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  2. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier (inhibitor or activator) might affect the rate. An enzyme (E) is a protein molecule that serves as a biological catalyst to facilitate and accelerate a chemical ...

  3. Deoxyribozyme - Wikipedia

    en.wikipedia.org/wiki/Deoxyribozyme

    Although RNA enzymes were discovered before DNA enzymes, the latter have some distinct advantages. DNA is more cost-effective, and DNA can be made with longer sequence length and can be made with higher purity in solid-phase synthesis. [30] Several studies have shown the usage of DNAzymes to inhibit influenza A and B virus replication in host ...

  4. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA. Conservation of enzyme requires that [28] = where is now the total enzyme concentration. After combining the two expressions some straightforward algebra leads to the following expression for the concentration ...

  5. Histone-modifying enzymes - Wikipedia

    en.wikipedia.org/wiki/Histone-modifying_enzymes

    Histone-modifying enzymes are enzymes involved in the modification of histone substrates after protein translation and affect cellular processes including gene expression. [ 1 ] [ 2 ] To safely store the eukaryotic genome , DNA is wrapped around four core histone proteins (H3, H4, H2A, H2B), which then join to form nucleosomes .

  6. Post-translational modification - Wikipedia

    en.wikipedia.org/wiki/Post-translational...

    Phosphorylation is highly effective for controlling the enzyme activity and is the most common change after translation. [2] Many eukaryotic and prokaryotic proteins also have carbohydrate molecules attached to them in a process called glycosylation, which can promote protein folding and improve stability as well as serving regulatory functions.

  7. Methyltransferase - Wikipedia

    en.wikipedia.org/wiki/Methyltransferase

    Inhibition of overall DNA methyltransferase activity has been proposed as a treatment option, but DNMT inhibitors, analogs of their cytosine substrates, have been found to be highly toxic due to their similarity to cytosine (see right); this similarity to the nucleotide causes the inhibitor to be incorporated into DNA translation, causing non ...

  8. Transcription-translation coupling - Wikipedia

    en.wikipedia.org/wiki/Transcription-translation...

    Translation promotes transcription elongation and regulates transcription termination. Functional coupling between transcription and translation is caused by direct physical interactions between the ribosome and RNA polymerase ("expressome complex"), ribosome-dependent changes to nascent mRNA secondary structure which affect RNA polymerase activity (e.g. "attenuation"), and ribosome-dependent ...

  9. Eukaryotic transcription - Wikipedia

    en.wikipedia.org/wiki/Eukaryotic_transcription

    Double stranded DNA that enters from the front of the enzyme is unzipped to avail the template strand for RNA synthesis. For every DNA base pair separated by the advancing polymerase, one hybrid RNA:DNA base pair is immediately formed. DNA strands and nascent RNA chain exit from separate channels; the two DNA strands reunite at the trailing end ...

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