Target Name: PHYHD1
NCBI ID: G254295
Review Report on PHYHD1 Target / Biomarker Content of Review Report on PHYHD1 Target / Biomarker
PHYHD1
Other Name(s): Phytanoyl-CoA dioxygenase domain-containing protein 1 (isoform a) | Phytanoyl-CoA dioxygenase domain containing 1 | Protein PHYHD1 | PHYD1_HUMAN | Phytanoyl-CoA dioxygenase domain-containing protein 1 | MGC16638 | PHYHD1 variant 1 | Phytanoyl-CoA dioxygenase domain containing 1, transcript variant 1 | phytanoyl-CoA dioxygenase domain containing 1

PHYHD1: A Potential Drug Target and Biomarker

PHYHD1, or Phytanoyl-CoA dioxygenase domain-containing protein 1, is a protein that has been identified as a potential drug target and biomarker for several diseases. PHYHD1 is a single-domain protein that is expressed in a variety of organisms, including plants, animals, and bacteria. It is characterized by a unique domain that includes a dioxygenase activity, as well as a conserved catalytic core that is involved in the oxidation of carboxylic acids.

The PHYHD1 gene has been identified in many organisms, including humans, and it is expressed in various cell types throughout the body. It has been shown to be involved in the metabolism of a variety of carboxylic acids, including those found in proteins, nucleic acids, and lipids. In addition to its role in metabolism, PHYHD1 has also been shown to play a role in several cellular processes, including cell signaling, DNA replication, and stress response.

One of the key reasons why PHYHD1 has potential as a drug target is its dioxygenase activity. Dioxygenase enzymes are involved in the production of reactive oxygen species (ROS), which can damage cellular components and contribute to a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. By modulating the activity of PHYHD1, researchers may be able to reduce the production of ROS and improve cellular health.

Another potential mechanism by which PHYHD1 could be targeted as a drug is its role in cell signaling. Many cellular signaling pathways involve the production of reactive oxygen species, which can either promote or inhibit cell growth and division. By modulating the activity of PHYHD1, researchers may be able to regulate cell signaling and improve cellular health.

In addition to its potential as a drug target, PHYHD1 also has potential as a biomarker. The dioxygenase activity of PHYHD1 has been shown to be involved in the production of ROS, which can be used as a marker for cellular stress and dysfunction. By detecting the levels of ROS in cells, researchers may be able to assess the cellular health and identify potential therapeutic interventions.

While the potential drug targets and biomarkers for PHYHD1 are still being explored, research into its role in disease is already underway. A number of studies have shown that modulating the activity of PHYHD1 can improve cellular health and reduce the production of ROS, which may be a promising strategy for the development of therapeutic interventions.

In conclusion, PHYHD1 is a protein that has potential as a drug target and biomarker for a variety of diseases. Its unique dioxygenase activity and conserved catalytic core make it an attractive target for therapeutic intervention, while its role in cell signaling and stress response also suggests that it may have important functions in cellular health. Further research is needed to fully understand the role of PHYHD1 in disease and to develop effective therapeutic interventions.

Protein Name: Phytanoyl-CoA Dioxygenase Domain Containing 1

Functions: 2-oxoglutarate(2OG)-dependent dioxygenase that catalyzes the conversion of 2-oxoglutarate to succinate and CO(2) in an iron-dependent manner (PubMed:21530488). However, does not couple 2OG turnover to the hydroxylation of acyl-coenzyme A derivatives, implying that it is not directly involved in phytanoyl coenzyme-A metabolism (PubMed:21530488). Does not show detectable activity towards fatty acid CoA thioesters (PubMed:21530488)

The "PHYHD1 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 PHYHD1 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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