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  2. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    Allosteric regulation of an enzyme. 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.

  3. Allosteric enzyme - Wikipedia

    en.wikipedia.org/wiki/Allosteric_enzyme

    Allosteric enzymes need not be oligomers as previously thought, [1] and in fact many systems have demonstrated allostery within single enzymes. [2] In biochemistry, allosteric regulation (or allosteric control) is the regulation of a protein by binding an effector molecule at a site other than the enzyme's active site.

  4. Transcriptional regulation - Wikipedia

    en.wikipedia.org/wiki/Transcriptional_regulation

    These mechanisms include control over protein localization or control over whether the protein can bind DNA. [32] An example of this is the protein HSF1 , which remains bound to Hsp70 in the cytosol and is only translocated into the nucleus upon cellular stress such as heat shock.

  5. Phosphofructokinase 1 - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase_1

    Phosphofructokinase-1 (PFK-1) is one of the most important regulatory enzymes (EC 2.7.1.11) of glycolysis. It is an allosteric enzyme made of 4 subunits and controlled by many activators and inhibitors. PFK-1 catalyzes the important "committed" step of glycolysis, the conversion of fructose 6-phosphate and ATP to fructose 1,6-bisphosphate and ...

  6. Histone deacetylase - Wikipedia

    en.wikipedia.org/wiki/Histone_deacetylase

    This is important because DNA is wrapped around histones, and DNA expression is regulated by acetylation and de-acetylation. HDAC's action is opposite to that of histone acetyltransferase . HDAC proteins are now also called lysine deacetylases (KDAC), to describe their function rather than their target, which also includes non-histone proteins ...

  7. Ribonucleotide reductase - Wikipedia

    en.wikipedia.org/wiki/Ribonucleotide_reductase

    Class IB reductases are not inhibited by dATP because they lack approximately 50 N-terminal amino acids required for the allosteric activity site. [23] Additionally, it is important that the activity of ribonucleotide reductase be under transcriptional and post-transcriptional control because the synthesis of damage-free DNA relies on a ...

  8. Histone acetylation and deacetylation - Wikipedia

    en.wikipedia.org/wiki/Histone_acetylation_and_de...

    The MYST proteins Esa1, Sas2 and Sas3 are found in yeast, MOF is found in Drosophila and mice while Tip60, MOZ, MORF, and HBO1 are found in humans. [9] Tip60 has roles in the regulation of gene transcription, HBO has been found to impact the DNA replication process, MORF is able to acetylate free histones (especially H3 and H4) as well as ...

  9. Ribose-phosphate diphosphokinase - Wikipedia

    en.wikipedia.org/wiki/Ribose-phosphate...

    One subunit of ribose-phosphate diphosphokinase consists of 318 amino acids; the active enzyme complex consists of three homodimers (or six subunits, a hexamer). The structure of one subunit is a five-stranded parallel beta sheet (the central core) surrounded by four alpha helices at the N-terminal domain and five alpha helices at the C ...