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  2. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    An enzyme inhibitor is a molecule that binds to an enzyme and blocks its activity. Enzymes are proteins that speed up chemical reactions necessary for life, in which substrate molecules are converted into products. [1] An enzyme facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the ...

  3. Competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Competitive_inhibition

    Once the inhibitor is bound to the enzyme, the slope will be affected, as the K m either increases or decreases from the original K m of the reaction. [4] [5] [6] Most competitive inhibitors function by binding reversibly to the active site of the enzyme. [1] As a result, many sources state that this is the defining feature of competitive ...

  4. CYP3A4 - Wikipedia

    en.wikipedia.org/wiki/CYP3A4

    CYP3A4. Cytochrome P450 3A4 (abbreviated CYP3A4) (EC 1.14.13.97) is an important enzyme in the body, mainly found in the liver and in the intestine, which in humans is encoded by CYP3A4 gene. It oxidizes small foreign organic molecules (xenobiotics), such as toxins or drugs, so that they can be removed from the body.

  5. β-Lactamase inhibitor - Wikipedia

    en.wikipedia.org/wiki/Β-Lactamase_inhibitor

    β-Lactamase inhibitor. Beta-lactamases are a family of enzymes involved in bacterial resistance to beta-lactam antibiotics. In bacterial resistance to beta-lactam antibiotics, the bacteria have beta-lactamase which degrade the beta-lactam rings, rendering the antibiotic ineffective. However, with beta-lactamase inhibitors, these enzymes on the ...

  6. 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 ...

  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. CYP2C9 - Wikipedia

    en.wikipedia.org/wiki/CYP2C9

    CYP2C9. Cytochrome P450 family 2 subfamily C member 9 (abbreviated CYP2C9) is an enzyme protein. The enzyme is involved in the metabolism, by oxidation, of both xenobiotics, including drugs, and endogenous compounds, including fatty acids. In humans, the protein is encoded by the CYP2C9 gene. [5][6] The gene is highly polymorphic, which affects ...

  9. Protease inhibitor (pharmacology) - Wikipedia

    en.wikipedia.org/wiki/Protease_inhibitor...

    Protease inhibitors (PIs) are medications that act by interfering with enzymes that cleave proteins. Some of the most well known are antiviral drugs widely used to treat HIV/AIDS, hepatitis C and COVID-19. These protease inhibitors prevent viral replication by selectively binding to viral proteases (e.g. HIV-1 protease) and blocking proteolytic ...

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