Results: Distinguishing the Interactions in the Fructose 1,6-Bisphosphate Binding
Site of Human Liver Pyruvate Kinase that Contribute to Allostery
The overall design of the experiment involved two ways in which protein activation could be altered, in this case, the activation of the human liver pyruvate kinase (hL-PYK). One of the methods used to alter activation was to use effector molecules other than fructose 1,6-bisphosphate (Fru-1,6-BP), which may have the ability to attach to the allosteric site of the hL-PYK, leading to an increase or decrease in protein activity. The second method was to enhance mutations on specific parts of the hL-PYK enzyme itself to see how it interacted with Fru-1,6-BP. Inducing mutations to areas located near the allosteric site of hL-PYK can alter the binding affinity …show more content…
Therefore, the results indicated that protein activation could be induced by effector molecules other than Fru-1,6-BP, or by inducing mutations on the enzyme itself. Essentially, there were three types of effector molecule interactions with the allosteric site, otherwise known as analogue binding. One type of analogue binding involved using analogues that were able to bind to the allosteric site in a similar fashion as Fru-1,6-BP. A second type involved analogues that were able to bind to the binding site, but in a weak manner. The third type of analogue binding involved analogues that were not able to bind to the allosteric site, or that did not lead to allostery, the activation of hL-PYK through
Site of Human Liver Pyruvate Kinase that Contribute to Allostery
The overall design of the experiment involved two ways in which protein activation could be altered, in this case, the activation of the human liver pyruvate kinase (hL-PYK). One of the methods used to alter activation was to use effector molecules other than fructose 1,6-bisphosphate (Fru-1,6-BP), which may have the ability to attach to the allosteric site of the hL-PYK, leading to an increase or decrease in protein activity. The second method was to enhance mutations on specific parts of the hL-PYK enzyme itself to see how it interacted with Fru-1,6-BP. Inducing mutations to areas located near the allosteric site of hL-PYK can alter the binding affinity …show more content…
Therefore, the results indicated that protein activation could be induced by effector molecules other than Fru-1,6-BP, or by inducing mutations on the enzyme itself. Essentially, there were three types of effector molecule interactions with the allosteric site, otherwise known as analogue binding. One type of analogue binding involved using analogues that were able to bind to the allosteric site in a similar fashion as Fru-1,6-BP. A second type involved analogues that were able to bind to the binding site, but in a weak manner. The third type of analogue binding involved analogues that were not able to bind to the allosteric site, or that did not lead to allostery, the activation of hL-PYK through