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  2. Anti-inflammatory - Wikipedia

    en.wikipedia.org/wiki/Anti-inflammatory

    Nonsteroidal anti-inflammatory drugs (NSAIDs) alleviate pain by counteracting the cyclooxygenase (COX) enzyme. [1] On its own, COX enzyme synthesizes prostaglandins, creating inflammation. In whole, the NSAIDs prevent the prostaglandins from ever being synthesized, reducing or eliminating the inflammation and resulting pain. [citation needed]

  3. Alcohol dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Alcohol_dehydrogenase

    Crystal structures indicate that the His-51 deprotonates the nicotinamide ribose, which deprotonates Ser-48. Finally, Ser-48 deprotonates the alcohol, making it an aldehyde. [27] From a mechanistic perspective, if the enzyme adds hydride to the re face of NAD +, the resulting hydrogen is incorporated into the pro-R position. Enzymes that add ...

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    [1]: 8.1.1 For example, flavin and heme cofactors are often involved in redox reactions. [1]: 17 Enzymes that require a cofactor but do not have one bound are called apoenzymes or apoproteins. An enzyme together with the cofactor(s) required for activity is called a holoenzyme (or haloenzyme).

  5. Protein acetylation - Wikipedia

    en.wikipedia.org/wiki/Protein_acetylation

    Protein acetylation (and deacetylation) are acetylation reactions that occur within living cells as drug metabolism, by enzymes in the liver and other organs (e. g., the brain). Pharmaceuticals frequently employ acetylation to enable such esters to cross the blood–brain barrier (and placenta ), where they are deacetylated by enzymes ...

  6. Peptidylglycine alpha-amidating monooxygenase - Wikipedia

    en.wikipedia.org/wiki/Peptidylglycine_alpha-ami...

    Peptidyl-glycine alpha-amidating monooxygenase, or PAM, is an enzyme that catalyzes the conversion of an n+1 residue long peptide with a C-terminal glycine into an n-residue peptide with a terminal amide group. In the process, one molecule of O 2 is consumed and the glycine residue is removed from the peptide and converted to glyoxylic acid. [5]

  7. Protein phosphatase - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphatase

    A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (), with up to 30% of all proteins being phosphorylated at any given time.

  8. Angiotensin-converting enzyme - Wikipedia

    en.wikipedia.org/wiki/Angiotensin-converting_enzyme

    The angiotensin converting enzyme gene has more than 160 polymorphisms described as of 2018. [24] Studies have shown that different genotypes of angiotensin converting enzyme can lead to varying influence on athletic performance. [25] [26] However, these data should be interpreted with caution due to the relatively small size of the ...

  9. Immobilized enzyme - Wikipedia

    en.wikipedia.org/wiki/Immobilized_enzyme

    Similarly, another crucial site for the functionality of an enzyme is the active-site, which should also be maintained while enzyme is being attached to a surface for immobilization, it is a must to have a selective method for the attachment of surface/material to not end up with an immobilized, but dysfunctional enzyme. [3]