What is the role of the small organic non-proteincompounds called coenzymes?A. Coenzymes are receivers of hydrides transferred fromone substrate to be added to another substrate.B. Coenzymes are acceptors of groups from a donorsubstrate in transfer reactions.C. Coenzymes are electron acceptors during free-radicalreactions.D. Both A and BE. All of these

Enzymes are the biocatalyst that can increase the rate of biochemical reaction without itself being…

Answered: What is the role of the small organic…

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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A histidine was determined to be the critical residue involved in an enzyme-catalyzed reaction. If the pKa of the histidine is known to be 6.5 in the active site and the pH of maximum catalytic activity is 7.2, what is likely the primary role of histidine in the catalytic reaction? A. forms a covalent bond with the substrate B. reduces the entropy of the substrate C. stabilizes a charged intermediate D. acts as a proton donor Aspartate and lysine are in the active site of an enzyme. They are both known to participate directly in catalysis. The pKa's of the residues are found to be 3.2 and 9.6, respectively for aspartate and lysine. The optimum pH for the enzyme is 6.4. Which forms of these two residues will predominate when the enzyme is most active? A. aspartate is protonated; lysine is deprotonated B. both residues are deprotonated C. aspartate is deprotonated; lysine is protonated D. both residues are protonated
What are NADH and FADH2? a. Oxidized coenzymes which carry electrons b. energy-producing organelles c. short-term, socially popular sources of hydrogen gas d. Reduced coenzymes which carry electrons
Which of the following enzyme classes catalyze reactions in which two molecules become covalently linked to each other? A. Kinase B. Hydrolase C. Isomerase D. Ligase
One of the functions of the pentose phosphate pathway is to make NADPH, which plays important roles in many functions. Which of the following is NOT the function of NADPH? O a. O b. O C. O d. O e. ROS detoxification Biosynthesis of fatty acids Translation Biosynthesis of cholesterol Drug metabolism
Explain which of the following substances ATP, CoA-SH, FAD and NAD+ have the subunits in their structure? A.Have 2 two ribose subunits.
ATP inhibits glycolysis by binding to an allosteric site on the last enzyme In the pathway, thus ATP is a... A. Competitive inhibitor B. Noncompetitive inhibitor C. Feedback inhibitor D. More than one of these answers. Please give the rationale as to why
ATP is high-energy storage molecule in part because: A. Its hydrolysis results in separation of like charges. B. The hydrolysis reaction has a high activation energy.C. Its ribose is oxidized during the process, which is exergonic.D. It is very soluble.
The most direct method of phosphorylation is ________ phosphorylation. a. substrate-level b. oxidative c. reductive
what is the transmembrane protein responsible for ATP synthesis during both photosynthesis and cellular respiration? a. Na+/K+ ATPase b. SGLUT-1 c. ATP synthase d. carbonic anhydrase e. rubisco
Which of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that apply
enzymes which are produced in inactive form in the living cells are called a. coenzymes b. papain c. lysozymes d. apoenzymes e. proenzymes
Why does the substrate bind to the enzyme? 1. The shape of the active site fits the shape of the substrate 2. None are true 3. The shape of the reaction site fits the shape of the substrate 4. The shape of the allosteric site fits the shape of the substrate

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