Which of the following statements regarding the catalytic mechanism of superoxide dismutase istrue?The D residue does not participate in acid-base catalysis during the course of the catalyzedreactionAll of the answers are trueThe coordinated Zn2+ participates in stabilizing Cu²+ in the reduction-oxidation reactions toconsume O₂The Cu²+ coenzyme is coordinated by H residues, positioning it precisely for consumption of0₂The overall reaction consumes two equivalents of O₂ and two proton equivalents in order toproduces one equivalent H₂O2

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Answered: Which of the following statements…

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 Beutler test is used to diagnose GALT (UDP-glucose uridyltransferase) deficiency in infants. Blood from the heel is spotted onto filter paper and the spot is then subjected to an enzyme assay. Galactose 1-phosphate, NADP+ and UDP-glucose are added as substrates to the dried blood. The increase in absorbance at 340nm is measured over time which corresponds to reduction of NADP+ to NADPH . The amount of GALT activity in the blood of patients is therefore measured by stoichiometric relationship to the amount of NADPH produced from NADP+. However, GALT does not directly reduce NADP+ as you can see in the above diagram. Instead, the glucose 1-phosphate product from this reaction is shuttled into the oxidative phase of the pentose phosphate pathway by enzymes also present in RBCs. Which three (or possibly more if you must) enzymes downstream of GALT allow for quantitative correlation of a product of GALT with the appearance of NADPH? What is the stoichiometric relationship…
Order the cofactors based on their use in the mechanism of the a-etogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 2 3 4 answer choices: lipoamide, biotin, 2 Fe - 2S cluster, TPP, NAD+, FAD
The following nutrient molecule is digested and transported to a cell where it undergoes further catabolism: но c-(CH;)14-CH3 di In the table below, list the important products of the complete B oxidation of this molecule. • In the first column of the table, write the chemical formula, name, or standard biochemical symbol for a product molecule. In the second column, write the total number of these molecules produced. • Only list the Important products, including (1) molecules with any of the carbon atoms that were in the original molecule, (2) energy storage molecules (like ATP), and (3) newly oxidized or reduced coenzymes. List each product molecule on a separate row. You can add more rows if you need them. • Be sure you write the number of product molecules formed by the complete B oxidation of the molecule above. • Do not include the products of any catabolic activity that happens before or after B oxidation, including any necessary activation. If the molecule contains small parts…
The following diagram shows reaction curves for aspartate transcarbamoylase (ATCase) with carbamoylphosphate and different concentrations of aspartate, in the absence of ATP (curve 1) and presence of ATP (curve 2). What do the shapes of the curves tell us about the ATCase enzyme? 2 جر [aspartate] It binds substrate through a sequential mechanism. It binds substte cooperatively. It obeys Michaelis-Menten kinetics. It binds substrate through a concerted mechanism.
Which type of enzyme (Table) catalyzes the following (given) reactions?
Given the active site diagram below, indicate the mechanism(s) of catalysis. 5 HO OH HN OH ΝΗ *HN ΝΗ Zn²+ Acid-base, Metal ion 3 Metal ion, By Approximation Metal ion Acid-Base, By Approximation Acid-base
Which of the following statements is correct for the reaction catalyzed by chymotrypsin? ○ The substrate carbon atom bonded to Ser195 in the acyl enzyme intermediate has a tetrahedral geometry ○ The Ser195 hydroxyl oxygen atom is the catalytic nucleophile for the deacylation phase of the overall reaction mechanism ○ The oxyanion hole accelerates the reaction by tightly binding the substrate carbonyl oxygen at the peptide bond that is cleaved ○ Asp102 stabilizes the tautomeric state of the catalytic histidine ○ The first reaction product contains a proton derived from an active-site water molecule
If the allosteric coefficient for ATCase increases from 250 to 1300, the rate of the N-carbamoylaspartate formation: O stays the same and the sigmoidal curve of reaction rate as a function of substrate shifts up. O decreases and the sigmoidal curve of reaction rate as a function of substrate shifts to the left. O increases and the sigmoidal curve of reaction rate as a function of substrate shifts to the left. O stays the same and the sigmoidal curve of reaction rate as a function of substrate shifts to the right. O decreases and the sigmoidal curve of reaction rate as a function of substrate shifts to the right. Question 9 Which of the following CANNOT be targeted for phosphorylation to modulate the activity of an enzyme? O Ser Ala O None of the amino acids listed can be targeted for phosphorylation to modulate enzyme activity The Tyr
Consider the following reaction occurring at 298 K: OH CH₂OH OH -0. OH OH +ATP k₁ k₂ 0- OCH, OH OH 0 OH OH Glucose Glucose 6-phosphate Hexokinase is an enzyme that catalyzes this reaction. When the hexokinase is present the rate of k₁ is 1.3 X10-3 M-15-1 Calculate the activation energy for the hexokinase catalyzed forward reaction.. +ADP
The structure of a metalloenzyme active site is down below(black picture). Describe, from a chemical and structural perspective, how the reactive site is designed to facilitate its catalytic reaction. The example below suggests the level of detail that is required. Make sure that you explain what the metal is doing, what the reaction is, and its biological significance.
Which class of enzymes have sigmoid or S-shaped plots of the rate of a reaction, v, versus the substrate concentration, [S], instead of the hyperbolic curves of the Michaelis-Menten equation? transferases holoenzymes O hydrolases O allosteric enzymes O ribozymes
Enolase has a glutamic acid residue in its active site. Describe the experiment that was done that provided evidence for the proposed function of the glutamic acid residue in catalysis by enolase.

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