Glycerol-3-Phosphate Dehydrogenase: Difference between revisions
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'''Glycerol 3-Phosphate Dehydrogenase''' | '''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 [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg 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 flavin adenine dinucleotide (FAD) | 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 [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg 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. <ref>PubMed:18296637</ref1> | ||
===Structure=== | ===Structure=== | ||
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain | GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap-Binding Domain, FAD-Binding 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> | ||