Glycerol-3-Phosphate Dehydrogenase

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	===Structure===		===Structure===
-	GlpD consists of two chains; α and β.	+	GlpD is a dimer that consists of two chains; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).
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	===Function===		===Function===

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Revision as of 23:45, 31 March 2010

Glycerol 3-Phosphate Dehydrogenase

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Contents 1 Introduction 1.1 Structure 1.2 Function 1.2.1 Metabolism 1.3 Diseases

Introduction

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD)active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components.

Structure

GlpD is a dimer that consists of two chains; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

Function

GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. 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 electrons to pass to nitrate or oxygen.

Metabolism

Diseases

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