Reactome | SCD desaturates ST-CoA to OLE-CoA

SCD desaturates ST-CoA to OLE-CoA

Stable Identifier

R-HSA-5690565

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum membrane, cytosol

Synonyms

2 Fe(II)-(cytochrome b5) + 2 H(+) + O2 + octadecanoyl-CoA => (9Z)-octadecenoyl-CoA + 2 Fe(III)-(cytochrome b5) + 2 H2O

ReviewStatus

5/5

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Acyl-CoA desaturase (SCD), located on the ER membrane, is the terminal enzyme of the liver microsomal stearyl-CoA desaturase system and is the rate-limiting enzyme in the cellular synthesis of monounsaturated fatty acids (MUFAs) from saturated fatty acids. SCD 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. This example shows stearoyl-CoA (ST-CoA) desaturation to oleoyl-CoA (OLE-CoA) (Li et al. 1994, Zhang et al. 1999). Studies of tagged recombinant enzyme overexpressed in transiently transfected cells suggest that the enzyme forms dimers and higher oligomers (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
7909540	Partial characterization of a cDNA for human stearoyl-CoA desaturase and changes in its mRNA expression in some normal and malignant tissues Wood, CB, Gilmour, RS, Fermor, BF, Li, J, Ding, SF, Habib, NA	Int J Cancer	1994
10229681	Human stearoyl-CoA desaturase: alternative transcripts generated from a single gene by usage of tandem polyadenylation sites Zhang, L, Stenn, K, Prouty, SM, Parimoo, S, Ge, L	Biochem. J.	1999