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  2. Dephosphorylation - Wikipedia

    en.wikipedia.org/wiki/Dephosphorylation

    Phosphorylation and dephosphorylation of hydroxyl groups belonging to neutral but polar amino acids such as serine, threonine, and tyrosine within specific target proteins is a fundamental part of the regulation of every physiologic process. Phosphorylation involves the covalent modification of the hydroxyl with a phosphate group through the ...

  3. Phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Phosphorylation

    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]

  4. Photophosphorylation - Wikipedia

    en.wikipedia.org/wiki/Photophosphorylation

    This word is taken from two Greek words, photos, which means light, and synthesis, which in chemistry means making a substance by combining simpler substances. So, in the presence of light, synthesis of food is called 'photosynthesis'. Noncyclic photophosphorylation through light-dependent reactions of photosynthesis at the thylakoid membrane.

  5. Light-dependent reactions - Wikipedia

    en.wikipedia.org/wiki/Light-dependent_reactions

    Light-dependent reactions of photosynthesis at the thylakoid membrane. Light-dependent reactions are certain photochemical reactions involved in photosynthesis, the main process by which plants acquire energy. There are two light dependent reactions: the first occurs at photosystem II (PSII) and the second occurs at photosystem I (PSI).

  6. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    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 ...

  7. Phosphatome - Wikipedia

    en.wikipedia.org/wiki/Phosphatome

    Most phosphorylation sites are not linked to a specific phosphatase, so the phosphatome approach allows a global analysis of dephosphorylation, screening to find the phosphatase responsible for a given reaction, and comparative studies between different phosphatases, similar to how protein kinase research has been impacted by the kinome approach.

  8. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    Conversely, it is referred to as dephosphorylation when the phosphorylated substrate donates a phosphate group and ADP gains a phosphate group (producing a dephosphorylated substrate and the high energy molecule of ATP). These two processes, phosphorylation and dephosphorylation, occur four times during glycolysis. [3] [4] [5]

  9. Adenosine diphosphate - Wikipedia

    en.wikipedia.org/wiki/Adenosine_diphosphate

    ADP and phosphate are needed as precursors to synthesize ATP in the payoff reactions of the TCA cycle and oxidative phosphorylation mechanism. [4] During the payoff phase of glycolysis, the enzymes phosphoglycerate kinase and pyruvate kinase facilitate the addition of a phosphate group to ADP by way of substrate-level phosphorylation .