Glycerol-3-Phosphate Dehydrogenase: Difference between revisions
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'''Glycerol 3-Phosphate Dehydrogenase''' | '''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 [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg 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<ref>PubMed:18296637</ref1> | 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 [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg 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<ref>PubMed:18296637</ref1> | ||
===Structure=== | ===Structure=== | ||
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<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene> | <scene name='Sandbox_189/Fad/2'>FAD Active Site</scene> | ||
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 membran<ref>PubMed:18296637</ref2> | 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 membran<ref>PubMed:18296637</ref2> | ||
===Function=== | ===Function=== | ||