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  2. Phosphorylase kinase - Wikipedia

    en.wikipedia.org/wiki/Phosphorylase_kinase

    Phosphorylase kinase was the first protein kinase to be isolated and characterized in detail, accomplished first by Krebs, Graves and Fischer in the 1950s. [ 3 ] [ 4 ] [ 5 ] At the time, the scientific community was largely unaware of the importance of protein phosphorylation in the regulation of cellular processes, and many in the field ...

  3. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    [citation needed] In 1956, Edmond H. Fischer and Edwin G. Krebs discovered that the interconversion between phosphorylase a and phosphorylase b was mediated by phosphorylation and dephosphorylation. [11] The kinase that transferred a phosphoryl group to Phosphorylase b, converting it to Phosphorylase a, was named Phosphorylase Kinase.

  4. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    It was found that an enzyme, named phosphorylase kinase and Mg-ATP were required to phosphorylate glycogen phosphorylase by assisting in the transfer of the γ-phosphoryl group of ATP to a serine residue on phosphorylase b. Protein phosphatase 1 is able to catalyze the dephosphorylation of phosphorylated enzymes by removing the phosphate group.

  5. Phosphorylase - Wikipedia

    en.wikipedia.org/wiki/Phosphorylase

    Phosphorylase a is the more active R form of glycogen phosphorylase that is derived from the phosphorylation of the less active R form, phosphorylase b with associated AMP. The inactive T form is either phosphorylated by phosphoylase kinase and inhibited by glucose, or dephosphorylated by phosphoprotein phosphatase with inhibition by ATP and/or ...

  6. Protein kinase - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase

    Above is a ball-and-stick model of the inorganic phosphate molecule (H PO 4 2−).Colour coding: P (orange); O (red); H (white). The chemical activity of a protein kinase involves removing a phosphate group from ATP and covalently attaching it to one of three amino acids that have a free hydroxyl group.

  7. PRKACA - Wikipedia

    en.wikipedia.org/wiki/PRKACA

    Edmond H. Fischer and Edwin G. Krebs at the University of Washington discovered PKA in the late 1950s while working through the mechanisms that govern glycogen phosphorylase. They realized that a key metabolic enzyme called phosphorylase kinase was activated by another kinase that was dependent on the second messenger cyclic AMP (cAMP). [9]

  8. Protein kinase A - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase_A

    In cell biology, protein kinase A (PKA) is a family of serine-threonine kinase [1] whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (EC 2.7.11.11). PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism.

  9. Glycogen phosphorylase - Wikipedia

    en.wikipedia.org/wiki/Glycogen_phosphorylase

    Glycogen phosphorylase kinase activates glycogen phosphorylase in the same manner mentioned previously. Glycogen phosphorylase b is not always inactive in muscle, as it can be activated allosterically by AMP. [6] [9] An increase in AMP concentration, which occurs during strenuous exercise, signals energy demand. AMP activates glycogen ...