Glycerol-3-Phosphate Dehydrogenase
From Proteopedia
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===Structure=== | ===Structure=== | ||
| - | GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD) | + | GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of of seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD). |
<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene> | <scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene> | ||
Revision as of 05:21, 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]
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