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Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its ...
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.
Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. [1] There are two main types of protein kinase.
Phosphorylation of glucose is imperative in processes within the body. For example, phosphorylating glucose is necessary for insulin-dependent mechanistic target of rapamycin pathway activity within the heart. This further suggests a link between intermediary metabolism and cardiac growth. [13]
Pyruvate kinase is the enzyme involved in the last step of glycolysis.It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), yielding one molecule of pyruvate and one molecule of ATP. [1]
Mutations in the genes encoding them or their potential activators or repressors can affect any number of functions within an organism. [3] [4] Phosphorylation is easily reversed by phosphatases. Therefore, it is an effective method of turning 'on' and 'off' kinase activity. Because of this it is recognized as an essential process in cell ...
MAP kinase not only plays an important function during growth of cell in the M phase phosphorylation cascade but also plays an important role during the sequence of signaling pathway. [2] In order to regulate its functions so it does not cause chaos, it can only be active when both tyrosine and threonine/serine residues are phosphorylated. [3]
Phosphorylation of selected tyrosine sites on receptor substrates is known to activate different pathways leading to increased glucose uptake, lipogenesis, and glycogen and protein synthesis, as well as to the stimulation of cell growth. In addition to the activation of these pathways by tyrosine phosphorylation, several mechanisms of ...