1 enzymes are a class of proteins that catalyze biochemical reaction.what are ribozymes? 2 what is the active side of an enzyme? 3 what is the proximity effect in catalysis? 4 what is the orientation effect in catalysis?
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- 12. Nirogenase is an enzyme that converts the remarkably stable triple bond in N2 into a usable form. It uses an iron sulfur cluster comprised of iron and the sulfur atoms of several active site cysteine residues. Based on your knowledge of Biochemistry what is the enzyme doing to effectively carry out this reaction? a) stabilizing the transition state for the reaction by hydrophobic effects b) stabilizing the ground state for the reaction by hydrophobic effects c) stabilizing the transition state for the reaction by metal ion catalysis d) stabilizing the ground state for the reaction by metal ion catalysis e) all of the above1.The class of enzyme that catalyzes addition of a group to a double bond is? oxidoreductases lyases ligases isomerases hydrolases transferases 2. Suppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the following would be true of the enzyme? the active site of the enzyme must be rigid the active site of the enzyme must be flexible only one substrate could be converted to product by the enzyme the enzyme could bind different substrates if the substrates shared a common motif somewhere in their structures the entire enzyme must be rigid 3. Which of the following enzymes is found in blood serum and is diagnostic of prostate cancer if enzyme levels are elevated? alanine aminotransferase phosphohexose isomerase lactate dehydrogenase acid phosphatase alkaline phosphatase 4. A blood test returns elevated aspartate aminotransferase levels. You suspect that the patient has suffered a heart attack. What other serum enzyme level of…1. What do some enzymes require for catalytic activity? What is a catalytically active complete enzyme called, along with its cofactor?2. Classify the enzymes. What class of enzymes are lactate dehydrogenase and alpha-amylase?3. What is the function of an enzyme as a catalyst? Where does an enzyme-catalyzed reaction occur?4. What is the most used enzyme activity unit? What is understood when one unit of enzyme activity is mentioned?5. What are the factors affecting the rate of an enzymatic reaction?6. What are the reasons why the rate of a reaction catalyzed by an enzyme decreases over time?7.Describe the relationship between ACE2 (Angiotensin converting enzyme 2) and the COVID-19 outbreak using bioinformatics tools.
- 1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent
- 6X9 X What are the steps for an enzyme to create a product in order: 1. The energy of activation is lowered so the reaction can happen quicker. 2. Substrate attaches to the active site. 3. The product is created and released from the active site. 4. The energy of activation is lowered so the reaction can happen slower. 5. A specific substrate attaches to the active site. Selected Answer: Answers: 5 -- 4 --> 3 5--1--> 3 2 1 -> 3 5 -- 4 --> 3 2--> 4 --> 37. What is the activation site of an enzyme? 8. What does it mean to denature an enzyme? 9. List at least 2 ways an enzyme may be denatured. 10. Explain the difference between endergonic and exergonic reactions.2.1 The Na'/K' pump is constantly working to push sodium out and potassium into the cell. What role does ATP play in the working of this pump? What do you think would happen to the cell did not have enough ATP to power the pump? 3. Enzymes. Enzymes act as a catalyst to speed up many biochemical reactions. This means that they will lower the energy needed to start a reaction. 3.1 In the picture below label the following: substrate, active site, enzyme, product. Briefly explain what is happening in each picture (figure 6.16 will be VERY helpful).
- 1 what is does the induced -fit model account for? 2 why are most enzyme inactive at higher temperature ( greater than 37degree Celsius) 3 Does this happen to all enzymes in all species? 4 What are the formulas for the reduced form of the coenzymes?1. You are studying the enzyme catalyzed reaction below, and you find the KM is 3.3x10-4 M,. You also find that k1 is 4.3x106 M-'s-1. What is the dissociation constant (KD) for the enzyme/substrate complex? k1 k2 E+S ES E+P k.1Sucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C 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…