In: Science

Submitted By KKWERTZ
Words 760
Pages 4
Biochemical Implications in Metabolic Disorders
Kim Wertz
Western Governors University
August 7, 2013

Biochemical Implications in Metabolic Disorders Enzymes play an important role and are involved in the process of fructose breakdown. The enzymes are catalysts, meaning, they work to lower activation energy without using the reaction.
Sucrose is plain table sugar and it is broken down into glucose and fructose that needs to be broken apart. This process known as glycolysis will break down glucose-producing pyruvate and then it goes into the citric acid cycle to produce ATP. Fructose will break down first, forming fructose 1-phosphate by the enzyme, fructokinase. Aldolase B then will convert the fructose 1-phosphate into DHAP and glyceraldehyde as they enter into the glycolysis pathway. When there is a deficit or a mutation of Aldolase B gene, then hereditary fructose intolerance will occur. Individuals are usually asymptomatic until they ingest sucrose, fructose or sorbitol. When the fructose is ingested, there is a block of the Aldolase B, which will cause an increase of the F1P. This is an autosomal recessive condition from mutation of the Aldolase gene. As of 1991, there have been eight structural defects found in the Aldolase B gene, as documented by Wikipedia. Mutant alleles result in many different mutations; one being base pair substitutes, small deletions, and areas of the splicing regions of the Aldolase B gene. The two by products of F1P can then metabolize and produce glucose, uric acid, lactate and glycogen. Without this process, the body is unable to break down fructose leading to the Cori Cycle. When the body is missing Aldolase B, it will be unable to change energy storage of glycogen into glucose. The body will experience a fall in sugar levels and a…...

Similar Documents

Introduction for Biochemistry Lab -Spectrophotometry

...where absorbance (A) of such solutions can be plotted against the concentration (c) of the test substance producing the color. Some important highlights in this method include that it is a destructive technique in which once the sample is reacted, it cannot be recovered, the chromophore reflects the complementary color that it absorbs and the calibration curves may vary with the different batches of reagents and standards used. Colorimetry is usually used to determine the concentrations of chemicals substance which can give colours either directly or indirectly or after the addition of other chemicals. In addition, with its efficiency in producing large amount of absorbance with relatively small amount of material, it is highly used in biochemistry assay. References Clark, J., (2007). UV-Vis Absorption Spectroscopy: Theorical principals. Retrieved at on 9th May 2014. Robinson, J, W., Frame, E.M.s., and G.M., (2004). UV spectra and the structure of organic molecules. Undergraduate Instrumental Analysis, 6th Ed, p350. Vo, K., (n,d). Spectrophotometry. Retrieved at on 9th May 2014....

Words: 716 - Pages: 3

What Is Biochemistry

...What is Biochemistry and why you should study it? Biochemistry or sometimes we called it as biological chemistry is defined as a scientific study of the chemistry of living organisms, especially the structure, the behavior of a living thing and the function of their chemical component such as proteins ,carbohydrates, lipids, and nucleic acids. Many of these molecules are complex molecules called polymers, which are made up of monomer subunits. Most people consider biochemistry to be same with molecular biology. Nowadays, biochemistry has become the root for understanding all biological processes. It has provided widely explanations for the causes of many diseases in humans, animals and plants. As a student, we should study it because it give to us many kind of knowledge on understanding the biological processes which are happen around us in every single minutes in our life. Since biochemistry is very important, we must study it to know how this biochemistry contributed for the sustainable of tomorrow in the main field of medicine, agriculture and industry. Biochemistry is applied in many health field such as dentistry, medicine and veterinary medicine. For example, in the field of medicine, biochemistry have contribute in the clinical study to maintain and to give a better and healthy life to the population of human all around the world. This have been done by the scientist on how they use biochemistry to diagnose and control the spreading of diseases, product a......

Words: 691 - Pages: 3

Biochemistry Experiment

...Suburb / Town | | Given Names* | | | State | Tas | Postcode | | | | | Preferred Name(optional) | | | Country(if outside Australia) | | Are you an International Student* Yes X No | | Contact Phone 1 | | Date of Birth | 2 | 3 | 0 | 1 | 1 | 9 | 7 | 9 | | Contact Phone 2 | | | | Unit Code* | SBI245 | Lecturer name* | Dr Hao Wang | Unit Name* | Biochemistry | Assignment Title* | Assignment 1: Experiment | Charles Darwin University is unable to accept and process assignments without a completed assignment cover sheet. PLEASE READ THE IMPORTANT INFORMATION ON THE REVERSE OF THIS FORM. Due date* | Posting date * | Semester | 10/04/14 | 10/04/14 | X Semester 1 Semester 2 Summer Semester Term 1 Term 2 Term 3 Term 4 | Have you applied for an extension? Yes X No Student Comments | | | | | | | Lecturer Comments | | | | | | | Biochemistry Experiment Pre-workout Exercise Enhancement & Weight Cutting Stack Abstract: This experiment was conducted to investigate the effects of a blend of supplements that could be used as a pre-workout and weight cutting stack for an individual who often undergoes weight cutting programs for competition purposes. The time taken to complete exercises, the recovery time, the number......

