CTH: A Protein Linked To Various Diseases as A Drug Target (G1491)

Target Name: CTH

NCBI ID: G1491

Content of Review Report on CTH Target / Biomarker

CTH

CTH: A Protein Linked To Various Diseases as A Drug Target

CTH (Cysteine-protein sulfhydrase), also known as cysteine 鈥嬧?媝rotease S (CPS), is a protein that is found in various cell types throughout the body. It plays a crucial role in the regulation of protein structure and function, particularly in the breaking down of disulfide bonds between proteins. Mutations in the cysteine 鈥嬧?媝rotein have been linked to a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. As a result, CTH has emerged as a promising drug target and biomarker for a variety of diseases.

CTH is a protein that is composed of two distinct subunits, a catalytic subunit and a regulatory subunit. The catalytic subunit consists of the amino acids Asp121, Asp122, Asp123, Asp124, and Asp125, while the regulatory subunit consists of the amino acids Asn126, Asn127, Asn128, and Asn129. The catalytic subunit contains the active site for protein-protein interaction, where it interacts with other proteins to break down disulfide bonds.

Disulfide bonds are covalent bonds that form between two amino acids when they are fused together. These bonds are important for the stability and function of proteins, as they allow them to fold into their specific shapes and perform their various functions. The cysteine 鈥嬧?媝rotein uses a specific mechanism to break down disulfide bonds, which involves the formation of a covalent bond between the sulfur atoms of the cysteine 鈥嬧?媠ide chain and the carbon atom of the adjacent protein.

Mutations in the cysteine 鈥嬧?媝rotein have been linked to a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. For example, studies have shown that mutations in the cysteine 鈥嬧?媝rotein are frequently observed in various types of cancer, including breast, ovarian, and prostate cancers. These mutations can disrupt the normal function of the cysteine 鈥嬧?媝rotein, leading to the formation of aberrant proteins that are resistant to apoptosis and can promote the growth and survival of cancer cells.

In addition to its role in cancer, CTH has also been linked to a number of other diseases. For example, studies have shown that CTH mutations are frequently observed in neurodegenerative diseases, including Alzheimer's and Parkinson's diseases. These mutations can disrupt the normal function of the cysteine 鈥嬧?媝rotein, leading to the formation of abnormal proteins that are involved in the progression of neurodegeneration. In addition, CTH mutations have also been linked to autoimmune disorders, such as rheumatoid arthritis and lupus.

As a result of its role in the regulation of protein structure and function, CTH has emerged as a promising drug target and biomarker for a variety of diseases. For example, studies have shown that blocking the activity of CTH can lead to the inhibition of the formation of aberrant proteins in cancer cells, leading to the regression of cancer growth. In addition, CTH has also been shown to be involved in the regulation of the immune response, leading to the suppression of autoimmune disorders.

In conclusion, CTH (Cysteine-protein sulfhydrase) is a protein that is found in various cell types throughout the body. It plays a crucial role in the regulation of protein structure and function, particularly in the breaking down of disulfide bonds between proteins. Mutations in the cysteine 鈥嬧?媝rotein have been linked to a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. As a result, CTH has emerged as a promising drug target and biomarker for a variety of diseases. Further research is needed to fully understand the role of CTH in these diseases and to develop effective treatments.

Protein Name: Cystathionine Gamma-lyase

Functions: Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate (PubMed:10212249, PubMed:19261609, PubMed:19961860, PubMed:18476726). Part of the L-cysteine derived from the trans-sulfuration pathway is utilized for biosynthesis of the ubiquitous antioxidant glutathione (PubMed:18476726). Besides its role in the conversion of L-cystathionine into L-cysteine, it utilizes L-cysteine and L-homocysteine as substrates (at much lower rates than L,L-cystathionine) to produce the endogenous gaseous signaling molecule hydrogen sulfide (H2S) (PubMed:10212249, PubMed:19261609, PubMed:19961860, PubMed:19019829). In vitro, it converts two L-cysteine molecules into lanthionine and H2S, also two L-homocysteine molecules to homolanthionine and H2S, which can be particularly relevant under conditions of severe hyperhomocysteinemia (which is a risk factor for cardiovascular disease, diabetes, and Alzheimer's disease) (PubMed:19261609). Lanthionine and homolanthionine are structural homologs of L,L-cystathionine that differ by the absence or presence of an extra methylene group, respectively (PubMed:19261609). Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function (PubMed:22169477). By generating the gasotransmitter H2S, it participates in a number of physiological processes such as vasodilation, bone protection, and inflammation (Probable) (PubMed:29254196). Plays an essential role in myogenesis by contributing to the biogenesis of H2S in skeletal muscle tissue (By similarity). Can also accept homoserine as substrate (By similarity). Catalyzes the elimination of selenocystathionine (which can be derived from the diet) to yield selenocysteine, ammonia and 2-oxobutanoate (By similarity)

The "CTH 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 CTH 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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