Glycerol-3-Phosphate Dehydrogenase
From Proteopedia
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===Structure=== | ===Structure=== | ||
| - | GlpD is a dimer that consists of two | + | 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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| + | <scene name='Sandbox_189/Cap_domain/1'>TextToBeDisplayed</scene> | ||
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| + | 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. | ||
<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 (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain of GlpD is embedded into the phospholipid membrane bilayer. | + | The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The 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 base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2> |
===Function=== | ===Function=== | ||
Revision as of 01:27, 1 April 2010
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
