Introduction

Overview

Stearoyl-CoA Desaturase is an integral membrane protein located in the endoplasmic reticulum and is conserved across all eukaryotes (Bai et al., 2015). SCD-1 is expressed in Mus musculus. The human homolog, SCD1, shares 85% sequence identity with all four SCD’s found in M. musculus (Scd1-Scd4).

Stearoyl-CoA Desaturase is an enzyme which speeds up desaturation of a double bond within a fatty acid hydrocarbon chain. The addition of a double bond is necessary for the biosynthesis of monounsaturated fatty acids such as: cholesterol, phospholipids, and triglycerides. SCD-1 is able to interact with two different substrates: stearoyl-CoA or palmitoyl-CoA. Figure 1 represents the that stearoyl-CoA substrate fits in to interact with the enzyme. Within the enzyme there exists a di-iron complex that is stabilized by 8 histidine residues (Histidine Stabilization image). SCD specifically catalyzes the C9-C10-cis desaturation of fatty stearoyl-CoA substrates from saturated fatty acids that come from an organism’s diet (Paton and Ntambi, 2009). Functioning SCD creates the balance between the accumulation and use of fats in the body. The enzyme plays a critical role in fatty acid metabolism pathways. Inhibition of SCD leads to possible treatment of metabolic disease and cancer.

Desaturation Mechanism

General Methods

Function

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Structure

Related Disease