Target Name: GGT5
NCBI ID: G2687
Review Report on GGT5 Target / Biomarker Content of Review Report on GGT5 Target / Biomarker
GGT5
Other Name(s): GGTLA1 | gamma-glutamyl transpeptidase-related enzyme | GGT-REL | Gamma-glutamyltransferase 5 | gamma-glutamyl transpeptidase-related protein | Glutathione hydrolase 5 proenzyme (isoform 1) | GGT5 variant 1 | gamma-glutamyltransferase 5 | DKFZp566O011 | Gamma-glutamyltranspeptidase 5 | gamma-glutamyl cleaving enzyme | Gamma-glutamyl cleaving enzyme | Glutathione hydrolase 5 heavy chain | gamma-glutamyltransferase-like activity 1 | Gamma-glutamyl transpeptidase-related protein | Glutathione hydrolase 5 | Gamma-glutamyl transpeptidase-related enzyme | Gamma-glutamyltransferase-like activity 1 | leukotriene-C4 hydrolase | GGT-rel | Glutathione hydrolase 5 light chain | Leukotriene-C4 hydrolase | Glutathione hydrolase 5 proenzyme | FLJ92733 | GGL | GGT5_HUMAN | gamma-glutamyltranspeptidase 5 | Gamma-glutamyltransferase 5, transcript variant 1 | GGT 5

GGTase-5: A Key Enzyme in Arsenic Detoxification

GGT5 (GGTLA1) is a gene that encodes for a protein known as GGTase-5 (also known as GSTM4). GGTase is a family of enzymes that are involved in the detoxification of xenobiotics, which are harmful substances that can be found in the environment and in our food and drinks. GGTase-5 is a member of the GGTase family and is responsible for the detoxification of arsenic, a highly toxic substance that is commonly found in natural water sources such as rivers, lakes, and groundwater.

Arsenic is a naturally occurring element that is found in soil, water, and various foods, including some fruits and vegetables. However, in high concentrations, arsenic is toxic and can cause serious health problems. The arsenic detoxification system is a complex process that involves the GGTase enzyme, which is responsible for breaking down arsenic and removing it from the body. GGTase-5 is a critical enzyme in this system, as it helps to facilitate the detoxification of arsenic by activating the detoxification pathway.

GGTase-5 is a transmembrane protein that is expressed in various tissues throughout the body, including the liver, spleen, and pancreas. It is a member of the superfamily of transmembrane protein (SMP) and is characterized by the presence of an extracellular domain, a transmembrane region, and an intracellular domain. The transmembrane region of GGTase-5 is responsible for its unique function in the detoxification of arsenic.

The transmembrane region of GGTase-5 contains a catalytic site that is responsible for the detoxification of arsenic. Arsenic is a highly reactive element that can form a cationic species, which is toxic to many cellular components, including proteins. The catalytic site of GGTase-5 is able to bind to arsenic and activate the detoxification pathway by creating a cationic species that is then able to interact with and remove the arsenic from the cell. This process is highly specific and targeted, and is able to remove arsenic from the cell even at low concentrations.

GGTase-5 is also involved in the detoxification of other xenobiotics, including arsenicicin, a compound that is found in some fruits and vegetables. Arsenicin is toxic to humans and can cause serious health problems if ingested in high concentrations. GGTase-5 is able to remove arsenicin from the body by activating the detoxification pathway and creating a cationic species that can interact with and remove the arsenicin from the cell.

In conclusion, GGTase-5 is a critical enzyme in the arsenic detoxification system. It is involved in the detoxification of arsenic and other xenobiotics, and is able to remove these substances from the body in a highly specific and targeted manner. GGTase-5 is a potential drug target and may be useful in the development of new treatments for arsenic-related diseases. Further research is needed to fully understand the role of GGTase-5 in the detoxification of arsenic and other xenobiotics, and to explore its potential as a drug target.

Protein Name: Gamma-glutamyltransferase 5

Functions: Cleaves the gamma-glutamyl peptide bond of glutathione and glutathione-S-conjugate such as leukotriene C4 (PubMed:21447318). Does not cleaves gamma-glutamyl compounds such as gamma-glutamyl leucine (PubMed:21447318). May also catalyze a transpeptidation reaction in addition to the hydrolysis reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound (PubMed:21447318). Acts as a negative regulator of geranylgeranyl glutathione bioactivity by cleaving off its gamma-glutamyl group, playing a role in adaptive immune responses (PubMed:30842656)

The "GGT5 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 GGT5 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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