Glycerol-3-Phosphate Dehydrogenase: Difference between revisions

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Andrea Gorrell, Indu Toora, Andrew Rebeyka, David Canner, Michal Harel, Jaime Prilusky, Alexander Berchansky

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 '''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 Cap-Domain,the flavin adenine dinucleotide (FAD)-Domain and a ubiquinone analogue, MD. <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 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===
-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).
+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)binding sites.
 <scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>
-The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.
+The C-terminal Cap-Domain consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.
 <scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>
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 ===Function===
-GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
+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 in E. Coli catalyzes and oxidizes the reaction of glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic 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.
+Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism.  The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.
 ====Metabolism====
 ===Diseases===