IDP phosphatase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: IDP + H2O = IMP + H+ + phosphate. [PMID:20385596, PMID:22849572, RHEA:35207]

IDP phosphatase activity is a catalytic activity that removes a phosphate group from an inositol polyphosphate (IP) molecule. Inositol polyphosphates are important signaling molecules that play a role in a variety of cellular processes, including cell growth, differentiation, and apoptosis. IDP phosphatases are involved in the regulation of these processes by controlling the levels of IP in the cell. The reaction catalyzed by IDP phosphatases is:

Inositol polyphosphate + H2O --u003e Inositol polyphosphate (dephosphorylated) + Pi

The specific substrate of an IDP phosphatase can vary, but the general mechanism of action is the same. The enzyme binds to the IP molecule and then removes the phosphate group from the molecule. This results in the production of a dephosphorylated IP molecule and inorganic phosphate (Pi).

IDP phosphatases are often found in the cytoplasm of cells, but they can also be located in the nucleus and other organelles. They are typically regulated by a variety of factors, including the levels of IP in the cell, the presence of specific cofactors, and the phosphorylation state of the enzyme itself.

Mutations in genes encoding IDP phosphatases can lead to a variety of diseases. For example, mutations in the gene encoding the enzyme inositol polyphosphate 5-phosphatase (INPP5) have been linked to X-linked intellectual disability. Mutations in the gene encoding the enzyme inositol polyphosphate 4-phosphatase (INPP4) have been linked to epilepsy.'
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Proteins (3)

Compounds (3)