peptidyl-histidine dephosphorylation

Definition

Target type: biologicalprocess

The removal of phosphoric residues from peptidyl-O-phospho-L-histidine to form peptidyl-histidine. [GOC:BHF, GOC:vk, PMID:12383260]

Peptidyl-histidine dephosphorylation is a crucial enzymatic process involved in the regulation of cellular signaling pathways. It specifically targets histidine residues within proteins that have been phosphorylated, removing the phosphate group and reversing the effects of phosphorylation. This process is catalyzed by a family of enzymes known as histidine phosphatases, which exhibit diverse substrate specificities and regulatory mechanisms. The dephosphorylation of histidine residues plays a vital role in controlling a wide range of cellular functions, including: signal transduction, protein-protein interactions, enzyme activity, and gene expression. For instance, in signal transduction pathways, histidine dephosphorylation can terminate a signal by returning a signaling protein to its inactive state. Furthermore, it can modulate protein-protein interactions by altering the binding affinity between proteins. The dephosphorylation of histidine residues in enzymes can also regulate their catalytic activity, either activating or inhibiting their function. In the context of gene expression, histidine dephosphorylation can influence the activity of transcription factors, thus affecting gene transcription. Overall, peptidyl-histidine dephosphorylation is an essential enzymatic process that contributes to the precise control of cellular signaling and various biological functions.'
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Proteins (1)

Compounds (6)