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  2. Phosphofructokinase - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase

    [2] [3] It is allosterically inhibited by ATP and allosterically activated by AMP, thus indicating the cell's energetic needs when it undergoes the glycolytic pathway. [4] PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha- (PFK1) and 4 beta ...

  3. Phosphofructokinase 1 - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase_1

    Phosphofructokinase-1 (PFK-1) is one of the most important regulatory enzymes (EC 2.7.1.11) of glycolysis. It is an allosteric enzyme made of 4 subunits and controlled by many activators and inhibitors .

  4. Phosphofructokinase 2 - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase_2

    PFK-2 is known as the "bifunctional enzyme" because of its notable structure: though both are located on one protein homodimer, its two domains act as independently functioning enzymes. [5] One terminus serves as a kinase domain (for PFK-2) while the other terminus acts as a phosphatase domain (FBPase-2). [6]

  5. Protein targeting - Wikipedia

    en.wikipedia.org/wiki/Protein_targeting

    Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations within or outside the cell. [1] [2] [note 1] Proteins can be targeted to the inner space of an organelle, different intracellular membranes, the plasma membrane, or to the exterior of the cell via secretion.

  6. Phosphofructokinase deficiency - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase_deficiency

    It is characterized as a deficiency in the Phosphofructokinase (PFK) enzyme throughout the body, including the skeletal muscles and red blood cells. Phosphofrucotkinase is an enzyme involved in the glycolytic process. The lack of PFK blocks the completion of the glycolytic pathway.

  7. 1-phosphofructokinase - Wikipedia

    en.wikipedia.org/wiki/1-phosphofructokinase

    In enzymology, 1-phosphofructokinase (EC 2.7.1.56) is an enzyme that catalyzes the chemical reaction. ATP + D-fructose 1-phosphate → ADP + D-fructose 1,6-bisphosphate. Thus, the two substrates of this enzyme are ATP and D-fructose 1-phosphate, whereas its two products are ADP and D-fructose 1,6-bisphosphate.

  8. PFKM - Wikipedia

    en.wikipedia.org/wiki/PFKM

    This 85-kDa protein is one of two subunit types that comprise the seven tetrameric PFK isozymes. [6] [7] The muscle isozyme is composed solely of PFKM.[6] [8] [9] The liver PFK (PFK-5) contains solely the second subunit type, PFKL, while the erythrocyte PFK includes five isozymes composed of different combinations of PFKM and PFKL.

  9. Binding site - Wikipedia

    en.wikipedia.org/wiki/Binding_site

    For example, phosphofructokinase (PFK), which phosphorylates fructose in glycolysis, is largely regulated by ATP. Its regulation in glycolysis is imperative because it is the committing and rate limiting step of the pathway. PFK also controls the amount of glucose designated to form ATP through the catabolic pathway. Therefore, at sufficient ...