PSAT1P3: A Potential Drug Target and Biomarker for Phosphoserine Aminotransferase 1

Target Name: PSAT1P3

NCBI ID: G729779

PSAT1P3

Other Name(s): Phosphoserine aminotransferase 1 pseudogene 3 | phosphoserine aminotransferase 1 pseudogene 3

PSAT1P3: A Potential Drug Target and Biomarker for Phosphoserine Aminotransferase 1

Phosphoserine aminotransferase 1 (PSAT1) is a enzyme located in the mitochondria that plays a crucial role in the regulation of cellular energy metabolism. The primary function of PSAT1 is to convert phosphatidylserine (PS) to phosphoserine (PSER) by transferring a phosphate group from a serine residue to a phosphate group. This reaction is essential for the proper functioning of mitochondria, as it enables the production of ATP, the primary source of cellular energy, and is critical for the maintenance of cellular homeostasis.

PSAT1 is a pseudogene, which means that it was once a functional gene but has lost its function over time due to genetic mutations. The loss of function of PSAT1 can lead to various cellular and mitochondrial disorders, including Charcot-Marie-Toitsson disease (CMT), a progressive muscle wasting disease caused by a deficiency of dystrophin.

PSAT1 has been identified as a potential drug target and biomarker due to its unique structure and its involvement in the regulation of cellular energy metabolism. In this article, we will discuss the PSAT1 protein, its function, its loss of function in Charcot-Marie-Toitsson disease, and its potential as a drug target and biomarker.

Structure and Function of PSAT1

PSAT1 is a 21-kDa protein that contains 116 amino acid residues. It has a molecular weight of 19,416 Da and a calculated pI of 9.95. PSAT1 is localized to the mitochondria and is primarily expressed in the cytoplasm. The protein is composed of two distinct domains: an N-terminal transmembrane domain and a C-terminal cytoplasmic domain.

The N-terminal transmembrane domain of PSAT1 consists of a single amino acid residue at position 2, which is a highly conserved glycine residue. This domain is responsible for the formation of the protein's transmembrane region and is involved in the regulation of the protein's stability and its interaction with other cellular components.

The C-terminal cytoplasmic domain of PSAT1 is responsible for the protein's cytoplasmic activity. It consists of a series of conserved amino acid residues that form a distinct subdomain that is involved in the regulation of PSAT1's catalytic activity.

Function of PSAT1

PSAT1 is involved in the regulation of cellular energy metabolism by participating in the citric acid cycle. In the citric acid cycle, PSAT1 is responsible for the conversion of phosphatidylserine (PS) to phosphoserine (PSER), which is the final step in the cycle and is critical for the production of ATP.

PSAT1 is also involved in the regulation of mitochondrial dynamics and in the control of cellular homeostasis. For instance, PSAT1 plays a role in the regulation of mitochondrial fission and fusion, as well as in the regulation of mitochondrial size and dynamics.

Loss of Function in Charcot-Marie-Toitsson Disease

Charcot-Marie-Toitsson disease (CMT) is a progressive muscle wasting disease caused by a deficiency of dystrophin, a protein that helps maintain muscle mass and function. The defect in dystrophin leads to muscle weakness and wasting, which can progress to the loss of muscle mass and eventually to death.

PSAT1 is involved in

Protein Name: Phosphoserine Aminotransferase 1 Pseudogene 3

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