what is the answers? Fill in the blanks:is the type of enzyme specificity exhibited by hydrolysis of urea using ureaseis a theory that explains the initial increase in the rate of rate of enzyme reaction whentemperature is increasedis a type of enzyme specificity exhibited by chymotrypsin hydrolyzing peptide bondsis a general term that refers to a substance that decreases rate of an enzyme reactionis the difference in free energy between the reactants and the transition state

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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 true
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 ?
Which of the following statements about enzyme character-istics is true?(a) Enzymes generally exhibit a high degree of specificityfor one particular substrate.(b) Enzyme-substrate complexes occur when a substratemolecule collides with the allosteric site of an enzyme.(c) Chemical bonds within a substrate are strength-ened when this substrate forms an enzyme-substratecomplex.(d) Enzymes have a region called the active site, which pro-vides an area where it can form a loose association withits substrate.(e) a and d.
Carbonic anhydrase is strongly inhibited by the drug acetazolamide, which is used as a diuretic (i.e., to increase the production of urine) and to lower excessively high pressure in the eye (due to accumulation of intraocular fluid) in glaucoma. Carbonic anhydrase plays an important role in these and other secretory processes because it participates in regulatingthe pH and bicarbonate content of several body fluids. The experimental curve of initial reaction velocity (as percentage of Vmax ) versus [S] for the carbonic anhydrase reaction is illustrated below (upper curve). When the experiment is repeated in the presence of acetazolamide, the lower curve is obtained. From an inspection of the curves and your knowledge of the kinetic properties of competitive and mixed enzyme inhibitors, determinethe nature of the inhibition by acetazolamide. Explain your reasoning.
The active (catalytic) site of an enzyme contains the side chains of amino acid residues that areconserved because they participate in the protein’s catalytic activity. The bulk of the enzyme,however, is not part of the active site. A substantial amount of energy is required to synthesizeenzymes. Why are these molecules so large?
Some metabolic conditions such as diabetesmellitus cause disturbances in the acid–basebalance of the body, which gives the bodyfluids an abnormally low pH. Explain howthis could affect enzyme–substrate reactionsand metabolic pathways in the body.
What are the description of the ff?A. Effect of pH with enzymaticactivity. Include example ofenzymes optimum pH.B. Effect of activators on theactivity of enzymes. Includeexamples.
Protease is an enzyme that catalyzes the breaking of amide bonds which is very stable at “mild” conditions, namely body temperature and pH 7 (if done in the lab requires hot conditions, concentrated HCl for hours). Some proteases have two aspartic acid residues at their active sites. Write the reaction mechanism (which follows general acid-base catalysis)
Which of the following is not true about enzymes? 4. Transition state stabilization can significantly increase the activation energy for a reaction. Nucleophilic groups can catalyze reactions through the transient formation of covalent bonds with the substrate. Zymogens are the inactive precursors of enzyme. Enzymes typically act under milder conditions of temperature and pH than non-enzyme chemical catalysts. Enzyme inhibitors interact reversibly or irreversibly with an enzyme to alter its Km and /or Vmax values.
Which of the following statements are correct? explain your answers.a. The active site of an enzyme usually occupies only a small fraction of the enzyme surface.B. catalysis by some enzymes involves the formation of a covalent bond between an amino acid side chain and a substrate molecule.c. a β sheet can contain up to five strands, but no more.d. The specificity of an antibody molecule is contained exclusively in loops on the surface of the folded light-chain domain.e. The possible linear arrangements of amino acids are so vast that new proteins almost never evolve by alteration of old ones. f. allosteric enzymes have two or more binding sites. G. noncovalent bonds are too weak to influence the three- dimensional structure of macromolecules.
In _____________ inhibition, the EI complex readily dissociates and the enzyme is again available for substrate binding.
Ethylene glycol (HO−CH2−CH2−OH) is a major component of antifreeze. In the body, it is first converted to HOOC−CHO (oxoethanoic acid) and then to HOOC−COOH (oxalic acid), which is toxic. What class of enzyme catalyzes both of the reactions of ethylene glycol? The treatment for the ingestion of ethylene glycol is an intravenous solution of ethanol. How might this help prevent toxic levels of oxalic acid in the body?

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