Words: 1776 - Pages: 8


...DNA Replication Jennifer Wilson Biochemistry GRT1 Margie Hayes January 18,2015 Deoxyribonucleic Acid (DNA) DNA is made of chemical building blocks called nucleotides. These building blocks (nucleotides) are made of phosphate, sugar and one of four types of nitrogen bases. The four types of nitrogen bases found in nucleotides are: adenine, thymine, guanine and cytosine. These nucleotides are either purine or pyrimidine based, called nucleotide subunits. The purine base are adenine and guanine. The pyrimidine based are thymine and cytosine. The DNA strand is formed when the nucleotides are linked into chains, with the phosphate and sugar group alternating. As you can see in the diagram above, adenine bonds with thymine and guanine bonds with cytosine. These bonds take place by hydrogen bonding. DNA Replication Fork Topoisomerases are enzymes that regulate the overwinding or underwinding of DNA, shown as the yellow wire above. Topoisomerases catalyze and guide the unknotting and unkinking of DNA. The double-helical configuration that DNA strands naturally reside makes them difficult to separate, so they must be separated by helicase enzymes. Helicase separates the strands of a DNA double helix by using the energy from ATP hydrolysis so replication can begin. The replication bubble allows replication to take place in 2 directions. Primase is an enzyme that synthesizes short RNA sequences called primers. These primers are the starting point for DNA synthesis at...

Words: 653 - Pages: 3

Biochemistry Wgu

...following points: • how chaperones normally act in the cell • the name of the specific protein that acts as a chaperone in BSE • how the protein that acts as a chaperone is different from typical chaperone proteins (Insert in-text citation here). 4. Insert your recommendation for ways that a country that does not have regulations in place can decrease the risk of BSE infecting the food source, based on your understanding of BSE and how it spreads (e.g., feeding practices, animal disposal). (Insert in-text citation here). References Insert your alphabetized reference list here. Click here for a help document that demonstrates how to cite commonly used Biochemistry sources. A sample reference is listed below. Wolfe, G. (2000). Thinkwell Biochemistry – section 3.4.2. Fluid Mosaic Model. Retrieved from-

Words: 656 - Pages: 3

Biochemistry 208.5.5

...fat diets can actually do more harm than good. The body needs moderation of all energy producing macronutrients; fats, carbohydrates and proteins. By not eating any fat, the body starts to utilize the fats stored in the body, thus depleting the stores and people lose weight. However, once those stores are gone, the good fats or HDL’s, are no longer able to filter out the bad cholesterol. This can lead to increased cholesterol levels in the blood and heart disease. A no fat diet also causes poor vitamin absorption of the necessary fat soluble vitamins A, D, E and K. Fats transport those vitamins from the liver to various parts of the body. Sanders, J. (2013). Fatty Acid Structure video. Wolfe, George. Thinkwell Biochemistry, Thinkwell Biology lectures....

Words: 601 - Pages: 3

Wgu Biochemistry

...! ! ! ! ! ! Western Governors University Biochemistry GRT Task 5: Lipids, The Importance of Fat in the Diet ! ! ! ! ! ! ! ! ! Melissa Robinson Student ID: 000389892 June 2015
 Fat is often maligned in the media, and is often named “public enemy #1” because of the obesity epidemic that our country has been struggling against for several years. However, fat is an essential component in the human body. Fat must be taken in and used by the body to maintain health. That said, moderation is key. Too much of a good thing, can lead to other health issues, as seen by the obesity level in this country. It is important to strike a balance between healthy consumption of fats that the body needs to function, and the other end of the spectrum, too much fat or no fat at all in the diet. Below is a brief overview of how the body uses fats, known as lipids, in the body and why lipids are essential to the body’s health. A. Energy Stored as Fat Food is often shared with others socially and enjoyed for its taste and aroma. Fatty foods are often considered pleasurable to eat because they provide people with richness of flavor, texture and an overall feeling of satisfaction. However, fat in foods is not just there for pleasure. The body uses fat an energy source. The fat is stored in tissue called “adipose tissue.” A special type of molecule, called a triglyceride, is used by the body to store fat. Triglycerides are used as large,......

