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  2. Dephosphorylation - Wikipedia

    en.wikipedia.org/wiki/Dephosphorylation

    The reversible phosphorylation-dephosphorylation reaction occurs in every physiological process, making proper function of protein phosphatases necessary for organism viability. Because protein dephosphorylation is a key process involved in cell signalling , [ 1 ] protein phosphatases are implicated in conditions such as cardiac disease ...

  3. Phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Phosphorylation

    Serine in an amino acid chain, before and after phosphorylation. In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. [1] This process and its inverse, dephosphorylation, are common in biology. [2] Protein phosphorylation often activates (or deactivates) many enzymes. [3] [4]

  4. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its function. [1] Approximately 13,000 human proteins have sites that are phosphorylated. [2] The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein ...

  5. Chemical modification - Wikipedia

    en.wikipedia.org/wiki/Chemical_modification

    Phosphorylation occurs when a PO 3 (phosphoryl) group is added to a protein. [3] This chemical modification is the most extensively studied and is reversible. The result of those studies has shown that phosphorylation acts as a regulator for proteins in two ways: the addition or removal of phosphoryl group can impact enzyme kinetics by turning on or off the enzymatic function via ...

  6. Phosphomimetics - Wikipedia

    en.wikipedia.org/wiki/Phosphomimetics

    In a laboratory setting, the use of recombinant proteins to artificially introduce phosphomimetics is a common tool for studying phosphorylation and protein activation. For example, the IRF3 protein must be phosphorylated for its normal activity (transcription of its target genes, like IFNβ ), but when serine amino acid residues were mutated ...

  7. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    [1] In biochemistry, a kinase (/ ˈ k aɪ n eɪ s, ˈ k ɪ n eɪ s,-eɪ z /) [2] is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the high-energy ATP molecule donates a phosphate group to the substrate molecule.

  8. Protein phosphatase - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphatase

    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 Mn 2+-dependent (PPM) family, composed primarily of PP2C. The protein Tyr phosphatase (PTP) super-family forms the second group, [1] and the aspartate-based protein phosphatases the ...

  9. Glycolysis - Wikipedia

    en.wikipedia.org/wiki/Glycolysis

    d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...