15 All of the following are characteristics of all enzymes EXCEPT? Select the correct response: • They are made up entirely of amino acid residues. They are water-soluble proteins with spherical shape. They have amino acid side chains that are critical for facilitating catalysis. They facilitate catalysis without being consumed in the over-all process. They have a catalytic region that stabilizes the substrate's transition state.

15 All of the following are characteristics of all enzymes EXCEPT? Select the correct response: • They are made up entirely of amino acid residues. They are water-soluble proteins with spherical shape. They have amino acid side chains that are critical for facilitating catalysis. They facilitate catalysis without being consumed in the over-all process. They have a catalytic region that stabilizes the substrate's transition state.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 9TYK: Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric...

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1.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…
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
According to the induced fit hypothesis of enzyme catalysis, O the binding of the substrate depends on the shape of the active site; some enzymes change their structure when activators bind to the enzyme; O substrate binding changes the shape of the enzyme's active site like Jimmy Fallon putting his "tight pants' on; O the active site creates a microenvironment ideal for the reaction; O similar to what occurs at your weekend party when you over-indulge.
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 site
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.
Indicate whether each of the following statements about an enzyme active site is true or false. It is the location where substrate molecules are produced. It always has a fixed, rigid geometry. It always has a geometrical shape exactly complementary to that of substrate. It always accommodates several structurally related substrates. It is the location where substrate molecules are converted to product molecules. It always has a shape that has a degree of flexibility to it. It always accommodates only one specific substrate.
Which of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active site
The classic concept of bond strain is more correctly described in what way? Select the correct response: The transfer of electron from one chemical moiety to another results to decrease in steric hindrance. The chemical bonds of the substrate is distorted due to the presence of metal ions in the vicinity of the active site. The transition state makes better contact with the enzyme than the substrate due to stabilization effect of various moieties in the active site. The electron cloud of the substrate is polarized by more electronegative moieties in the active site.
8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.
Competitive inhibitors have been developed as pharmaceuticals are not naturally occurring must be identical in shape and charge to the enzyme's natural substrate prevent the enzyme from binding its natural target even in the presence of an excess of that natural target
Which statement is NOT completely true? O In the Induced-fit theory, the conformation of the active site changes to accommodate an incoming substrate. O A urease which hydrolyzes only urea is an example of an enzyme that exhibits relative specificity. O Cofactors that are organic also go by the name coenzymes O Many enzymes require a second substance present (cofactor) in order to be active. O Enzymes are protein based catalysts. O Enzymes are sensitive to heat and pH O Enzymes catalyze at their "active site". O Apoenzymes are inactive enzymes.
. To catalyze a biochemical reaction, an enzyme typically dissociates into additional reactant molecules, thereby increasing the геaction ratе decomposes and releases energy to increase the number of successful collisions between reactant molecules binds temporarily to reactant molecules to lower the activation energy of the reaction drives the reaction to completion by consuming byproducts of the reaction CLEAR ALL