Words: 998 - Pages: 4


...Protein Function Biochemistry Task #3 Diane Pruchnicki Student ID# 000472055 Oxygenated vs. Deoxygenated Hemoglobin OXYGENATED HEMOGLOBIN • Heme shape is flattened or planar, due to oxygen tugging on iron • Hemoglobin can better bind with oxygen, known as R-state, or relaxed state • Iron can easily picks up oxygen • Hemoglobin reaches the lungs and an oxygen molecule adheres to the iron • Blood is bright red in color, due to oxygenated blood traveling from heart to systemic circulation DEOXYGENATED HEMOGLOBIN • Heme shape is pyramid/dome shaped • Hemoglobin binding without oxygen, known as a T-state, or tense state • T-state makes oxygen binding more difficult • Blood is maroon/blue in color, due to decreased amount of oxygen. Blood is traveling back to heart from systemic circulation pH Impact on Binding & Release of Oxygen by Hemoglobin Comparison between Hemoglobin and Myoglobin Structure Hemoglobin Diseased Cells Difference from Normal RBC’s in Oxygen Transportation • Normal RBC’s keep a disc-like shape (doughnut shape minus the hole), while moving easily through the small arteries and capillaries, where they release oxygen to the peripheral tissues. These normal RBC’s carry oxygen from the lungs to the rest of the body without difficulty. • Sickle cells are known to be sticky/stiff and form into a sickle, or crescent, shape when they lose oxygen. With the loss of oxygen,......

Words: 473 - Pages: 2

Biochemistry C624

...Task 4 Western Governors University Biochemistry C624 November 9, 2015 A1. Describe two important features that make all enzymes catalysts. An enzyme is a protein that serves as catalysts of biological reactions converting a substrate into a product. The catalyst can increase the rate of the reaction. A catalyst does not change, or get consumed, during the reaction. A2. Create an original diagram, or series of diagrams with clear labels depicting the enzymatic cycle (lock and key or induced fit model). A3. Create a diagram that illustrates the aE of a reaction in the presence and absence of an enzyme. A4. Explain the reactions catalyzed by enzymes in the first two steps of fructose metabolism in the liver. Fructose in the blood passes through the cell membrane into the liver cell and initiates phosphoralation with fructokinase for the metabolism of fructose. The fructokinase then uses the phosphate and produces F-1-P (fructose 1 phosphate). F-1-P is the substrate for the enzyme Aldolase B. Aldolase B takes the F-1-P and makes DHAP and glyceraldehyde, the products of Aldolase B. The DHAP and glyceraldehyde are intermediates in glycolysis and continue down to make pyruvate which then can make ATP synthesis or fatty acids. (Sanders, J. 2013) A5. Discuss how a deficiency in aldolase B is responsible for HFI. Hereditary Fructose Intolerance (HFI) results from a deficiency of aldolase B activity primarily in the liver, but also in the kidneys and small......

Words: 1113 - Pages: 5


...Running head: BIOCHEMISTRY TASK 2 Biochemistry Task 2 Terry Buckman Western Governor's University Biochemistry Task 2 I want to talk about 4 of the bonds or interaction that stabilize a protein’s structure at the tertiary level. The first bond is the ionic bonding which is most sensitive to pH changes and can occur between oppositely charged R groups. The next one is disulfide bonds which are covalent bonds that can take place between two cysteine R groups. Another one is hydrophobic interactions which is nonpolar. These R groups will cluster together on the interior of the protein and this will minimize their contact with water. The last one is van der Waals interactions takes place between the tightly packed nonpolar R groups on the interior of the protein. I would like to talk about BSE or bovine spongiform encephalopathy, in other words mad cow disease. This disease is called by misfolding prions at the molecular level. There are harmful and nonharmful forms of prions. The nonharmful form is PrPc and the harmful form is PrPsc. The PrPsc are hydrophobic and will cause the normal proteins to conform to their misfolding and harmful prion shape. This happens by way of a chaperonin. A polypeptide chain will enter the chaperonin and with proper environment of chaperonin, the polypeptide chain will fold correctly and exit as the normal prion, PrPc. Now in BSE, a polypeptide chain will enter into a “bad” chaperonin, the prion, and will get a misfolded prion to exit,......

