available. Research an enzyme that is needed in the human body. Address the following topics: 1. Describe the structure of that enzyme. 2. Explain the specific action of that enzyme in the body. 3. What disorders/diseases would you expect if there was a deficiency of this enzyme?
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- I. Indicate whether each of the following statements are true or false. _1. According to the lock-and-key model of enzyme action, the active site of an enzyme is flexible in shape. 2. In an enzyme-catalyzed reaction, the compound that undergoes a chemical change is called the substrate. 3. The nonprotein portion of a conjugated enzyme is the enzyme's active site. _4. Simple enzymes have inorganic cofactors, and conjugated enzymes have organic cofactors. 5. Vitamins are required in minute quantities for normal cellular function. 6. vitamins are found in all food groups. 7. Ribose sugars are found on one chain of the DNA molecule and deoxyribose sugars are found on the other chain of the DNA molecule. 8. A DNA molecule has a double helix at one end of the molecule and a single helix at the other end of the molecule. _9. Complementary bases are held together by covalent bonds. 10. DNA molecules always contain the nitrogenous base thymine.moodle.aaup.edu/mod/quiz/attem MISTRY I Section1 Lecture (20202_100213 purses / BIOCHEMISTRY I Section1 Lecture (20202_100213111 AAUP - JENIN) / 1 May -7 May Time left 0:37: Which of the following is not true for isozymes? O a. Many enzymes occur in several molecular structures called isozymes O b. Isozymes are enzymes that have a different other allosteric site O c. Various isozymes are expressed in different tissues of the body O d. Different isozyme catalyze the same chemical reactions, but differ slightly in their primary sequence and kinetic properties Next page pril 26 (Glycolysis, plysis Control + genesis Part I) Jump to...Amino acid degradation and biosynthesis are related metabolic processes, but they are not identical. Indicate two ways in which they are similar and one in which they are different. Be as specific as you can.
- The following statements refer to enzyme inhibition. Match the statement to the one of the following descriptors to which it is best associated. Descriptors: competitive inhibition; non-competitive inhibition; un-competitive; covalent inhibition. 9a. Inhibition is not reversed even after the inhibitor (1) is removed from solution by dialysis or drug metabolism/excretion. 9b. Inhibitor and substrate reversibly compete for occupancy of a common binding site 9c. The inhibitor binds reversibly only to the preformed E.S (enzyme-substrate) complex forming an inactive E.S.I. 9d. The inhibitor binds reversibly and independently of substrate to an allosteric site producing E.I or a ternary E.S.I complex which can't form product. 9f. The relative amount of inhibition decreases as [S] (the concentration of substrate) increases and S better competes for occupancy of the active site.1. Discuss the glycogen synthesis. Give the three enzymes required for this process and their functions. 2. Discuss the glycogen degradation. Give the three enzymes required for this process and their functions.C. running the reaction at 70 What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify each description of an inhibitor that is either competitive or noncompetitive. A. Increasing substrate reverses inhibition. B. It binds to the enzyme's surface but not to the active site. C. Its structure is similar to that of the substrate.…
- Select all statements that are correct. Enzyme inhibitors more than 1 correct statement. reduce the activation energy of a reaction 1 prevent the formation of the enzyme-substrate complex and no product can be formed reduce the rate at which products are formed by making it harder for the enzyme-substrate complex or the product to be formed prevent the product from being released from the enzyme reduce the activity of the enzyme Note there mightInstructions. Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. _____________________ Name: alkaline phosphatase Reaction: a phosphate monoester + H2O = an alcohol + phosphate _____________________ Reaction: L-threonine = D-threonine. Other information: Inverts both chiral centers, a racemase. _____________________ Name: glycine-N-acylase Reaction: acyl-COA + glycine = CoA + N-acylglycine _____________________ Name: lysine decarboxylase Reaction: L-lysine = cadaverine + CO2 _____________________ Name: methanol dehydrogenase Reaction: methanol + NAD+ = formaldehyde + NADH + H+Instructions. Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. _____________________ Name: alkaline phosphatase Reaction: a phosphate monoester + H2O = an alcohol + phosphate _____________________ Reaction: L-threonine = D-threonine. Other information: Inverts both chiral centers, a racemase. _____________________ Name: glycine-N-acylase Reaction: acyl-COA + glycine = CoA + N-acylglycine _____________________ Name: lysine decarboxylase Reaction: L-lysine = cadaverine + CO2 _____________________ Name: methanol dehydrogenase Reaction: methanol + NAD+ = formaldehyde + NADH + H+ _____________________ Name: citryl-CoA synthetase Reaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA _____________________ Name: D-xylulose reductase Reaction: xylitol + NAD+ = D-xylulose + NADH + H+ _____________________ Name: cellobiose phosphorylase Reaction:…
- Od. Vitamin B2 s page Hexokinase catalyzes phosphorylation of glucose to clucose-6-phosphate, where ATP is used as a donor of phosphate group, this an example of: Select one: NAVIGATION a. Oxidoreductase b. Ligase c. Lyase d. Transferase Next pageI. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4Name: Sincere Frias Date: (0/2/2od0 Period Ced th nzy ck. Enzyme Models & Factors Affecting Enzyme Action PART I – Lock and Key Model st In this part you will construct models of enzymes. Remove the last page and cut all shapes out. 2. The different shapes will represent both enzymes and substrates. 3. Match up as many of the pieces as you can. 1. Questions 1. The enzyme maltase combines the substrates h ydrolysis + Starch molecule to produce the disaccharide maltose. 2. The enzyme ATPase combines the substrates_molecule and to produce the ATP (Adenosine TriPhospate). Iriglyceride 3. The enzyme lipase works on the substrate called 4. The enzyme phosphatase works on the substrate called 5. What is the relationship between the substrate and the enzyme?