FADS3
FADS3 (fatty acid desaturase 3, also known as CYB5RP and LLCDL3) is an endoplasmic reticulum membrane desaturase of the fatty acid desaturase family. It introduces cis double bonds into sphingoid bases and into fatty acyl chains. Browse Assay Genie's current range of FADS3 research reagents below, or read on for the biology behind the target.
FADS3 is a desaturase that introduces a cis (Z) double bond between carbon 14 and carbon 15 of the sphingoid base, also known as the long chain base. Acting on sphing-4-enine (sphingosine), the predominant sphingoid base in mammalian ceramides, it produces sphinga-4,14-dienine. It prefers sphingosine-containing ceramides as substrates, can also metabolise free sphingosine, and shows activity towards dihydrosphingosine-containing ceramides. Its desaturase mechanism involves electron transfer facilitated by cytochrome b5.
Sphinga-4,14-dienine ceramides occur widely in mammalian tissues and cells. Because of their cis double bond, they may have an opposite, negative role in lipid microdomain formation relative to conventional ceramides. FADS3 could also contribute to the detoxification of 1-deoxysphingolipids, by desaturating the cytotoxic 1-deoxysphinganine to 1-deoxysphingenine. It produces 14Z-sphingosine-containing sphingolipids, which can be found in patients with DEGS1 mutations. FADS3 also acts as a methyl-end fatty acyl coenzyme A desaturase, converting (11E)-octadecenoate (trans-vaccenoate) to (11E,13Z)-octadecadienoate, a conjugated linoleic acid.
The FADS3 gene belongs to the fatty acid desaturase type 1 family. FADS family members are considered fusion products of an N-terminal cytochrome b5-like domain and a C-terminal multiple membrane-spanning desaturase portion, both with conserved histidine motifs. The gene is clustered with FADS1 and FADS2 at 11q12-q13.1, and the cluster is thought to have arisen by gene duplication, based on similar exon/intron organisation.
FADS3 generates sphinga-4,14-dienine from sphingosine, making it a key enzyme for studying sphingoid base diversity in mammalian ceramides.
Ceramides with a cis double bond may act oppositely to conventional ceramides in lipid microdomain formation, a question FADS3 helps address.
FADS3 may help detoxify cytotoxic 1-deoxysphinganine by desaturating it to 1-deoxysphingenine under pathological conditions.
As a methyl-end acyl-CoA desaturase, FADS3 converts trans-vaccenoate to conjugated linoleic acid, relevant to fatty acid metabolism studies.
FADS3 is a desaturase that introduces a cis double bond between carbons 14 and 15 of the sphingoid base, converting sphingosine-containing ceramides into sphinga-4,14-dienine forms. It also acts as a methyl-end fatty acyl-CoA desaturase, converting trans-vaccenoate to (11E,13Z)-octadecadienoate.
FADS3 is also known as CYB5RP and LLCDL3, and its full name is fatty acid desaturase 3. The HGNC group places it among the fatty acid desaturases and the cytochrome b5 domain containing genes, reflecting its N-terminal cytochrome b5-like domain.
FADS3 is clustered with FADS1 and FADS2 at 11q12-q13.1, and the cluster is thought to have arisen by gene duplication. Mouse and rat both have a Fads3 ortholog. Check the datasheet of any product for its validated reactivity.
Other members of the FADS gene cluster, sharing a cytochrome b5-like domain and a membrane-spanning desaturase region.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9Y5Q0; product specifications from Assay Genie datasheets.