SCD5 desaturates ST-CoA to OLE-CoA

Stable Identifier
Reaction [transition]
Homo sapiens
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Stearoyl-CoA desaturase 5 (SCD5, also known as acyl-CoA desaturase 4), located on the ER membrane, utilises O2 and electrons from reduced ferrocytochrome b5 (Fe(2+)Cb5) to catalyse the insertion of a double bond into a range of fatty acyl-CoA substrates. SCD5 is most abundant in brain and pancreas. The reaction annotated here shows stearoyl-CoA (ST-CoA) desaturation to oleoyl-CoA (OLE-CoA). Studies of tagged recombinant enzyme overexpressed in transiently transfected cells suggest that the enzyme forms dimers and higher oligomers (Wang et al. 2005; Zhang et al. 2005).

Literature References
PubMed ID Title Journal Year
15610069 Characterization of human SCD2, an oligomeric desaturase with improved stability and enzyme activity by cross-linking in intact cells

Shi, Y, Yang, Y, Zhang, S

Biochem. J. 2005
15907797 Characterization of HSCD5, a novel human stearoyl-CoA desaturase unique to primates

Cao, G, Wang, J, Su, C, Yu, L, Huang, X, Schmidt, RE, Gould, K

Biochem. Biophys. Res. Commun. 2005
Catalyst Activity

stearoyl-CoA 9-desaturase activity of SCD5 dimer [endoplasmic reticulum membrane]

Orthologous Events
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