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 [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. In E. coli, many newly discovered structures of GlpD seem to play a role in the transfer of electrons into the respiratory pathway by catalytic dehyrogenation of GlpD. a The GlpD enzyme is a dimer consisting of two subunits which contain the flavin adenine dinucleotide (FAD) active site. <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 [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 flavin adenine dinucleotide (FAD) active site, Cap-Domain and . <ref>PubMed:18296637</ref1>


===Structure===
===Structure===

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Andrea Gorrell, Indu Toora, Andrew Rebeyka, David Canner, Michal Harel, Jaime Prilusky, Alexander Berchansky