triphosphohydrolases

Triphosphohydrolases are a class of enzymes that catalyze the hydrolysis of phosphate bonds within triphosphorylated molecules. Their primary function is to remove terminal phosphate groups from nucleoside triphosphates, diphosphates, and other similar compounds. This enzymatic activity releases inorganic phosphate and a less phosphorylated molecule, often serving as a crucial step in energy metabolism or signal transduction pathways. The reaction typically involves the addition of water across a phosphoanhydride bond, leading to its cleavage. The specific substrates for triphosphohydrolases can vary widely, with some enzymes exhibiting broad specificity while others are highly selective for particular triphosphorylated compounds. This enzymatic class plays a vital role in regulating the intracellular concentrations of activated nucleotides and their breakdown products, thereby influencing a multitude of cellular processes. Dysfunction of triphosphohydrolases has been implicated in various diseases, highlighting their importance in maintaining cellular homeostasis. Examples of molecules that can be substrates for triphosphohydrolases include adenosine triphosphate (ATP), guanosine triphosphate (GTP), and cyclic adenosine monophosphate (cAMP), although the specific enzymes involved in their hydrolysis differ.