Target Name: FADS3
NCBI ID: G3995
Review Report on FADS3 Target / Biomarker Content of Review Report on FADS3 Target / Biomarker
FADS3
Other Name(s): delta(13) desaturase | CYB5RP | Cytochrome b5-related protein | delta(13) fatty acid desaturase | fatty acid desaturase 3 | Delta(13) desaturase | delta-9-desaturase | Delta-9 fatty acid desaturase | delta-9 fatty acid desaturase | Delta-9-desaturase | Linoleoyl-CoA desaturase (delta-9-desaturase)-like 3 | Delta(13) fatty acid desaturase | cytochrome b5-related protein | linoleoyl-CoA desaturase (delta-9-desaturase)-like 3 | FADS3_HUMAN | Fatty acid desaturase 3 | LLCDL3

FADS3: A Key Enzyme in The?9-Fatty Acid Oxidation Pathway

FADS3 (未-13 desaturase) is a gene that encodes a protein involved in the fatty acid oxidation pathway, which is a critical process for the maintenance of cellular energy homeostasis. FADS3 is a key enzyme in the 螖9-fatty acid oxidation pathway, which is a central metabolic pathway for the production of long-chain fatty acids from the 螖9 fatty acids, such as omega-3 and omega-6 fatty acids. The 螖9-fatty acid oxidation pathway is also known as the \"endogenous synthesis\" pathway because it is generated by the body's own metabolic processes, rather than being synthesized from scratch.

FADS3 is a 24-kDa protein that is expressed in various tissues, including brain, heart, liver, and muscle. It is a member of the NAD+-dependent enzyme superfamily 3 (NAD+-dependent enzymes), which includes other enzymes involved in energy metabolism, such as FAD (nicotinamide adenine dinucleotide) and CoQ10. FADS3 is characterized by its catalytic active site, which is located at the N-terminus of the protein and is responsible for the substrate-dependent desaturation of fatty acids.

FADS3 functions as a critical enzyme in the 螖9-fatty acid oxidation pathway, which is involved in the production of long-chain fatty acids from the 螖9 fatty acids. The 螖9-fatty acid oxidation pathway is a central metabolic pathway for the maintenance of cellular energy homeostasis and is critical for the survival of all living organisms.

FADS3 is a protein that is expressed in various tissues and is involved in the 螖9-fatty acid oxidation pathway. It is a key enzyme in this pathway and is involved in the production of long-chain fatty acids from the 螖9 fatty acids. As a result, FADS3 may be a drug target or biomarker for various diseases associated with the 螖9-fatty acid oxidation pathway, such as heart disease, cancer, and neurological disorders.

FADS3 as a drug target

FADS3 has been identified as a potential drug target for various diseases associated with the 螖9-fatty acid oxidation pathway. One of the main reasons for this is the fact that FADS3 is involved in the production of long-chain fatty acids, which are important energy sources for the body. Disruptions in the 螖9-fatty acid oxidation pathway have been linked to the development of various diseases, including heart disease, cancer, and neurological disorders.

For example, individuals with a genetic defect in the FADS3 gene have been shown to have an increased risk of developing heart disease. This is because individuals with the genetic defect are unable to produce long-chain fatty acids from the 螖9 fatty acids, which can lead to an imbalance in the levels of omega-3 and omega-6 fatty acids in the body. This imbalance has been linked to an increased risk of developing heart disease.

FADS3 has also been shown to be involved in the development of certain cancers, such as breast and ovarian cancer. Studies have shown that individuals with certain genetic mutations, such as those in the FADS3 gene, are more likely to develop these cancers. This is because these mutations can disrupt the 螖9-fatty acid oxidation pathway and lead to an imbalance in the production of long-chain fatty acids.

In addition to its involvement in the production of long-chain fatty acids, FADS3 is also involved in the regulation of cellular energy homeostasis. This is important because maintaining cellular energy homeostasis is critical for the survival of all living organisms. Disruptions in

Protein Name: Fatty Acid Desaturase 3

Functions: Mammals have different sphingoid bases that differ in their length and/or pattern of desaturation and hydroxyl groups. The predominant sphingoid base in mammalian ceramides is sphing-4-enine (sphingosine or SPH) which has a trans desaturation at carbon 4. FADS3 is a ceramide desaturase that introduces a cis double bond between carbon 14 and carbon 15 of the SPH-containing ceramides, producing sphinga-4,14-dienine-containing ceramides (SPD ceramides). SPD ceramides occur widely in mammalian tissues and cells. Due to their unusual structure containing a cis double bond, SPD ceramides may have an opposite, negative role in lipid microdomain formation relative to conventional ceramides (PubMed:31916624). FADS3 also acts as a methyl-end fatty acyl coenzyme A (CoA) desaturase that introduces a cis double bond between the preexisting double bond and the terminal methyl group of the fatty acyl chain. Desaturates (11E)-octadecenoate (trans-vaccenoate, the predominant trans fatty acid in human milk) at carbon 13 to generate (11E,13Z)-octadecadienoate (also known as conjugated linoleic acid 11E,13Z-CLA)

The "FADS3 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about FADS3 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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