerol 3-Phosphate Dehydrogenase
Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in reaction of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide (FAD)-Domain and a ubiquinone analogue, MD. [1]
Proteopedia Page Contributors and Editors (what is this?)
Indu Toora, Michal Harel, Alexander Berchansky, David Canner, Andrea Gorrell, Andrew Rebeyka, Jaime Prilusky
