Exploring the Structural and Functional Significance of Aspartate Transcarbamoylase Bound to CTP,See the following pdb files for Aspartate transcarbamoylase bound to CTP (PDB

Exploring the Structural and Functional Significance of Aspartate Transcarbamoylase Bound to CTP

Aspartate transcarbamoylase (ATCase) is a key enzyme in the pyrimidine biosynthetic pathway, catalyzing the condensation of carbamoyl phosphate and aspartate (1). Aspartate transcarbamoylase bound to CTP (ATCase-CTP) plays a critical role in regulating the pyrimidine biosynthetic pathway, and has been studied extensively in recent years. Several structural and functional studies have been conducted to explore the structural and functional significance of ATCase-CTP. In 2016, a study was conducted to investigate the binding mechanism of ATCase-CTP using X-ray crystallography (2). The results of the study showed that the structure of ATCase-CTP was stabilized by hydrogen bonds and hydrophobic interactions. Additionally, the study showed that CTP-binding induced conformational changes in ATCase, which was critical for stabilizing the active site of the enzyme. More recently, a study was conducted in 2020 to investigate the structural and functional roles of ATCase-CTP in the catalytic cycle (3). The results of the study demonstrated that binding of CTP to ATCase increased the affinity of the enzyme for its substrates, leading to increased catalytic efficiency. Additionally, the study showed that CTP-binding induced conformational changes in ATCase, which were essential for stabilizing the active site and improving the efficiency of the catalytic cycle. Cont……