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  2. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, [1]: 19 it is the most important part as it directly catalyzes the chemical ...

  3. Competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Competitive_inhibition

    The active site is a region on an enzyme to which a particular protein or substrate can bind. The active site will thus only allow one of the two complexes to bind to the site, either allowing a reaction to occur or yielding it. In competitive inhibition, the inhibitor resembles the substrate, taking its place and binding to the active site of ...

  4. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    A catalytic triad is a set of three coordinated amino acids that can be found in the active site of some enzymes. [1][2] Catalytic triads are most commonly found in hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases).

  5. Activation energy - Wikipedia

    en.wikipedia.org/wiki/Activation_energy

    This is possible due to a release of energy that occurs when the substrate binds to the active site of a catalyst. This energy is known as Binding Energy. Upon binding to a catalyst, substrates partake in numerous stabilizing forces while within the active site (e.g. hydrogen bonding or van der Waals forces). Specific and favorable bonding ...

  6. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    Allosteric regulation. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.

  7. Serine protease - Wikipedia

    en.wikipedia.org/wiki/Serine_protease

    proteins. Crystal structure of Trypsin, a typical serine protease. Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. [1] They are found ubiquitously in both eukaryotes and prokaryotes.

  8. Activity diagram - Wikipedia

    en.wikipedia.org/wiki/Activity_diagram

    Activity diagrams [1] are graphical representations of workflows of stepwise activities and actions [2] with support for choice, iteration, and concurrency. In the Unified Modeling Language, activity diagrams are intended to model both computational and organizational processes (i.e., workflows), as well as the data flows intersecting with the related activities.

  9. Pyruvate decarboxylase - Wikipedia

    en.wikipedia.org/wiki/Pyruvate_decarboxylase

    proteins. Pyruvate decarboxylase is an enzyme (EC 4.1.1.1) that catalyses the decarboxylation of pyruvic acid to acetaldehyde. It is also called 2-oxo-acid carboxylase, alpha-ketoacid carboxylase, and pyruvic decarboxylase. [1] In anaerobic conditions, this enzyme participates in the fermentation process that occurs in yeast, especially of the ...