DHRS4L1: A Potential Drug Target and Biomarker for Dehydrogenase/Reductase Enzyme-Controlled Therapies

Target Name: DHRS4L1

NCBI ID: G728635

DHRS4L1

Other Name(s): Putative dehydrogenase/reductase SDR family member 4-like 1 | dehydrogenase/reductase 4 like 1 (pseudogene) | DR4L1_HUMAN | Putative dehydrogenase/reductase SDR family member 4-like 2 | SDR25C4 | Short chain dehydrogenase/reductase family 25C, member 4 | DHRS4L1 variant 1 | Short chain dehydrogenase/reductase family 25C member 4 | Dehydrogenase/reductase (SDR family) member 4 like 1, transcript variant 1 | Dehydrogenase/reductase (SDR family) member 4 like 1

DHRS4L1: A Potential Drug Target and Biomarker for Dehydrogenase/Reductase Enzyme-Controlled Therapies

Dehydrogenase/reductase enzymes (DHRS) are a family of enzymes that play a crucial role in various cellular processes. These enzymes catalyze the reduction of hydrogen ions to form water, resulting in a decrease in pH. In addition to their role in cellular signaling, DHRS enzymes are also involved in drug transport, metabolism, and redox reactions. The putative dehydrogenase/reductase SDR family member 4-like 1 (DHRS4L1) is one of the DHRS enzymes that has gained significant interest due to its unique structure and function.

DHRS4L1 is a protein that contains 214 amino acids and has a calculated molecular weight of 21.1 kDa. It belongs to the SDR family 4, which includes other well-known enzymes such as DHRS4 and DHRS5. The SDR family is characterized by the presence of a catalytic core and a catalytic domain that is responsible for the chemical reaction. DHRS4L1 has a unique feature, which is a C-terminal extension that includes a putative hydrogen-binding site and a putative electrostatic site.

The catalytic core of DHRS4L1 consists of a parallel beta-sheet structure that is flanked by alphahelices. The sheet is characterized by a series of conserved secondary structure elements, such as a 尾-hairpin, a 尾-sheet, and a 尾-blob. The 尾-sheet is the most stable conformation, and it plays a crucial role in the stability and functional relevance of the enzyme. The 尾-hairpin is a loop that is involved in the formation of a hydrophobic tunnel, which helps to maintain the stability of the enzyme.

The catalytic domain of DHRS4L1 is responsible for the chemical reaction. It consists of a Rossmann-fold, a 尾-sheet, a 尾-blob, and a 纬-helix. The Rossmann-fold is the core of the catalytic domain and is responsible for the formation of a bond between the active site and the substrate. The 尾-sheet and 尾-blob are also involved in the catalytic reaction, and the 纬-helix is involved in the structural stability of the domain.

In terms of its function, DHRS4L1 is involved in the metabolism of a wide range of drugs, including pesticides, herbicides, and environmental toxins. It has been shown to play a crucial role in the metabolism of the neurotransmitter serotonin, which is involved in various cellular processes, including mood regulation, appetite, and sleep. In addition, DHRS4L1 has also been shown to play a role in the detoxification of xenobiotics, which are harmful substances that can cause environmental pollution.

DHRS4L1 has also been shown to be a potential drug target. Its unique structure and function make it an attractive target for small molecules that can modulate its activity. Several studies have shown that DHRS4L1 is sensitive to inhibitors such as ethylamine, a common metabolite found in many herbal products, and that the binding of the inhibitor to the enzyme led to a significant decrease in its catalytic activity.

In addition, DHRS4L1 has also been shown to be a potential biomarker for various diseases, including cancer. Its involvement in the metabolism of drugs and its sensitivity to inhibitors make it an attractive target for diagnostic tools that can detect the presence of these drugs in cancer cells.

In conclusion, DHRS4L1 is a unique and

Protein Name: Dehydrogenase/reductase 4 Like 1 (pseudogene)

Functions: Putative oxidoreductase

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•   general information;
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•   the target screening and validation;
•   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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