Search results
Results from the WOW.Com Content Network
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.
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 .
It is orchestrated by transcription factors and other proteins working in concert to finely tune the amount of RNA being produced through a variety of mechanisms. Bacteria and eukaryotes have very different strategies of accomplishing control over transcription, but some important features remain conserved between the two. Most importantly is ...
This is a diagram of allosteric regulation of an enzyme. When inhibitor binds to the allosteric site the shape of active site is altered, so substrate cannot fit into it. An allosteric site is a site on an enzyme, unrelated to its active site, which can bind an effector molecule. This interaction is another mechanism of enzyme regulation.
Glucose-6-phosphate dehydrogenase is the rate-controlling enzyme of this pathway [citation needed]. It is allosterically stimulated by NADP + and strongly inhibited by NADPH. [7] The ratio of NADPH:NADP + is the primary mode of regulation for the enzyme and is normally about 100:1 in liver cytosol [citation needed]. This makes the cytosol a ...
After being produced, the stability and distribution of the different transcripts is regulated (post-transcriptional regulation) by means of RNA binding protein (RBP) that control the various steps and rates controlling events such as alternative splicing, nuclear degradation (), processing, nuclear export (three alternative pathways), sequestration in P-bodies for storage or degradation and ...
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 ...
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. [4]