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Biochemistry

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Submitted By cherryface
Words 1057
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Biochemistry Task 4 00046260

A.
1. Two features that make all enzymes catalysts are that they increases the rate in chemical reaction without being used or modified and the thermodynamic properties of the reaction do not change (Hudon-Miller, 2012).
2.

(Gresham HS IB Biology, 2007)
3.
(Shmoop Editorial Team, 2008)

4. The first two steps of fructose metabolism in the liver is fructose is broken down by fructokinase into fructose -1-phosphate substrate and then Aldolase B converts fructose-1-phostpate into DHAP-glyeraldehyde product. At this step, it can go into glycolysis and make ATP or gluconegenesis to eventually make glycogen (Hudon-Miller, 2012).

5.
a. With the lack of aldolase B, there is no longer made product of DHAP-glyerldehyde and therefore, there is no product going into glycolysis to make ATP or product going into gluconegenesis to eventually make glycogen. Fructose is still being broken down to make fructose-1-phospate but it is building up in the liver because there is not enzyme to convert it to DHAP-glyerldehyde. Fructose is no longer being used as energy in the liver (Sanders, 2012).

b. Fructose is still being broken down to make fructose-1-phospate but it is building up in the liver because there is not enzyme to convert it to DHAP-glyerldehyde. The phosphate is stuck with fructose and as this is being made, phosphate is being depleted in the cells. The Electron Transport Chain uses free phosphate to make ATP. If there is a lack of phosphate then the Electron Transport chain cannot make ATP. The production of ATP slows down and the liver cells low energy causes liver failure (Sanders, 2012).

B.
1. Cori cycle basically happens when a muscle is undergoing anaerobic conditions. It takes glucose and converts it into lactate during exercise. Then the lactate is brought to the liver and converted back to glucose. The liver has access to oxygen and the muscle does not. In order for glucose to be converted into lactate in the muscle, the liver gives 6 ATP to the muscle so that the muscle can have 2 ATP. Essentially the liver loses 6 ATP to help the muscle cell. This however, cannot be sustained. If the Cori cycle were to remain in the muscle cell it would be a catastrophe because the muscle cell uses only anaerobic process which means it has no access to oxygen and it borrows ATP from the liver to make at least 2 ATP. If this process were not able to take place the muscle would have no way of making any ATP. Borrowing ATP from the liver to make ATP in the muscle is the only source an anaerobic muscle has. Therefore, if the Cori cycle were to happen in the muscle cell, it would have no chance of surviving and the body would be in a severely damaged (Hudon-MIller, 2013).

2.

The Citric cycle is essential in making products such as FAD2, NADH and GTP that enter the Electron transport chain. The electrons in the electron transport chain will be picked up by oxygen. Oxygen is a terminal electron accepter and will combine with hydrogen that are floating by and make water. This is essential in aerobic metabolism (Sanders, 2015).

3. The enzyme chosen for the hypothetical defect is Citrate Synthase. The defect of this enzyme would cause a cease of product Citrate and side product COA-SH. A new Acetyl-CoA would not be made and the next enzyme would not be able to do its job. Thus, the entire cycle would not continue to function and products from the rest of the enzymes would not be made. Production of ATP would decrease because the electron transport chain would not have access and not be able to convert the NADH, FADH, and GTP into ATP. This would decrease ATP because the NADH, FADH and GTP would not be made by the enzymes because the line of work in the cycle would not even happen (Sanders, 2015).

4. FADH2 and NADH are products made in the Citric cyle that carry electrons. They enter the electron transport chain which is located in the intermembrane space of Mitochondria. In this space there are 4 membrane complexes that exchange electrons. NADH will donate an electron to complex one and become NAD+. FAD2 will donate its electron to complex 2 and becomes FAD. Coenzyme Q accepts electrons from complex to 1 and 2 and donates to complex 3. Then complex 3 will transport its electron using the protein cytochrome C to complex 4. That electron will go to oxygen and form water as its product. Complex1, 3, and 4 in the process of transferring electrons will pump out Hydrogen ions to the other side of membrane. Lots of hydrogen ions are made and need to go somewhere where there is not a lot of them. ATP synthase will allow these hydrogen ions to go to the matrix in a controlled manner. The energy from these hydrogen ions will aid ADP and phosphate to make ATP. The formation of ATP in this process is called oxidative phosphorylation. The energy used in NADH and FAD2 is used to form the proton gradient (Sanders, 2013).

C. References

Citric acid cycle with aconitate 2.svg. (2008, September 12). Retrieved January 3, 2016, from https://en.wikipedia.org/wiki/File:Citric_acid_cycle_with_aconitate_2.svg Enzymes in Detail - Shmoop Biology. Retrieved January 3, 2016, from http://www.shmoop.com/energy-flow-enzymes/enzymes.html
Gresham HS IB Biology. (2007) Retrieved from http://science.halleyhosting.com/sci/ibbio/chem/notes/chpt8/enzyme.gif
Hudon-MIller, S. (2013). Cori cycle. Retrieved from http://wgu.hosted.panopto.com/Panopto/Pages/Viewer.aspx?id=d0651973-3ef6-4c01-bb4d-4288c30e3ffe
Hudon-Miller, S. (2012). Enzymes. Retrieved from http://wgu.hosted.panopto.com/Panopto/Pages/Viewer.aspx?id=c99ccc40-4cf5-4e53-b8b1-ccbb100a65c2
Sanders, J. (2015). The Centrality of the Citric Acid Cycle. Retrieved from http://wgu.hosted.panopto.com/Panopto/Pages/Viewer.aspx?id=5f56ada4-2229-4f96-9770-21dc2738c98e
Sanders, J. (2013). Electron transport chain. Retrieved from http://wgu.hosted.panopto.com/Panopto/Pages/Viewer.aspx?id=9ec716ab-3610-47a4-bb37-41b4805935d6
Sanders, J. (2012) Hereditary fructose intolerance. Retrieved from http://wgu.hosted.panopto.com/Panopto/Pages/Viewer/Default.aspx?id=4b4de18d-60f5-4866-a77c-b673ce51aab6 In-text citation: Sanders, 2013

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