Glycerol-3-Phosphate Dehydrogenase
From Proteopedia
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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, where it uses the carbons from Glycerol 3-Phosphate for phospholipids biosynthesis, respiration and further metabolism. In E. coli, many newly discovered structures of GlpD seem to play a role in the transfer of electrons into the respiratory pathway by catalytic dehyrogenation of GlpD. a The GlpD enzyme is a dimer consisting of two subunits which contain the flavin adenine dinucleotide (FAD) active site. <ref>PubMed:18296637</ref1> | 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, where it uses the carbons from Glycerol 3-Phosphate for phospholipids biosynthesis, respiration and further metabolism. In E. coli, many newly discovered structures of GlpD seem to play a role in the transfer of electrons into the respiratory pathway by catalytic dehyrogenation of GlpD. a The GlpD enzyme is a dimer consisting of two subunits which contain the flavin adenine dinucleotide (FAD) active site. <ref>PubMed:18296637</ref1> | ||
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===Structure=== | ===Structure=== | ||
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding 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 a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD). | ||
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===Diseases=== | ===Diseases=== | ||
===References=== | ===References=== | ||
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Revision as of 04:06, 1 April 2010
Template:STRUCTURE 2r4e Glycerol 3-Phosphate Dehydrogenase
Introduction
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 reactionof Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions, where it uses the carbons from Glycerol 3-Phosphate for phospholipids biosynthesis, respiration and further metabolism. In E. coli, many newly discovered structures of GlpD seem to play a role in the transfer of electrons into the respiratory pathway by catalytic dehyrogenation of GlpD. a The GlpD enzyme is a dimer consisting of two subunits which contain the flavin adenine dinucleotide (FAD) active site. [1]
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Indu Toora, Michal Harel, Alexander Berchansky, David Canner, Andrea Gorrell, Andrew Rebeyka, Jaime Prilusky
