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 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 catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

StructureStructure

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 CAP-Domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane. The CAP-domain is responsible in gene transcription and helical turns.

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 FAD-domain plays a major role in metabolism and energy synthesis.

FunctionFunction

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the glycerol metabolism pathway. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions.

ReferencesReferences

Glycerol 3-Phosphate Dehydrogenase

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