Glycerol-3-Phosphate Dehydrogenase
From Proteopedia
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GlpD is a dimer that consists of two chains; 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 chains; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD). | ||
| - | FAD Active Site | ||
<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene> | <scene name='Sandbox_189/Fad/2'>FAD Active Site</scene> | ||
| - | + | The N-terminal FAD-Binding Domain region consists of residues from 1 to 388. The FAD-Binding Domain of GlpD is embedded into the phospholipid membrane bilayer. | |
===Function=== | ===Function=== | ||
Revision as of 00:21, 1 April 2010
Glycerol 3-Phosphate Dehydrogenase
Contents |
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.
Structure
GlpD is a dimer that consists of two chains; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).
The N-terminal FAD-Binding Domain region consists of residues from 1 to 388. The FAD-Binding Domain of GlpD is embedded into the phospholipid membrane bilayer.
Function
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. 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 electrons to pass to nitrate or oxygen.
Metabolism
Diseases
| Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell. |
Proteopedia Page Contributors and Editors (what is this?)
Indu Toora, Michal Harel, Alexander Berchansky, David Canner, Andrea Gorrell, Andrew Rebeyka, Jaime Prilusky
