AGTPBP1: A Protein Deglutamylase Enzyme and Potential Drug Target

Target Name: AGTPBP1

NCBI ID: G23287

AGTPBP1

AGTPBP1: A Protein Deglutamylase Enzyme and Potential Drug Target

Glutamylase (also known as glutamyl-prognathyl-caseinase or GPCR) is a protein that is involved in the regulation of protein degradation in the body. It is a widely expressed enzyme that is found in various cell types, including the brain, pancreas, and muscle. Glutamylase has been implicated in a wide range of physiological processes, including cell signaling, inflammation, and neurodegeneration.

One of the unique features of glutamylase is its ability to regulate protein degradation in a highly specific and targeted manner. It is able to cleave only certain types of proteins, such as neurotransmitters, without causing general protein degradation. This property makes glutamylase an attractive target for drug development.

AGTPBP1: A Promising Protein Deglutamylase Enzyme

The AGTPBP1 protein is a member of the Glutamylase family and is expressed in various tissues and cells in the body. It is highly conserved and has a highly predicted transmembrane domain. AGTPBP1 is known to regulate the degradation of neurotransmitters, such as dopamine, serotonin, and endocannabinoids.

In addition to its role in neurotransmitter degradation, AGTPBP1 has also been shown to play a role in the regulation of inflammation and cellular signaling. It has been shown to be involved in the regulation of the chemokine network, which is a complex system of cytokines and their receptors that is involved in immune and inflammatory responses.

AGTPBP1 has also been shown to play a role in the regulation of cell survival and proliferation. It has been shown to be involved in the regulation of cell cycle progression, cell adhesion, and cell survival.

Drug Targeting AGTPBP1

The potential drug targeting of AGTPBP1 is due to its unique ability to regulate protein degradation in a highly specific and targeted manner. There are several potential drug targets for AGTPBP1, including inhibitors of glutamylase activity and modulators of its activity.

One approach to drug targeting AGTPBP1 is to inhibit its activity with small molecules. One class of small molecules that have been shown to inhibit AGTPBP1 activity is the benzodiazepine class of drugs. These drugs work by binding to GABA receptors and inhibiting the activity of glutamylase.

Another approach to drug targeting AGTPBP1 is to modulate its activity with proteins that can interact with it. One approach is to use antibodies that can bind to AGTPBP1 and prevent it from cleaving its target proteins. This approach has been shown to be effective in animal models of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease.

AGTPBP1 as a Biomarker

In addition to its potential as a drug target, AGTPBP1 has also been shown to be a valuable biomarker for a variety of diseases. For example, it has been shown to be involved in the regulation of neurotransmitter degradation, which is a key factor in the development of neurodegenerative diseases.

In addition, AGTPBP1 has also been shown to play a role in the regulation of inflammation and cellular signaling. It has been shown to be involved in the regulation of the chemokine network, which is a complex system of cytokines and their receptors that is involved in immune and inflammatory responses.

Conclusion

AGTPBP1 is a protein that is involved in the regulation of protein degradation in the body. It is a widely conserved enzyme that has been implicated in a wide range of physiological processes, including cell signaling, inflammation, and neurodegeneration. Its unique ability to regulate protein degradation in a highly specific and targeted manner makes it an attractive target for drug development. In addition to its potential as a drug

Protein Name: ATP/GTP Binding Carboxypeptidase 1

Functions: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins (PubMed:22170066, PubMed:24022482, PubMed:30420557). Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin (PubMed:22170066, PubMed:24022482, PubMed:30420557). Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate (PubMed:24022482). Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of alpha-tubulin as well as non-tubulin proteins such as MYLK (PubMed:22170066). Involved in KLF4 deglutamylation which promotes KLF4 proteasome-mediated degradation, thereby negatively regulating cell pluripotency maintenance and embryogenesis (PubMed:29593216)

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•   expression level;
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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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