PHYKPL: A Key Enzyme in Lysine Phosphorylation (G85007)

Target Name: PHYKPL

NCBI ID: G85007

PHYKPL

PHYKPL: A Key Enzyme in Lysine Phosphorylation

PHYKPL (5-phosphohydroxy-L-lysine phospho-lyase) is a protein that is expressed in various tissues and cells in the human body. It is a key enzyme in the pathway of lysine phosphorylation, which is a process that is involved in the Regulation of various cellular processes, including cell signaling, DNA replication, and protein synthesis. Mutations in the PHYKPL gene have been linked to various diseases, including cancer, neurodegenerative diseases, and developmental disorders. As a result, PHYKPL has become an attractive target for drug development and research.

The PHYKPL gene is located on chromosome 11 and encodes a protein that has a molecular weight of approximately 110 kDa. The protein has four known isoforms, which are produced by alternative splicing of the gene. These isoforms include PHYKPL1, PHYKPL2, PHYKPL3, and PHYKPL4 , which differ in their N- and C-terminus extensions. PHYKPL1 is the most abundant isoform, and it is expressed in various tissues and cells, including muscle, liver, kidney, and brain. The other isoforms are less abundant and are mainly expressed in the brain and nervous system.

PHYKPL is involved in the regulation of lysine phosphorylation, which is a critical post-translational modification (PTM) that plays a crucial role in the regulation of various cellular processes. Lysine phosphorylation is the process by which the amino acid lysine is added to a target protein, usually through a phosphate group. This modification is involved in the regulation of protein stability, localization, and interactions with other cellular components. It is also involved in the regulation of DNA replication, gene transcription, and cell signaling.

PHYKPL is a key enzyme in the pathway of lysine phosphorylation. It is responsible for the initial step of this process, which involves the conversion of the lysine acetyl group to an acetyl-modified lysine. This conversion is critical for the regulation of protein stability and localization. PHYKPL catalyzes the conversion of lysine acetyl groups to lysine esters using ATP and a specific set of co-factors. The resulting acetyl-modified lysine is then available to participate in subsequent steps of lysine phosphorylation.

Mutations in the PHYKPL gene have been linked to various diseases, including cancer, neurodegenerative diseases, and developmental disorders. For example, mutations in the PHYKPL gene have been linked to the development of neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and Huntington's disease. These mutations have been shown to disrupt the regulation of lysine phosphorylation and to lead to the misfolding and aggregation of misfolded proteins.

In addition to its role in the regulation of lysine phosphorylation, PHYKPL is also a potential drug target. The high level of expression of PHYKPL in various tissues and cells makes it an attractive target for small molecule inhibitors. Several compounds have been shown to inhibit the activity of PHYKPL, including inhibitors that target the active site of the enzyme and inhibitors that bind to the negative regulatory domain of the enzyme. These compounds have been shown to be effective in various cellular assays, including cell-based assays and in animal models of disease.

Furthermore, the study of PHYKPL has also provided new insights into the regulation of lysine phosphorylation. The structure and function of the enzyme have been studied using various techniques, including crystallization, X-ray crystallography, and biochemical assays. These studies have provided new insights into the mechanisms of lysine phosphorylation and have led to the identification of new

Protein Name: 5-phosphohydroxy-L-lysine Phospho-lyase

Functions: Catalyzes the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate and 2-aminoadipate semialdehyde

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