Words: 394 - Pages: 2

Biochemistry Task 2 Wgu

...Biochemistry Task 2 Brandy McDowell 000499302 November 30, 2015 A. (Lyman, 2013) B. (Wolfe, 2000) (Wolfe, 2000) B. (Wolfe, 2000) (Wolfe, 2000) C. (Hudon-Miller, 2012) D. (Hudon-Miller, 2012) E. The four forces that stabilize a protein. * Hydrophobic interactions which are interactions by nonpolar amino acids. The weakest of the four types of bonds. * Hydrogen bond made up of interactions of polar or charged amino acids. The amino acids share their hydrogen. This is also a weak bond, but it is stronger than the hydrophobic interaction. * Ionic bonds are made up of charged amino acids. A positive charge of an amino acid attracts to a negative charge of another amino acid. This bond is a little stronger than the hydrogen bond, but not as strong as the polypeptide bond. * Disulfide bond only occurs between two cysteine amino acids. Two cysteine amino acids form a sulfa-sulfa bridge. This is a strong covalent interaction. (Borges, 2014) F1.  Explain the role of prions in BSE, including each of the following: ●How prions are formed – Prions are malformed proteins. Instead of reproducing, the prions cause normal proteins to change to the malformed version. The normal prion (PrPc) is bound to the surface of neurons. PrPc can be altered and become misfolded taking on a different conformation which is then known as PrPsc. ●The connection between misfolding and aggregation – Because the misfolded prions are......

Words: 664 - Pages: 3


...when there are excessive amounts in the body (Neitzel n.d.). References Fat chemistry 101 - Low Carb Steve. (n.d.). Retrieved May 11, 2016, from Neitzel, J. J. (n.d.). Fatty acid molecules: A Role in Cell Signaling. Retrieved May 11, 2016, from 14231940 O’Malley, M. (2014). Fatty acid oxidation. Retrieved from 9467b4360cd7 Sanders, J. (2013). Fatty acid structure. Retrieved from d72a7e3334a3 Wolfe, G. (2000). Thinkwell Biochemistry – section 3.4.2. Fluid mosaic model. Retrieved from 820589&levelTwoID=350661&mode=browse...

Words: 473 - Pages: 2


...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......

Words: 1057 - Pages: 5


...Heather Mandigo Biochemistry task 2 Student ID #000598641 BIOCHEMISTRY TASK 2 2 A. (Yatherajam, 2015)     B. (Wolfe, 2000) (Khan Academy, 2016) B. (Khan Academy, 2016) C & D.  (Hudon-Miller, 2012)     E.  The four forces that stabilize the protein structure at the tertiary level are hydrophobic interactions, ionic bonding, disulfide bridges and hydrogen bonds (Wolfe, 2000) Hydrophobic interactions occur when the amino acids have a R group that is hydrophobic/nonpolar (Wolfe, 2000). These hydrophobic groups migrate to the inside of the molecule since they are rejected by water (Wolfe, 2000). These hydrophobic molecules are water fearing. Ionic bonding occurs when the R group is charged and there is an attraction between positive and negative charges (Wolfe, 2000). Disulfide bridges occur between 2 cysteine molecules and only occurs between these 2 molecules (Wolfe, 2000). These types of bonds have very strong covalent bonds (Wolfe, 2000). Hydrogen bonds occur between R groups that are polar or charged (Borges, 2014). What happens is, a hydrogen atom is shared with another amino acid between a nitrogen atom or an oxygen atom, creating the hydrogen bond (Borges, 2014). These are the weakest of the bonds (Borges, 2014). F. Prions play a significant role in the development of bovine spongiform encephalopathy or Mad Cow Disease. Prions are proteins which cause disease......

Words: 770 - Pages: 4


...                            Biochemistry Task 3                                                             A.                                                                                                             (Hudon­Miller, Hemoglobin…, 2012)    1.  Two differences between oxygenated and deoxygenated hemoglobin are shape and  color. Color change is reflected in the amount of oxygen bound to the hemoglobin. The  more oxygen there is, the brighter red the hemoglobin will be. In the oxygenated state the  shape changes as well. In this state, the protein is in what is known as the R or relaxed  state. (Hudon­Miller, 2012) When the oxygen leaves the the hemoglobin the heme changes  to a dome shape, which in turn, changes the shape of the protein. This is known as the T or  tense state. (Hudon­Miller, Oxygenated....,2012)    2.  Oxygen binds more at higher pH and is released better at a lower pH. Our lunges are  higher pH which is where hemoglobin gets saturated with oxygen. Our periphery is more  acidic at a lower pH. Hemoglobin is able to release oxygen easier at lower pH levels. This is  what allows oxygen to make it to our fingers and toes. (Hudon­Miller, The Bohr…,2012)  2a.                                                                                           (Hudon­Miller, The  Bohr…,2012)    3.                                                                      (Hudon­Miller, ......

Words: 540 - Pages: 3

Les Indestructibles 2 FRENCH DVDSCR 2018 | 蚁人2:黄蜂女现身.2018.HDTC.1080P.X264.AAC.CHS.mp4 | Chapter 52