is the type of enzyme specificity exhibited by hydrolysis of urea using urease
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Q: Explain Maple syrup urine disease . which enzyme is deficient in it ?
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Q: The following enzymes belong to the same class of enzymes, except for A. Chymotrypsin B. Thrombin C.…
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Q: GLUCONEOGENESIS Reactant Coenzyme/ Product Cofactor Enzymes
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Q: What classification of enzyme is catalase? Give the Enzyme Commission (E.C.) number of catalase.
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- Match the classes of enzymes with their functions: Catalyze cleavage of molecules driven by addition of water Catalyze transfer of functional groups within a molecule Catalyze linking two molecules into a larger one Catalyze electron transfer reaction between two molecules Catalyze transfer of functional groups between different molecules Hydrolyze peptide bonds [Choose ] [Choose] [Choose ] [Choose ] [Choose] [ Choose ] Proteases Transferases Oxidoreductases Ligases Hydrolases Isomerases + + + + ‡Identify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.Which of the following is the most probable catalytic triad of an enzyme that follows general acid base catalysis? -Glu-His-Cys -Leu-His-Ser -Glu-Phe-Ser -Asp-His-Ala -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -
- If you can clearly visualize the chymotrypsin mechanism of action, you should be able to picture the structure of the transition state right after the enzyme attacks the first substrate. Think hard about what we have covered, and visualize that transition state accurately:Which of the following statements are true about enzyme regulation via noncovalent interactions? Select all that apply. Molecules can cause a change in enzyme shape because they're able to bind to the enzyme somewhere other than the active site The function of an enzyme is altered by a chemical change in its primary structure, which is called phosphorylation Molecules that are similar to the substrate in both size and shape can compete with the substrate for access to the enzyme's active site Molecules that are similar to the substrate in both size and shape can compete with the substrate for access to a location other than the active siteName: Date: Year/Section: Score: ACTIVITY 5.1.1 Determine the catalytic power of jack bean urease in catalyzing the hydrolysis of urea given the following conditions: At 20C, the rate constant for enzyme-catalyzed reaction is 3x104/sec The rate constant for the uncatalyzed hydrolysis of urea is 3x10-10/sec. ACTIVITY 5.1.2 Give examples of enzymatic reaction for each type of specificity 96 Copyright 2019. All Rights Reserved. 2--------
- Define enzyme inhibition. Explain in detail the different types of inhibitions with suitable examples.Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are trueOne mechanism by which lead exerts its poisonous effect on enzymes can be stopped by chelation therapy with EDTA. Describe this type of lead poisoning and explain why it is reversible.
- 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.One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. Enzyme Substrate Turnover number (per second) Ribonuclease RNA 100 Fumarase fumarate 800 Lactate dehydrogenase lactate 1000 Urease urea 10,000 How many molecules of urea can one molecule of urease act on in 12.0 min ?Consider the mechanism of enolase, as indicated below. Which of the following correctly describes the roles of the Mg2+ as illustrated in the figure? (This is a multi- select question). Mg2+ Mg2 Enolase PO3- OH -C-C-H H OH HO H-N-H Lys 345 Glu211 2-Phosphoglycerate bound to enzyme Mg2+ Mg2 PO3- OH C-C-H OH HO H H-N*-H Lys 345 O Glu211 Enolic intermediate HOH PO3- H Phosphoenolpyruvate The metal ion (Mg2+) is helping to stabilize the extra negative charge that developed on the carboxyl group in the enolic intermediate. The metal ion (Mg2+) is serving as a general base, removing a proton in order to improve the quality of the nucleophile. The metal ion (Mg2+) is assisting in the oxidation of the carboxyl carbon through metal ion catalysis. The metal ion (Mg2+) is helping to orient the substrate properly in the active site. The metal ion (Mg2+) is accepting a proton in order to improve the quality of the leaving group.