Target Name: SAT2
NCBI ID: G112483
Review Report on SAT2 Target / Biomarker Content of Review Report on SAT2 Target / Biomarker
SAT2
Other Name(s): diamine acetyltransferase 2 | spermidine/spermine N(1)-acetyltransferase 2 | Thialysine N-epsilon-acetyltransferase | SAT2_HUMAN | diamine N-acetyltransferase 2 | OTTHUMP00000135292 | SSAT-2 | Spermidine/spermine N1-acetyltransferase family member 2, transcript variant 3 | Thialysine N-epsilon-acetyltransferase (isoform 3) | Diamine N-acetyltransferase 2 | SSAT2 | polyamine N-acetyltransferase 2 | SAT2 variant 3 | Spermidine/spermine N(1)-acetyltransferase 2 | Spermidine/spermine-N1-acetyltransferase 2 | Spermidine/spermine N1-acetyltransferase 2 | Polyamine N-acetyltransferase 2 | spermidine/spermine N1-acetyltransferase family member 2

SAT2: A Key Enzyme in Aromatic Amino Acid Metabolism

SAT2 (Diamine Acetyltransferase 2) is a enzyme that plays a crucial role in the metabolism of aromatic amino acids, which are important building blocks of many drugs, including anti-cancer agents. Aromatic amino acids are modified by the acetyl group, which is added to the carbon atom of the amino acid via a complex biochemical pathway that involves the enzyme SAT2.

The SAT2 enzyme is a key player in this process, as it catalyzes the transfer of the acetyl group from the carbon atom of the aromatic amino acid to the carbon atom of another amino acid, such as Gly-4-carboxyl-Lys-7-aspartate (Glu-4-ASP). This modifies the aromatic amino acid and gives it a new function in the cell.

SAT2 is a protein that consists of 215 amino acids and has a calculated molecular mass of 33 kDa. It is a monomer and has a single transmembrane domain. The enzyme has a unique fold, with a distinct N-terminus and a C-terminus that is involved in the catalytic cycle.

The SAT2 enzyme is widely expressed in various tissues and cells, including the liver, lung, heart, kidney, and brain. It is also expressed in various cell lines, including human embryonic stem cells (ESCs) and human cancer cells. The enzyme is purified from various tissues and cells using techniques such as column chromatography and affinity purification.

SAT2 has been shown to play a critical role in the metabolism of many aromatic amino acids, including L-tryptophan, L-tyrosine, and L-histidine. These amino acids are important for the growth, development, and function of cells. For example, L-tryptophan is a key precursor of niacin, which is involved in the synthesis of many important compounds in the body, including neurotransmitters, antioxidants, and compounds involved in inflammation. L-tyrosine is a precursor of neurotransmitters, including dopamine and norepinephrine, which are involved in the transmission of signals in the brain. L-histidine is a histamine receptor antagonist and is involved in the regulation of inflammation and immune responses.

In addition to its role in the metabolism of aromatic amino acids, SAT2 has also been shown to play a critical role in the regulation of cellular processes. For example, the enzyme has been shown to play a role in the regulation of cell growth, as well as the regulation of cell death.

SAT2 has also been shown to have potential as a drug target in cancer therapy. For example, inhibition of the SAT2 enzyme has been shown to result in the inhibition of the growth of cancer cells. This is because the acetylation of aromatic amino acids, which is a critical step in the metabolism of these amino acids, is a critical step in the growth and development of cancer cells. By inhibiting the SAT2 enzyme, researchers have been able to inhibit the growth of cancer cells and potentially lead to a more effective cancer treatment.

In conclusion, SAT2 is a crucial enzyme in the metabolism of aromatic amino acids and has been shown to play a critical role in the regulation of cellular processes. Its potential as a drug target makes it an attractive target for the development of cancer therapies. Further research is needed to fully understand the role of SAT2 in the regulation of cellular processes and its potential as a drug target.

Protein Name: Spermidine/spermine N1-acetyltransferase Family Member 2

Functions: Catalyzes the N-acetylation of the amino acid thialysine (S-(2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene group substituted with a sulfur (PubMed:15283699). May also catalyze acetylation of polyamines, such as norspermidine, spermidine or spermine (PubMed:12803540). However, ability to acetylate polyamines is weak, suggesting that it does not act as a diamine acetyltransferase in vivo (PubMed:15283699)

The "SAT2 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 SAT2 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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