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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The production of ATP (cellular respiration) is actually a(n) rxn. However, the reaction requires the of Glucose. A. catabolic : anabolism B. anabolic : catabolism C. exergonic : endergonic conversion D. hydrolytic : dehydration
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
Sketch the arrow pushing mechanism for the acid base catalyzed formation of phospho-serine from protein kinase a. You may shorthand the emzyme, the ribose and the adenine ring in ATP
Name the isoform of hexokinase enzyme in human and explain the role in carbohydrate metabolism.
This enzyme, dehydrogenase, belongs to the following group of EC number: O a. EC1: Oxidoreductase O b. EC2: Transferase Oc. EC3: Hydrolase O d. EC4: Lyase
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 electron carriers are in the reduced form? Note - there may be more than one. A. FAD B. FADH2 C. NAD+ D. NADH E. NADP+
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
Looking at the image shown here, which of the following statements DOES NOT correctly identifies the location of metabolites related to photosynthesis and/or respiration in the diagram of Chlamydomonas? F G H O A. Fermentation occurs in D. B. Glyceraldehyde-3-phosphate (G3P) is generated in C. O C. ATP can be found in D. D. Pyruvate is generated in G. O O O
Why does the velocity reach a plateau (asymptote) at high substrate concentrations? a. At high substrate concentrations, the product becomes an inhibitor of the reaction that created it. b. At high substrate concentrations, all enzymes are saturated with substrates. c. At high substrate concentrations, all substrates have been converted to products. d. At high substrate concentrations, the product concentration is high and the reaction starts running in reverse.
Consider the function of the cofactor FAD. Which of the following makes it unique (different) from NAD+? Select all that apply. a. Can facilitate single electron transfers b. Is associated with an enzyme and not a mobile electron carrier c. Serves to facilitate redox reactions d. s an electron carrier in the TCA cycle
Which of the following enzymatic regulation mechanisms involves direct interaction between substrate and enzymatic active site? Select one: O A. Allosteric activation O B. Noncompetitive inhibition O C. Feedback inhibition O D. Cooperativity OE. Allosteric inhibition

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