Glycerol-3-Phosphate Dehydrogenase

From Proteopedia

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 in reaction of 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.

Structure

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).

The C-terminal consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

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 base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. ^[1]