Recombinant Human FMO3, N-His

Reference: YHD95801
Product nameRecombinant Human FMO3, N-His
Uniprot IDP31513
Origin speciesHomo sapiens (Human)
Expression systemProcaryotic expression
Protein delivered with Tag?N-Terminal His Tag
Buffer0.01M PBS, pH 7.4.
Delivery conditionDry Ice
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Host speciesEscherichia coli (E.coli)
Aliases /SynonymsDimethylaniline oxidase 3, FMO form 2, Dimethylaniline monooxygenase [N-oxide-forming] 3, FMO3, FMO II, FMO 3, Trimethylamine monooxygenase, Hepatic flavin-containing monooxygenase 3
NoteFor research use only

Description of Recombinant Human FMO3, N-His

Introduction to Recombinant Human FMO3, N-His

Recombinant Human FMO3, N-His is a protein that plays a crucial role in the metabolism of various drugs and xenobiotics in the human body. It is a member of the flavin-containing monooxygenase (FMO) family of enzymes and is primarily found in the liver. This enzyme is encoded by the FMO3 gene and is responsible for the oxidation of a wide range of drugs, chemicals, and other foreign substances.

Structure of Recombinant Human FMO3, N-His

The recombinant form of FMO3, N-His is a 532 amino acid protein with a molecular weight of approximately 60 kDa. It is composed of two major domains, the FAD-binding domain and the substrate-binding domain. The FAD-binding domain contains the active site of the enzyme and is responsible for binding to the cofactor flavin adenine dinucleotide (FAD). The substrate-binding domain, on the other hand, is responsible for binding to the various substrates that are metabolized by FMO3. This enzyme also contains a histidine tag (N-His) at the N-terminus, which allows for purification and detection of the protein.

Activity of this protein

The primary function of FMO3, N-His is to catalyze the oxidation of nucleophilic heteroatoms, such as sulfur, nitrogen, and phosphorus, in various substrates. This process involves the transfer of an oxygen atom from molecular oxygen to the substrate, resulting in the formation of a hydroxylated product. This reaction is essential for the detoxification and elimination of drugs and other xenobiotics from the body.

FMO3, N-His has a broad substrate specificity and is capable of metabolizing a wide range of compounds, including drugs such as tamoxifen, caffeine, and codeine. It is also involved in the metabolism of dietary compounds, such as trimethylamine (TMA), which is found in fish and other seafood. Defects in FMO3, N-His activity can lead to a condition known as trimethylaminuria, where individuals are unable to metabolize TMA, resulting in a fishy odor in their urine, sweat, and breath.

Application of Recombinant Human FMO3, N-His

The ability of FMO3, N-His to metabolize drugs and other foreign substances has made it a valuable target for drug development. By understanding the structure and activity of this enzyme, researchers can design drugs that are less susceptible to metabolism by FMO3, thus increasing their efficacy and reducing potential side effects. Additionally, FMO3, N-His can also be used as a biomarker for drug metabolism and drug-drug interactions.

Furthermore, mutations in the FMO3 gene have been linked to various diseases, including trimethylaminuria, hypertension, and chronic kidney disease. Therefore, the study of FMO3, N-His can provide valuable insights into the underlying mechanisms of these diseases and aid in the development of potential treatments.

In conclusion, Recombinant Human FMO3, N-His is a vital enzyme involved in the metabolism of drugs and other foreign substances in the human body. Its structure, activity, and application make it a valuable target for drug development and a potential biomarker for various diseases. Further research on this enzyme can lead to a better understanding of drug metabolism and the development of more effective and safer drugs.


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