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  2. Fructose 1,6-bisphosphatase - Wikipedia

    en.wikipedia.org/wiki/Fructose_1,6-bisphosphatase

    Fructose 1,6-bisphosphate aldolase is another temperature dependent enzyme that plays an important role in the regulation of glycolysis and gluconeogenesis during hibernation. [14] Its main role is in glycolysis instead of gluconeogenesis, but its substrate is the same as FBPase's, so its activity affects that of FBPase in gluconeogenesis.

  3. Linear biochemical pathway - Wikipedia

    en.wikipedia.org/wiki/Linear_biochemical_pathway

    Linear pathways follow a step-by-step sequence, where each enzymatic reaction results in the transformation of a substrate into an intermediate product. This intermediate is processed by subsequent enzymes until the final product is synthesized. A linear chain of four enzyme-catalyzed steps. A linear pathway can be studied in various ways.

  4. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Daniel Koshland's theory of enzyme-substrate binding is that the active site and the binding portion of the substrate are not exactly complementary. [10] The induced fit model is a development of the lock-and-key model and assumes that an active site is flexible and changes shape until the substrate is completely bound.

  5. Substrate (chemistry) - Wikipedia

    en.wikipedia.org/wiki/Substrate_(chemistry)

    Enzymes catalyze chemical reactions involving the substrate(s). In the case of a single substrate, the substrate bonds with the enzyme active site, and an enzyme-substrate complex is formed. The substrate is transformed into one or more products, which are then released from the active site. The active site is then free to accept another ...

  6. Firefly luciferase - Wikipedia

    en.wikipedia.org/wiki/Firefly_luciferase

    During a reaction, luciferase has a conformational change and goes into a "closed" form with the two domains coming together to enclose the substrate. This ensures that water is excluded from the reaction and does not hydrolyze ATP or the electronically excited product. [5] Diagram of the secondary structure of firefly luciferase.

  7. Glutamine synthetase - Wikipedia

    en.wikipedia.org/wiki/Glutamine_synthetase

    Glutamate is another product of glutamine metabolism; however, glutamate is a substrate for GS inhibiting it to act as a regulator to GS.2 Each inhibitor can reduce the activity of the enzyme; once all final glutamine metabolites are bound to GS, the activity of GS is almost completely inhibited. [8]

  8. Metabolic pathway - Wikipedia

    en.wikipedia.org/wiki/Metabolic_pathway

    The reactants, products, and intermediates of an enzymatic reaction are known as metabolites, which are modified by a sequence of chemical reactions catalyzed by enzymes. [1]: 26 In most cases of a metabolic pathway, the product of one enzyme acts as the substrate for the next. However, side products are considered waste and removed from the cell.

  9. Enzyme activator - Wikipedia

    en.wikipedia.org/wiki/Enzyme_activator

    Hexokinase-I (HK-I) is an enzyme activator because it draws glucose into the glycolysis pathway. Its function is to phosphorylate glucose releasing glucose-6-phosphate (G6P) as the product. HK-I not only signals the activation of glucose into glycolysis but also maintains a low glucose concentration to facilitate glucose diffusion into the cell.