Glycerol-3-Phosphate Dehydrogenase
From Proteopedia
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===Structure=== | ===Structure=== | ||
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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). | ||
| - | <scene name='Sandbox_189/Cap_domain/1'> | + | <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-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. | ||
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===Function=== | ===Function=== | ||
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GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. | GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. | ||
| - | GlpD in E. Coli catalyzes | + | 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. |
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| + | 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. | ||
====Metabolism==== | ====Metabolism==== | ||
Revision as of 03:38, 1 April 2010
Template:STRUCTURE 2r4e Glycerol 3-Phosphate Dehydrogenase
Introduction
Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components. [1]
Proteopedia Page Contributors and Editors (what is this?)
Indu Toora, Michal Harel, Alexander Berchansky, David Canner, Andrea Gorrell, Andrew Rebeyka, Jaime Prilusky
