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  2. 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 ...

  3. Phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Phosphorylation

    [9] [10] Liver cells are freely permeable to glucose, and the initial rate of phosphorylation of glucose is the rate-limiting step in glucose metabolism by the liver. [ 9 ] The liver's crucial role in controlling blood sugar concentrations by breaking down glucose into carbon dioxide and glycogen is characterized by the negative Gibbs free ...

  4. Protein kinase domain - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase_domain

    The protein kinase domain is a structurally conserved protein domain containing the catalytic function of protein kinases. [2] [3] [4] Protein kinases are a group of enzymes that move a phosphate group onto proteins, in a process called phosphorylation. This functions as an on/off switch for many cellular processes, including metabolism ...

  5. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    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.

  6. Protein kinase - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase

    Deregulated kinase activity is a frequent cause of disease, in particular cancer, wherein kinases regulate many aspects that control cell growth, movement and death. Drugs that inhibit specific kinases are being developed to treat several diseases, and some are currently in clinical use, including Gleevec ( imatinib ) and Iressa ( gefitinib ).

  7. Cyclin-dependent kinase - Wikipedia

    en.wikipedia.org/wiki/Cyclin-dependent_kinase

    During G1, high levels of CKIs prevent cell cycle events from occurring out of order, but do not prevent transition through the Start checkpoint, which is initiated through G1/S-CDKs. Once the cell cycle is initiated, phosphorylation by early G1/S-CDKs leads to destruction of CKIs, relieving inhibition on later cell cycle transitions. [4]

  8. Protein phosphatase - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphatase

    Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification , with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred ...

  9. Tyrosine phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Tyrosine_phosphorylation

    Cartoon representation of the molecular structure of protein domain: p56 lck tyrosine kinase. Tyrosine phosphorylation is the addition of a phosphate (PO 4 3−) group to the amino acid tyrosine on a protein. It is one of the main types of protein phosphorylation. This transfer is made possible through enzymes called tyrosine kinases. Tyrosine ...