Introduction

Stearyol CoA Desaturase (SCD1) functions as a lipogenic enzyme which is essential for fatty acid metabolism. SCD1 desaturates the sigma bond, within the 18-carbon acyl-CoA ligand, that attaches carbons 9 and 10. The desaturated ligand is used in the synthesis of cholesteryl esters and triglycerides. The exact origin of SCD1 is unknown. Current studies have used mouse SCD to determine the structure and function of the enzyme. The metal ions within the structure of SCD1 were determined by X-Ray Flourescense. The structure of the ligand before the reaction takes place and how it interacts with the enzyme was determined by using zinc as the metal ions which inhibits the enzymes activity. The structure of the ligand post reaction was determined by using [hhttps://en.wikipedia.org/wiki/Iron iron] as the metal ions which allowed the enzyme to be active and complete the reaction. SCD1 is a transmembrane protein title with 4 helices within the membrane, and 8 helices in cytoplasm. This protein acquires electrons via an electron transport chain which includes cytochrome B5 reductase and cytochrome B5. The electrons are transferred via a ternary complex and accepted by SCD1 by the iron metal ions. SCD1 has 8 helices that are hydrophobic, 4 helices that are hydrophilic, and 3 helices that are amphipathic.

Biological Relevance

Position within membrane

General Structure

Hydrophobicity of helices, type of assembly in biological system (Dimer/monomer/homo/hetero?), ST9 Ligand, MPG Ligand, how substrate enters/leaves

Necessary Structural Elements

Overall Structure

The SCD catalytic area is made possible by the coordination of two ions, originally believed to be zinc, but now known to be iron. These molecules are coordinated by 9

Desaturase Enzyme

SCD function ^[1]

Disease

Structural highlights