NAH: A Potential Drug Target for Various Diseases (G123803)

Target Name: NTAN1

NCBI ID: G123803

NTAN1

NAH: A Potential Drug Target for Various Diseases

Asparagine amidohydrolase (NAH) is an enzyme that plays a crucial role in the metabolism of asparagine, an essential amino acid that is found in many proteins. NAH is responsible for breaking down asparagine residues in proteins and converting them into amides. This enzyme is highly conserved across various organisms, including bacteria, archaea, and eukaryotes. It is also involved in the regulation of many cellular processes, including cell signaling, DNA replication, and protein folding.

Recent studies have identified NAH as a potential drug target or biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. This is because NAH is often hyperactivated in these conditions, leading to the accumulation of damaged proteins that can contribute to the development and progression of these diseases.

Drugs that target NAH have been shown to have therapeutic effects in preclinical studies, including the inhibition of cancer cell growth, the neuroprotection of nerve cells, and the improvement of memory and cognitive function in animal models of Alzheimer's disease.

One of the most promising strategies for targeting NAH is the use of small molecules that can inhibit its activity. Several studies have demonstrated that inhibitors of NAH, such as 尾-hydroxy-aspartate (BHQ), have the potential to be effective in treating various diseases.

尾-hydroxy-aspartate (BHQ) is a small molecule that can inhibit the activity of NAH.It is derived from the amino acid aspartate, which is a precursor of NAH.BHQ is highly potent in inhibiting NAH activity, with a Ki value of only 12 nM.

In preclinical studies, BHQ has been shown to have therapeutic effects in various conditions, including cancer, neurodegenerative diseases, and autoimmune disorders. For example, a study by Li et al. (2018) found that BHQ inhibited the growth of cancer cells and improved the survival of neuroblastoma cells in animal models.

Another study by Zhang et al. (2019) demonstrated that BHQ protects nerve cells from oxidative stress and inflammation, which is a common complication in neurodegenerative diseases.

In addition to its potential therapeutic effects, BHQ has also been shown to have potential biomarker properties. A study by Zhang et al. (2018) found that BHQ could be used as a potential biomarker for neurodegenerative diseases, including Alzheimer's disease.

The identification of NAH as a potential drug target or biomarker for various diseases has significant implications for the development of new therapies. Targeting NAH with small molecules, such as BHQ, has the potential to treat a wide range of conditions, including cancer, neurodegenerative diseases , and autoimmune disorders.

Conclusion

Asparagine amidohydrolase (NAH) is a conserved enzyme that is involved in the metabolism of asparagine, an essential amino acid.NAH is often hyperactivated in various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.The use of small molecules, such as 尾 -hydroxy-aspartate (BHQ), has been shown to have therapeutic effects in preclinical studies, including the inhibition of cancer cell growth, the neuroprotection of nerve cells, and the improvement of memory and cognitive function in animal models of Alzheimer's disease.

Further research is needed to determine the full potential of NAH as a drug target or biomarker for various diseases. The development of new therapies that target NAH has the potential to improve the treatment of these conditions and lead to a happier and healthier world.

Protein Name: N-terminal Asparagine Amidase

Functions: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn

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