Glycerol-3-Phosphate Dehydrogenase

Template:STRUCTURE 2r4e 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 reactionof 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>

StructureStructure

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).

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 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>

FunctionFunction

GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. 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.

ReferencesReferences

Glycerol 3-Phosphate Dehydrogenase

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