Target Name: FMO2
NCBI ID: G2327
Review Report on FMO2 Target / Biomarker Content of Review Report on FMO2 Target / Biomarker
FMO2
Other Name(s): Flavin containing dimethylaniline monoxygenase 2, transcript variant 1 | FMO2_HUMAN | Flavin containing monooxygenase 2 (non -functional) | flavin containing dimethylaniline monoxygenase 2 | flavin containing monooxygenase 2 (non-functional) | pulmonary flavin-containing monooxygenase 2 | Pulmonary flavin-containing monooxygenase 2 | FMO 1B1 | Flavin-containing monooxygenase 2 (isoform a) | FMO2 variant 1 | FMO 2 | FLJ40826 | dimethylaniline oxidase 2 | FMO1B1 | Flavin-containing monooxygenase 2 | dimethylaniline monooxygenase [N-oxide-forming] 2 | Dimethylaniline oxidase 2 | FMO, pulmonary

FMO2: A Potential Drug Target for Flavin Derivatives

FMO2, also known as Flavin containing dimethylaniline monoxygenase 2, is a protein that plays a crucial role in the metabolism of flavin derivatives, which are a group of pigments found in many plants and animals. Flavin derivatives are involved in a wide range of physiological processes in the cell, including photosynthesis, signaling, and cellular signaling pathways.

FMO2 is a key enzyme in the pathway for the synthesis of flavin derivatives from tryptophan, which is the most abundant amino acid in the human body. Tryptophan is a key precursor for the synthesis of niacin, which is a well-known molecule that plays a central role in the production of energy in the body. Niacin is also involved in the regulation of various cellular processes, including cell signaling, inflammation, and blood clotting.

FMO2 is a protein that is expressed in a variety of tissues throughout the body, including the brain, heart, liver, and kidneys. It is primarily localized to the endoplasmic reticulum, which is the network of ribosomes and other cellular structures that synthesize and transport proteins to the cell surface.

FMO2 is involved in the metabolism of flavin derivatives by catalyzing the conversion of tryptophan to niacin via a series of enzymatic steps. The first step in this process is the conversion of tryptophan to 5-methyl-indole-3-carboxylic acid (5-MeICAC), which is then converted to niacin through the action of the enzyme tryptophan aminotransferase (TAT).

FMO2 is a potent inhibitor of TAT, which is an enzyme that catalyzes the conversion of tryptophan to niacin via a series of steps. TAT is a key enzyme in the pathway for the production of niacin, which is involved in the regulation of various cellular processes, including cell signaling, inflammation, and blood clotting.

By inhibiting TAT, FMO2 can inhibit the production of niacin, which can have a wide range of therapeutic potential. For example, niacin has been shown to have anti-inflammatory effects, which can be useful in the treatment of a variety of inflammatory conditions. Additionally, niacin has been shown to have neuroprotective effects, which can be useful in the treatment of neurodegenerative conditions.

FMO2 is also involved in the metabolism of other flavin derivatives, including menhypterin and indole-3-carboxylic acid. These molecules are involved in various cellular processes, including signaling, DNA replication, and metabolism.

In addition to its role in the metabolism of flavin derivatives, FMO2 is also a potential drug target. The high level of homogeneity between FMO2 and TAT makes them a promising target for small molecule inhibitors. Additionally, the known interactions between FMO2 and various drug compounds suggest that they may be useful in the development of new therapeutic agents.

In conclusion, FMO2 is a protein that plays a crucial role in the metabolism of flavin derivatives, which are involved in a wide range of physiological processes in the cell. The inhibition of FMO2 by small molecule inhibitors has the potential to be a useful therapeutic approach for the treatment of a variety of conditions. Further research is needed to fully understand the role of FMO2 in the flavin pathway and to develop new therapeutic agents that can target this protein.

Protein Name: Flavin Containing Dimethylaniline Monoxygenase 2

Functions: Catalyzes the oxidative metabolism of numerous xenobiotics, including mainly therapeutic drugs and insecticides that contain a soft nucleophile, most commonly nitrogen and sulfur and participates to their bioactivation (PubMed:9804831, PubMed:15294458, PubMed:15144220, PubMed:18948378, PubMed:18930751). Specifically catalyzes S-oxygenation of sulfur derived compounds such as thioureas-derived compounds, thioetherorganophosphates to their sulfenic acid (PubMed:9804831, PubMed:15144220). In vitro, catalyzes S-oxygenation of the second-line antitubercular drugs thiacetazone (TAZ) and ethionamide (ETA), forming a sulfinic acid and a carbodiimide via a postulated sulfenic acid intermediate (PubMed:18948378, PubMed:18930751). Also catalyzes S-oxygenation of the thioether-containing organophosphate insecticides, phorate and disulfoton (PubMed:15294458)

The "FMO2 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 FMO2 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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