AGTPase

AGTPase refers to a class of enzymes that catalyze the hydrolysis of guanosine triphosphate (GTP). These enzymes play crucial roles in various cellular processes, including signal transduction, protein synthesis, and cell motility. The hydrolysis of GTP to guanosine diphosphate (GDP) releases energy that is utilized by the protein to perform its function.

Many AGTPases are part of the large GTPase superfamily, which are characterized by their ability to bind and hydrolyze GTP. These proteins typically possess a conserved GTP-binding motif and a catalytic site. Their activity is often regulated by accessory proteins such as guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). GEFs promote the binding of GTP, thereby activating the GTPase, while GAPs stimulate GTP hydrolysis, leading to inactivation.

Examples of AGTPases include Ras, Rho, and Rab proteins, which are involved in cell growth, cytoskeleton organization, and intracellular trafficking, respectively. Other AGTPases are involved in ribosome function, protein folding, and DNA replication. The precise mechanism and cellular context of AGTPase activity vary widely depending on the specific enzyme and its associated protein partners. Dysregulation of AGTPase function has been implicated in various diseases, including cancer and neurological disorders.