XDH: A Pro-Active Enzyme in Uridine Metabolism and Disease (G7498)

Target Name: XDH

NCBI ID: G7498

Content of Review Report on XDH Target / Biomarker

XDH

XDH: A Pro-Active Enzyme in Uridine Metabolism and Disease

XDH (Xanthine dehydrogenase/oxidase), also known as UAP (Uridine-2-伪-proteinase), is a protein that is expressed in a variety of tissues throughout the body, including the brain, heart, kidneys, and liver. It is a critical enzyme involved in the metabolism of uridine, a simple nucleotide that is found in all living cells. Uridine is a key component of DNA and RNA, and it is involved in various cellular processes, including DNA replication, transcription, and repair.

XDH is a enzyme that catalyzes the conversion of uridine to xanthine, a modified form of uridine that is involved in the production of reactive oxygen species (ROS) that can cause damage to cells if not properly controlled. XDH is a pro-active enzyme, meaning that it produces reactive oxygen species when it is activated, rather than being a reactant, like most enzymes.

The role of XDH in the control of cellular processes is vast and varied. In addition to its role in the metabolism of uridine, XDH is involved in the regulation of various cellular processes, including cell death, cell signaling, and inflammation. It is also involved in the production of various signaling molecules, including apologize, which plays a role in cell signaling and is involved in the regulation of cell growth, differentiation, and survival.

XDH is a potential drug target for a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Its role in the regulation of uridine metabolism has led to the development of drugs that target the uridine pathway, including the anti-cancer drug Umapimab. Umapimab is an investigational drug that targets the B-cell maturation antigen (BCMA), a protein that is expressed in various types of cancer, including breast, ovarian, and prostate cancer.

In addition to its potential as a drug target, XDH is also a potential biomarker for a variety of diseases. Its role in the regulation of uridine metabolism is well established, and its levels have been used as a diagnostic marker in various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. In addition, its production has been associated with the development of certain diseases, such as xanthinuria, a genetic disorder that is characterized by the accumulation of xanthine in the urine and gastrointestinal tract.

In conclusion, XDH is a critical enzyme that is involved in the regulation of various cellular processes, including cell death, cell signaling, and inflammation. Its role in the metabolism of uridine and its potential as a drug target make it an attractive target for the development of new treatments for a variety of diseases. Further research is needed to fully understand its role in the regulation of uridine metabolism and its potential as a biomarker for various diseases.

Protein Name: Xanthine Dehydrogenase

Functions: Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro)

The "XDH 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 XDH 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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