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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.
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.
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 ADP. Glycolysis is the foundation for respiration, both anaerobic and aerobic.
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 ...
The allosteric binding site in PC offers a target for modifiers of activity that may be useful in the treatment of obesity or type II diabetes, and the mechanistic insights gained from the complete structural description of RePC (R. etli) permit detailed investigations into the individual catalytic and regulatory sites of the enzyme.
[1] [2] This reversible step acts as the key regulatory control point in sucrose biosynthesis, and is an excellent example of various key enzyme regulation strategies such as allosteric control and reversible phosphorylation. [3] This enzyme participates in starch and sucrose metabolism. [2]
The advocates of murburn concept have provided precepts and proof of concept for murburn models of diverse life processes (drug metabolism, cellular respiration, thermogenesis, homeostasis, photosynthesis, electrophysiology, photo-transduction in retina, lactate metabolism in liver, role of hemoglobin in erythrocytes, etc.).
In a) the allosteric enzyme functions normally. In b), it is inhibited. This type of enzymes presents two binding sites: the substrate of the enzyme and the effectors. Effectors are small molecules which modulate the enzyme activity; they function through reversible, non-covalent binding of a regulatory metabolite in the allosteric site (which ...