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In biochemistry, dephosphorylation is the removal of a phosphate (PO 3− 4) group from an organic compound by hydrolysis. It is a reversible post-translational modification . Dephosphorylation and its counterpart, phosphorylation , activate and deactivate enzymes by detaching or attaching phosphoric esters and anhydrides .
The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. [3] The amino acids most commonly phosphorylated are serine, threonine, tyrosine, and histidine.
This process and its inverse, dephosphorylation, are common in biology. [2] Protein phosphorylation often activates (or deactivates) many enzymes . [ 3 ] [ 4 ]
The tandem work of kinases and phosphatases constitute a significant element of the cell's regulatory network. [9] Phosphorylation (and dephosphorylation) is among the most common modes of posttranslational modification in proteins, and it is estimated that, at any given time, up to 30% of all proteins are phosphorylated.
Phosphorylation and dephosphorylation summary. A phosphorylation cascade is a sequence of signaling pathway events where one enzyme phosphorylates another, causing a chain reaction leading to the phosphorylation of thousands of proteins. This can be seen in signal transduction of hormone messages.
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In contrast, protein phosphatases (PPs) are the primary effectors of dephosphorylation and can be grouped into three main classes based on sequence, structure and catalytic function. The largest class of PPs is the phosphoprotein phosphatase (PPP) family comprising PP1, PP2A, PP2B, PP4, PP5, PP6 and PP7, and the protein phosphatase Mg 2+ - or ...