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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 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]
The kinase domain is vital for JAK activity, since it allows JAKs to phosphorylate (add phosphate groups to) proteins. There are seven STAT proteins: STAT1, STAT2, STAT3, STAT4, STAT5A, STAT5B and STAT6. [1] STAT proteins contain many different domains, each with a different function, of which the most conserved region is the SH2 domain. [2]
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 ...
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.
Phosphorylation is a key reversible modification that regulates protein function, subcellular localization, complex formation, degradation of proteins and therefore cell signaling networks. With all of these modification results, it is estimated that between 30–65% of all proteins may be phosphorylated, some multiple times.
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]
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]