Dephosphorylation

The reversible phosphorylation-dephosphorylation reaction occurs in every physiological process, making proper function of protein phosphatases necessary for organism viability.

In 1955, Edwin Krebs and Edmond Fischer used radiolabeled ATP to determine that phosphate is added to the serine residue of phosphorylase to convert it from its b to a form via phosphorylation.

Finally, after purifying the phosphorylated form of the enzyme, phosphorylase a, from rabbit liver, ion exchange chromatography was used to identify phosphoprotein phosphatase I and II.

[5] Edwin Krebs and Edmond Fischer won the 1992 Nobel Prize in Physiology or Medicine for the discovery of reversible protein phosphorylation.

[6] Phosphorylation and dephosphorylation of hydroxyl groups belonging to neutral but polar amino acids such as serine, threonine, and tyrosine within specific target proteins is a fundamental part of the regulation of every physiologic process.

Phosphorylation of a protein produces many biochemical effects, such as changing its conformation to alter its binding to a specific ligand to increase or reduce its activity.

Phosphorylation and dephosphorylation can be used on all types of substrates, such as structural proteins, enzymes, membrane channels, signaling molecules, and other kinases and phosphatases.

[9] During the synthesis of proteins, polypeptide chains, which are created by ribosomes translating mRNA, must be processed before assuming a mature conformation.

The complex utilizes an enzyme to capture photons of light, providing the greater photosynthesis process with all of the electrons needed to produce ATP.

[13] Excessive dephosphorylation of the membrane ATPases and proton pumps in the gastrointestinal tract leads to higher secretory rates of caustic peptic acids.

In combination with Helicobacter pylori infection, peptic ulcer disease is caused by the elevated pH dephosphorylation elicits.

[17] Inhibition of proton pumps[14] significantly decreases the acidity of the gastrointestinal tract, reducing the symptoms of acid-related diseases.

[20] Alkaline phosphatases, which remove the phosphate group present at the 5′ terminus of a DNA molecule, are often sourced naturally, most commonly from calf intestine, and are abbreviated as CIP.

PTEN, a phosphatase.
Crystallographic structure of human phosphatase and tensin homolog (PTEN). The active site of the blue N-terminal phosphatase domain is shown in yellow. The C-terminal C2 domain is shown in red. [ 7 ]
The ancestral state reconstruction and cross-species orthologous alignment. a Ancestral state reconstruction for human Val129 (red arrow) based on the Maximum Parsimony (MP) method in MEGA11. b Regional alignment comprising the human Val129 site (black arrow above the alignment).