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Based on this infomation; vou draw the conclusion that inhibitor binds which enzyme form(s)? (3 pts)...

Question

Based on this infomation; vou draw the conclusion that inhibitor binds which enzyme form(s)? (3 pts)

Based on this infomation; vou draw the conclusion that inhibitor binds which enzyme form(s)? (3 pts)



Answers

Consider an enzyme that is subject to allosteric regulation. If a competitive inhibitor (not an allosteric inhibitor) is added to a solution containing such an enzyme, the ratio of enzyme molecules in the active form to those in the inactive form increases. Explain this observation.

This question asks us. Explain how an inhibitor condition Upton enzymes action without binding to the active site. So when we think about enzymes, we usually think about what is called competitive in addition, and that is basically where, UM, some substrate where the thing that binds to the enzyme binds to the enzymes active site and blocks it. And then the enzyme can no longer bind to the substrate that it needs to. And the enzyme is basically inactivated and inhibition has occurred, right? But in this question we're looking at How can we disrupt the enzymes action without binding to that active site? Can we bind at a different site? And the answer is yes. There's this process called non competitive inhibition and basically a noncompetitive inhibition or al Oh, Starik Regulation. And specifically we're looking at Alice Derek inhibition. We can bind ah substrate to another site on the enzyme and cause a confirmation or shape change of that enzyme. So if we look a little bit closer at the diagrams here, Ah, specifically, we are looking at inhibition, so we are only going to focus on this right side, right here, left side, and so we won't focus on this. On the left side, we're looking at Alice Derek inhibition. So what happens is they We haven't enzyme given by r. C. And there are two sites on that enzyme. There's the usual, um, active site to which the substrate minds and there's the Alistair Excite toe, which another substrate combined. But that binding will cause that enzyme to change shape. So what happens is if we have this, um, substrate coming and bind to that Alistair Excite. We get a shape change of this active site, so the active site basically closes up and the substrate no longer combined to it. So that is why um, we can inhibit an enzyme without having to bind to the active site itself. So that is called non competitive inhibition or Alice Derek inhibition.

Remember in times or biological catalysts that lower that lower the activation, energy and speed of chemical reactions, and they work in environmental conditions that are specific to them. So, for example, the enzymes in your body operate at your body temperature, and another example is the enzymes that work for digestion in your stomach. Operate at an acidic in an acidic environment. So enzymes have specific environmental conditions where they optimally operate. We want to talk about a few of these, so I picked four. They operate at a specific within a specific range of temperatures, So if the enzymes are from your body, they operate at your body temperature. Insides that work and other organisms say reptiles probably operate at a different environmental temperature. Because some reptiles live in the desert, those enzymes are gonna have a specific operating temperature. Some reptiles live in places where there's Ah, winter, and so the temperature drives in somatic function. And those were gonna be highly specific to the organism in which the enzymes function and the environmental condition in which the enzymes were found. The second environmental condition that's important is Ph. Ph. Kid really influenced Instamatic activity, for example, in your stomach. You have enzymes that Onley function when the pH of the stomach drops to between 1.5 and three. Those enzymes are denatured or basically rendered function lis once they go to the small intestine, because the pH of the 1st 3rd of the small intestine is brought up to a more neutral level. And so pH influences Theobald bility of enzymes to function the's last year that we're gonna talk about talk about concentration, concentration of the enzyme. It's really important. If the ends on concentration is fairly low, then the substrate is limited by how many combined to those few enzymes, so the rate of reaction for an individual reaction with these sped up. But the rate of reaction overall for the population of substrate would be pretty slow, because the ends on concentration wasn't adequate to handle the amount of substrate that's found in that environment. The flip side of that is true if you have a substrate, constant concentration that's too low and the enzyme concentration is high. The production of products will be slowed because there's not enough substrate, and so inside concentration and substance, straight concentration really influence how quickly reactions take place. And so there's an optimal enzyme concentration and an optimal substrate concentration, where you get a peek in the amount of products that's produced from the substrate by the insides. So just keep in mind the enzymes optimally function in certain environmental conditions, and these environmental conditions, if changed, may actually cause the insides to fail to function.

This question is asking us about Alice Terek sites in biochemical pathways. So let's review really quick what an Alice Terek site is. And what does Alice Terek mean? So Alice Terek alot means other. So an Alice Terek site is a site other than the active site in which things such as activators or inhibitors combined. So if we remember active, the active site is where the substrate binds. However, an Alice Terek site is when an activator, so activators activate the enzyme, so make it work faster or more. An inhibitor can buy into this Alice Derek site. So inhibitors basically turn off this enzyme. So an al historic site is a place other than the active site in which these two things combined. So now if we have a biochemical pathway, so we have a BC and D. N. E. And we have enzyme one and them two ends M. Three and M. Four catalyzing this pathway. In order, the question is asking us, where would be most likely bind in this pathway and most likely have an Alice terek site. So, final products of a lot of biochemical pathways are great way to regulate this entire pathway. If it binds to the primary very first enzyme in the pathway. So why is this? It's because if we have control of this very first step, we can then increase all of these concentrations of B. C. And D. Or decreased B. C and D. In order to then have a resultant final product at the concentrations we want. So binding out hysterically, the enzyme for won't really help us to control this entire pathway. However, binding to the very first enzyme allows us to have a lot of control over all of these steps. So the most likely place for an Alice Terek site would be enzyme one. Therefore the answer here is going to be a enzyme one would be the best place for the final product e uh to bind Alice terrifically to have a control of this biochemical pathway.

So the compound that we see is quite structurally similar to an intermediate of the rear cycle that is centrally so. The structure of sertraline that should that we see sertraline is an amino acid that is formed by the addition of a carbon mile group from Carbondale phosphate to an amino acid. All tonight the enzyme all tonight trans cover called Majlis catalyzed this reaction So therefore the inhabited due to a structural resemblance of the product sertraline kind, inhibit the enzyme all tonight trans carbon Millie's. So this prevents the direct synthesis our target products. So this would in turn block the rear cycle and result in a toxic accumulation of ammonia. Yeah.


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