How does ATP regulate the activity of PFK-1?ATP binds to PFK-1 at the catalytic site as a competitive inhibitor, decreasing PFK-1 activity.ATP binds to the allosteric site as an inhibitor, decreasing PFK-1 activity.ATP binds to the catalytic site as a substrate, increasing PFK-1 activity.ATP binds to the allosteric site as an activator, increasing PFK-1 activity. The graph shows the effect of ATP on the allosteric enzyme phosphofructokinase-1 (PFK-1).PFK-1 activity (% of Vmax)100806040200Low[ADP][ATP]High[ADP]For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but thereis a point beyond which increasing the concentration of ATP inhibits the enzyme.

The enzyme phosphofructokinase 1 (PFK-1) catalyzes the following reaction: Fructose 6-P + ATP –>…

Answered: How does ATP regulate the activity of…

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 specialized lysine-linked co-enzyme often participates in the transfer of carbon fragments within an enzyme complex. Which group of three enzymes below make use of lysine-linked co-enztmes. Pyruvate dehydrogenase complex, a-Ketoglutarate dehydrogenase complex, NADH-Q oxidoreductase Pyruvate dehydrogenase complex, Succinate-Q oxidoreductase, Pyruvate carboxylase Pyruvate dehydrogenase complex, a-Ketoglutarate dehydrogenase complex, Pyruvate carboxylase Pyruvate dehydrogenase complex, Succinate-Q oxidoreductase, NADH-Qoxidoreductase Coordinate regulation occurs when different metabolic pathways are impact by a common compound. Which molecules below are compounds of coordinated regulation? Acety-CoA Molecular oxygen ATP NADH
Choose the conditions that are expected to INCREASE the rate of an enzymatic reaction add more enzyme add a non-competitive inhibitor add more substrate add an allosteric inhibitor adjust pH to optimal level
Succinate dehydrogenase is a/an Select the correct response: Oxidoreductase isomerase hydrolase transferase lyase ligase
How come high levels of NADH indicate reduced coenzymes rather than oxidized coenzymes? Isn't pyruvate oxidized by the reduction of NAD+ to NADH? Why is the answer reduced then?
The effectiveness of allosteric effectors in regulating metabolic pathways is based on their ability to— interact with multiple substrate-binding sites on the target enzyme(s). interfere with competitive inhibitors. alter the concentration of the target enzyme(s). denature the target enzyme(s). change the conformation of the target enzyme(s).
. Heterotrophic eukaryotes generate exactly how many of the following product molecules, in the consumption of one molecule of glucose, during aerobic respiration? twelve C6H12O6 molecules, six H2O molecules, and three CO2 molecules are produced twelve H2O molecules and six CO2 molecules are produced six C6H12O6 molecules, three H2O molecules, and six CO2 molecules are produced six H2O molecules and twelve CO2 molecules are produced one C6H12O6 molecule, one H2O molecule, and two CO2 molecules are produced
Which statement on the biosynthesis of cannabinoids is NOT TRUE? Select one: O a. Geranyl pyrophosphate is formed as a precursor via the deoxyxylulose pathway in cannabis O b. Divarinic acid is the precursor for the production of propyl cannabinoid acids. O C. When prenyl-transferase enzyme uses olivetolic acid as substrate cannabigerivarinic acid (CBGVA) is formed. O d. THCA-synthase, CBDA-synthase, and CBC- synthase enzymes can use both CBGA and GBGVA as substrate.
How could a competitive inhibitor enhance the rate of the ATCase reaction?
Which of the following are examples of cofactors? Select all that apply. Fe²+ Carbon FADH₂ Zn²+ NADH
Which of the following statements regarding the active site of cytochrome P450s is correct? Cytochrome P450-catalyzed monooxygenation proceeds with low stereoselectivity Cytochrome P450-catalyzed monooxygenation requires two electrons supplied by the redox process involving NADPH and NADP+. The 5th distal position (below the plane of the porphyrin ring) in cytochrome P450 is always occupied by His Cytochrome P450 is responsible for the metabolism of the minority of prescription drugs Cytochrome P450 contains manganese
The cytochrome P450 family of monooxygenase enzymes are involved in the clearance of drugs/medications from our body. Many adverse drug -drug interactions are known to occur as a result of interaction with the cytochrome P450 enzymes. A large number of drugs are metabolized by the enzyme P450 3A4. Human P450 3A4 is known to metabolize midazolam, a sedative, to a hydroxylated product, 1'- hydroxymidazolam. The kinetic data shown below are for the reaction catalyzed by P450 3A4. a. Focusing on the first 2 columns, determine the Km and Vmax for the P450 3A4 enzyme. b. Ketoconazole, an antifungal drug, is known to cause adverse drug interactions when taken along with midazolam. Using the data in the table, determine the type of inhibition caused by ketoconazole. Explain how you arrived at your answer. Midazolam (uM) 00 AN1 2 14 8 Rate of product formation (pmol min-1) 100 156 222 323 Rate of product formation in presence of ketoconazole pmol min-1) 11 18 27 40
Which of the following statements best explains why the activity of ATP-citrate lyase and malic enzyme are often paired together? The use of ATP by ATP-citrate lyase means that NADH needs to be regenerated cytosolically so that more ATP can be generated via shuttle systems and replace the ATP used by ATP-citrate lyase ATP-citrate lyase produces ATP and malic enzyme produces NADPH, both needed in the fatty acid biosynthetic pathway The activity of ATP-citrate lyase and malic enzyme never are correlated, they always function in different realms of metabolism The generation of acetyl CoA is a substrate for fatty acid synthesis in the cytosol and NADPH is generated as the anabolic electron carrier

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