Target Name: PHYH
NCBI ID: G5264
Review Report on PHYH Target / Biomarker Content of Review Report on PHYH Target / Biomarker
PHYH
Other Name(s): Phytanoyl-CoA dioxygenase, peroxisomal (isoform b) | PHYH1 | Phytanoil-CoA alpha hydroxylase | phytanoyl-CoA dioxygenase, peroxisomal | Phytanoyl-CoA dioxygenase | PHYH variant 1 | phytanoyl-CoA alpha-hydroxylase | Phytanoyl-CoA 2-hydroxylase, transcript variant 2 | Phytanoyl-CoA alpha-hydroxylase | PAHX | LN1 | PHYN | phytanic acid oxidase | PHYH variant 2 | PAHX_HUMAN | PhyH | Phytanoyl-CoA dioxygenase, peroxisomal | Phytanoyl-CoA 2 oxoglutarate dioxygenase | Phytanoyl-CoA 2-hydroxylase | Phytanoyl-CoA hydroxylase (Refsum disease) | Phytanic acid oxidase | phytanoyl-CoA 2-hydroxylase | Phytanoyl-CoA dioxygenase, peroxisomal (isoform a) | RD | LNAP1 | Phytanoyl-CoA 2-hydroxylase, transcript variant 1 | phytanoil-CoA alpha hydroxylase | phytanoyl-CoA 2 oxoglutarate dioxygenase

PHYH: A Potential Drug Target for Cellulose Metabolism

PHYH, or Phytanoyl-CoA Dioxygenase, is a peroxisomal enzyme that is involved in the metabolism of phytanoyl-coenzyme A (PCA), a crucial compound in the production of cellulose and other plant cell walls. This enzyme is a key player in the cell's ability to produce and break down cellulose, and is a potential drug target or biomarker for a variety of diseases.

PHYH is a single-chain transmembrane protein that is located in the peroxisome, a small organelle that is responsible for the production and breaking down cellulose. The peroxisome is a common organelle in eukaryotic cells and is characterized by a double membrane and a protein-rich cytoplasm. PHYH is one of the proteins that is associated with the peroxisome and is responsible for the final step of the cell's ability to break down cellulose.

PHYH is a critical enzyme in the breakdown of cellulose, as it converts the phytanoyl-coenzyme A to its active form, which is necessary for the production of cellulose. This conversion occurs through a series of chemical reactions that involve the transfer of a carbon atom from the substrate to the active site of the enzyme. The active site of PHYH contains a catalytic pocket that is optimized for the transfer of carbon atoms, and the enzyme is able to catalyze this transfer with high efficiency.

PHYH is also involved in the regulation of other cellular processes. For example, it has been shown to be involved in the metabolism of pantothenic acid, a crucial coenzyme that is involved in the production of energy from fatty acids. In addition, PHYH has been shown to be involved in the regulation of protein synthesis and to play a role in the detoxification of xenobiotics.

As a drug target, PHYH has the potential to be used for the treatment of a variety of diseases. One of the most promising applications for PHYH is its potential as a therapeutic agent for diseases caused by the buildup of toxic cellulose, such as cancer, neurodegenerative diseases, and chronic obstructive pulmonary disease (COPD).

PHYH has also been shown to have potential as a biomarker for a variety of diseases. For example, it has been shown to be elevated in the blood of patients with cancer, and to be decreased in the blood of patients with neurodegenerative diseases. These findings suggest that PHYH may be a useful biomarker for the diagnosis and monitoring of these diseases.

In conclusion, PHYH is a peroxisomal enzyme that is involved in the metabolism of phytanoyl-coenzyme A and has the potential to be a drug target or biomarker for a variety of diseases. Further research is needed to fully understand the role of PHYH in cellular processes and to develop effective treatments for the diseases that are caused by its dysfunction.

Protein Name: Phytanoyl-CoA 2-hydroxylase

Functions: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (PubMed:9326939, PubMed:10744784, PubMed:12031666, PubMed:12923223). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl- and 4-methyl-branched acyl-CoAs (PubMed:10744784, PubMed:12923223)

The "PHYH 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 PHYH 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

More Common Targets

PHYHD1 | PHYHIP | PHYHIPL | PHYKPL | PI15 | PI16 | PI3 | PI4K2A | PI4K2B | PI4KA | PI4KAP1 | PI4KAP2 | PI4KB | PIANP | PIAS1 | PIAS2 | PIAS3 | PIAS4 | PIBF1 | PICALM | PICART1 | PICK1 | PICSAR | PID1 | PIDD1 | PIERCE1 | PIERCE2 | PIEZO1 | PIEZO2 | PIF1 | PIFO | PIGA | PIGB | PIGBOS1 | PIGC | PIGF | PIGG | PIGH | PIGK | PIGL | PIGM | PIGN | PIGO | PIGP | PIGQ | PIGR | PIGS | PIGT | PIGU | PIGV | PIGW | PIGX | PIGY | PIGZ | PIH1D1 | PIH1D2 | PIK3AP1 | PIK3C2A | PIK3C2B | PIK3C2G | PIK3C3 | PIK3CA | PIK3CA-DT | PIK3CB | PIK3CD | PIK3CD-AS1 | PIK3CD-AS2 | PIK3CG | PIK3IP1 | PIK3IP1-DT | PIK3R1 | PIK3R2 | PIK3R3 | PIK3R4 | PIK3R5 | PIK3R6 | PIKFYVE | PILRA | PILRB | Pim Kinase | PIM1 | PIM2 | PIM3 | PIMREG | PIN1 | PIN1-DT | PIN1P1 | PIN4 | PINCR | PINK1 | PINK1-AS | PINLYP | PINX1 | PIP | PIP4K2A | PIP4K2B | PIP4K2C | PIP4P1 | PIP4P2 | PIP5K1A