Glycerol-3-Phosphate Dehydrogenase: Difference between revisions
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<StructureSection load='1yj8' size='350' side='right' scene='' caption='Glycerol-3-phosphate dehydrogenase trimer [[1yj8]]'> | |||
'''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 [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate, with NADH as the reductant. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. <ref name="cellfunction">PMID:18296637</ref>The GlpD is a dimer consisting of two subunits which contain the catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD. | |||
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 [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate, with NADH as the reductant. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. <ref name="cellfunction"> | |||
===Structure=== | ===Structure=== | ||
[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]] | [[Image:FINAL.png|left|thumb|Glycerol 3-Phosphate Dehydrogenase]] | ||
{{Clear}} | |||
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains 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). | GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains 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). | ||
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<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene> | <scene name='Sandbox_189/Fad/2'>FAD Active Site</scene> | ||
The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis. | The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis. The active site is found in a cleft between the two domains<ref>PMID:14717590</ref>. | ||
===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 [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions. | 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 (DHAP) 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 (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate) or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions. | ||
===Metabolic Pathways=== | ===Metabolic Pathways=== | ||
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====Phosphoplipid Biosynthesis==== | ====Phosphoplipid Biosynthesis==== | ||
GlpD reduces | GlpD reduces DHAP to glycerol 3-phosphate. Then the glycerol 3-phosphate is catalyzed by acyl transferase to 1-acylglyverol-3-phosphate, and then another acyl transferase catalyzes that to a phosphatidic acid. head groups are added to the phosphatidic acid to synthesize phospholipids. | ||
====Glyceroneogenesis==== | ====Glyceroneogenesis==== | ||
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===Diseases=== | ===Diseases=== | ||
GlpD is involved in diseases such as | GlpD is involved in diseases such as Alzeheimer`s, muscle dystrophy, hyaline membrane diseases and many more. | ||
==3D structures of glycerol-3-phosphate dehydrogenase== | ==3D structures of glycerol-3-phosphate dehydrogenase== | ||
[[Glycerol-3-phosphate dehydrogenase 3D structures]] | |||
</StructureSection> | |||
==References== | |||
<references /> | <references /> | ||
[[Category:Topic Page]] | |||