bis(5'-adenosyl)-triphosphatase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: P(1),P(3)-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP + 2 H+. [EC:3.6.1.29, RHEA:13893]

Bis(5'-adenosyl)-triphosphatase activity is a molecular function that refers to the enzymatic cleavage of a bis(5'-adenosyl)-triphosphate (AppppA) molecule into two molecules of adenosine 5'-diphosphate (ADP). AppppA, also known as diadenosine tetraphosphate, is a dinucleotide that plays a role in various cellular processes, including signal transduction, gene expression, and cell cycle regulation.

The bis(5'-adenosyl)-triphosphatase enzyme catalyzes the hydrolysis of the phosphoanhydride bond between the beta and gamma phosphates of AppppA, resulting in the release of two ADP molecules. This enzymatic reaction is typically specific for AppppA and does not involve other dinucleotides or triphosphates.

Bis(5'-adenosyl)-triphosphatase activity is important for maintaining cellular homeostasis by controlling the levels of AppppA. Elevated levels of AppppA can interfere with normal cellular processes, while depletion of AppppA can lead to dysfunction. The enzyme's ability to hydrolyze AppppA effectively regulates its cellular concentration, ensuring proper cellular function.

The bis(5'-adenosyl)-triphosphatase enzyme can be found in various organisms, including bacteria, yeast, plants, and animals. It is often associated with specific cellular compartments, such as the cytoplasm or the nucleus, depending on the organism and its specific function.

In summary, bis(5'-adenosyl)-triphosphatase activity is a crucial enzymatic function that maintains cellular homeostasis by hydrolyzing AppppA into two ADP molecules. This activity ensures proper cellular function by regulating AppppA levels and preventing potential disruptions in cellular processes.'
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Proteins (3)

Compounds (5)