KDM1B: The Potential Drug Target of Amine Oxidase (Flavin Containing) Domain 1

Target Name: KDM1B

NCBI ID: G221656

KDM1B

KDM1B: The Potential Drug Target of Amine Oxidase (Flavin Containing) Domain 1

Amine oxidase (flavin containing) domain 1 (KDM1B) is a protein that plays a crucial role in the detoxification of potentially toxic amines, such as those found in drugs, toxins, and other environmental pollutants. This enzyme is a member of the superfamily of NAD+-dependent enzymes, which are involved in a wide range of cellular processes, including metabolism, energy production, and signaling. KDM1B is also known as NAD+-dependent 210 kDa flavin hydrate reductase, and it is localized to the endoplasmic reticulum (ER) and to various organelles, including the mitochondria, where it is involved in the detoxification of amines.

The Importance of KDM1B in Human Health

KDM1B is involved in the detoxification of potentially toxic amines, which are harmful to human health and can cause a wide range of serious health problems, including cancer, neurodegenerative diseases, and cardiovascular diseases. Many of these amines are produced by the body's own metabolism, but some can be derived from environmental sources, such as drugs, pesticides, and other industrial chemicals. These toxins can accumulate in the body and cause damage to cells and organs, leading to a wide range of health problems.

KDM1B's Role in Drug Detoxification

KDM1B is a key enzyme in the detoxification of many drugs, including many Schedule II and III drugs, which are commonly prescribed in humans. Many of these drugs can cause amine-containing metabolites, which can be difficult to eliminate from the body and can contribute to the development of drug-induced toxicity. KDM1B helps to metabolize these amine-containing metabolites and reduce their toxicity.

KDM1B's Role in Environmental Pollution

KDM1B is also involved in the detoxification of environmental pollutants, such as those found in air, water, and soil. Many of these pollutants are toxic to human health and can cause a wide range of health problems, including cancer, neurological and psychiatric disorders, and reproductive problems. KDM1B helps to metabolize these pollutants and reduce their toxicity.

KDM1B as a Drug Target

KDM1B's role in drug detoxification and environmental pollution makes it an attractive target for drug developers. Many drugs that are used to treat a wide range of diseases, including cancer, neurodegenerative diseases, and cardiovascular diseases, cause amine-containing metabolites that can be difficult to eliminate from the body. By targeting KDM1B, drugs can reduce the production of these metabolites and improve the overall safety of these drugs.

In addition, KDM1B may also be a potential biomarker for a variety of diseases, including cancer, neurodegenerative diseases, and cardiovascular diseases. The levels of KDM1B have been shown to be elevated in the bodies of individuals who have been treated with a wide range of drugs, including many cancer medications. This suggests that KDM1B may be a useful biomarker for tracking the effectiveness of these drugs and for identifying potential drug targets.

Conclusion

KDM1B is a protein that plays a crucial role in the detoxification of potentially toxic amines and in the detoxification of environmental pollutants. Its role in drug detoxification and environmental pollution makes it an attractive target for drug developers. In addition, KDM1B may also be a potential biomarker for a variety of diseases. Further research is needed to fully understand the role of KDM1B in human health and to identify potential drug targets and biomarkers for this protein.

Protein Name: Lysine Demethylase 1B

Functions: Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of GLYR1 to achieve such activity, they form a multifunctional enzyme complex that modifies transcribed chromatin and facilitates Pol II transcription through nucleosomes (PubMed:30970244)

The "KDM1B 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 KDM1B 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;
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•   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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