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  2. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    This kinase uses an ATP molecule to supply the phosphate to thymidine, as shown below. This transfer of a phosphate from one nucleotide to another by thymidine kinase, as well as other nucleoside and nucleotide kinases, functions to help control the level of each of the different nucleotides. Overall reaction catalysed by thymidine kinase.

  3. Protein kinase - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase

    A protein kinase is a kinase which selectively modifies other proteins by covalently adding phosphates to them (phosphorylation) as opposed to kinases which modify lipids, carbohydrates, or other molecules.

  4. Tyrosine kinase - Wikipedia

    en.wikipedia.org/wiki/Tyrosine_kinase

    Protein tyrosine kinase plays a role in this task, too. A protein tyrosine kinase called pp125, also referred to as focal adhesion kinase (FAK) is likely at hand in the influence of cellular focal adhesions, as indicated by an immunofluorescent localization of FAK. Focal adhesions are macromolecular structures that function in the transmission ...

  5. 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 ...

  6. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    Phosphorylation of the enzyme GSK-3 by AKT (Protein kinase B) as part of the insulin signaling pathway. [31] Phosphorylation of src (pronounced "sarc") tyrosine kinase by C-terminal Src kinase (Csk) induces a conformational change in the enzyme, resulting in a fold in the structure, which masks its kinase domain, and is thus shut "off". [32]

  7. Adenylate kinase - Wikipedia

    en.wikipedia.org/wiki/Adenylate_kinase

    Adenylate kinase (EC 2.7.4.3) (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of the various adenosine phosphates (ATP, ADP, and AMP). By constantly monitoring phosphate nucleotide levels inside the cell, ADK plays an important role in cellular energy homeostasis .

  8. Pyruvate kinase - Wikipedia

    en.wikipedia.org/wiki/Pyruvate_kinase

    The reaction catalyzed by pyruvate kinase is the final step of glycolysis. It is one of three rate-limiting steps of this pathway. Rate-limiting steps are the slower, regulated steps of a pathway and thus determine the overall rate of the pathway.

  9. Phosphofructokinase - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase

    The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. [1] Phosphofructokinase catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway.