Question 14We can measure the rate of reaction for some dehydrogenases by measuring changes in the absortance of the teaction miure at 340nm in a spectrophotometer What molecule s changing m absorbiance in this teachonOa ghicoseO FADOc hexekinaseONADHAMoving to another question will cave this response

When light passes through a sample solution, it is absorbed by the sample and measured by a…

Answered: Question 14 We can measure the rate 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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Question 10 Match the enzyme and the phrase that carresponds to it v used during strenuous exercise to regenerate NAD+ A aicohol denydrogenasa v converts pyuvate (a molecule with 3 carbars) to acelaldehyde (a molecule with 2 cartions) B. hexokanase v reduces acetaldehyde to ethanol using NADH C. decartoxylase v phosphoryiates the 6-carbon sugar mannose o.lactate delydrugenase A Moving to another question wel save this response.
QUESTION 3 In a spontaneous reaction O A. the total amount of energy in the reacting system increases O B. the total amount of energy in the reacting system decreases O C. More energy is created than is used O D. free energy of the reactants is greater than the free energy of the products E. free energy of the products is greater than the free energy of the reactants QUESTION 4 Coupling 2 reactions O A. makes the non spontaneous reaction become spontaneous B. pairs an endergonic reaction with an exergonic reaction C. allows for a series of reactions to have a net positive delta G D.A and B OE. A and B and C QUESTION 5 Breaking down glucose in cellular respiration O A. allows the cell to make energy B. transforms energy from the chemical bonds of glucose C. is a catabolic reaction O D.A and B O E. B and C
Question 13 Which of the following is the correct structure of the tripeptide Gly-Phe-Ala? a. H-N. Ph H. N. b. HN OH с. H,N. Ph d. OH но Ph NH, O a O b O d * Previous ASSIFICATION OF AMINO ACOS perbes, tis ed on the in chemican VE CLASS CLASSIFI tende nd the LG their co0 useful POLARITY of their R polar, aliphatic R group R group R ter at biological pH, near pH 7.0). ged R group d(basic) Rgroup cidic) Rgroup saov OM HHHIN
QUESTION 3 Semipermeable menbra Salt olecules Woter Mevemant of weter melendes Equel "concentretin" of weter In this figure, you can see water moving from one side of a semipermeable membrane in a beaker toward the other side. The side with only water is v to the side with salt. The side with salt is v to the side with only water. The side with salt is rising because water will move toward the hypotonic v side.
Question 11 The breakdown of large molecules by the enzymatic addition of water is an example of what kind of reaction? O 1. oxidation O 2. reduction O 3. condensation O 4. hydrolysis O 5. decarboxylation A Moving to another question will save this response. W AR SONY ASSIST BUtton, Onetouch
QUESTION 10 Which one of the following statements does NOT correctly describe the current state of the chymotrypsin-substrate complex below or the next mechanistic step that occurs? s,' G193 S195 NH NH R -NH R-NH HN- Ser-195 His-57 HN Asp-102 OA. This intermediate is part of a nucleophilic acyl substitution reaction. OB. In the next step His-57 protonates Ser-195. O C. In the next step His-57 activates a water molecule. O D. In the next step His-57 protonates the leaving group. OE. In the next step the N-terminal fragment of the original substrate departs.
QUESTION 18 Stable molecules that resemble the transition state of enzyme catalyzed reactions are very potent inhibitors. Provide an explanation as to why these compounds are better than inhibitors based on the substrate. TT TT Paragraph v v 3 (12pt) = - E · T Arial T T, O Mashups 66 HTHL CSS CS Scanned with CamScanner
QUESTION 2 Compound X is a potent competitive inhibitor of enzyme Y. Addition of 10 nM compound X increases the measured Km for enzyme Y by a factor of 3. What are the values for a and a' under these conditions? O a of 1 and a' of 3 a of 1/3 and a' of 1 O a of 1 and a' of 1/3 a of 3 and a' of 1 Show transcribed image text
Question 17 If glucose is labeled with 14C at its C6 position, where will the label appear in fructose 6-phosphate? Oa Ca Ob carbon that is connected to the phosphoryl group Oe C2 Od it will be released as carbon dioxide (CO2) AMoving to another question will save this respanse.
QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
QUESTION 6 In Proline racemase, two cysteines are positioned on opposite sides of the ring to add and remove protons This is an example of what type of enzyme mechanism? O transition state stabilization O general acid/base catalysis O nucleophilic intermediate O coenzymes / cofactors
QUESTION 38 In a 250µl reaction containing 0.3 nmol of a Michaelis enzyme with Km = 4.4 x 10 M and saturating substrate concentration, product was formed at an initial velocity of 6.3 x 10 M min-1. What is kcat for this enzyme? Give your answer in 3 sigfigs in scientific notation, for example 1.20 e -3 Click Save and Submit to save and submit. Click Save All Answers to save all answers. O Type here to search 78°F Mostly cloudy End 4) DII PrtScn F8 Home F9 F6 F2 F3 F4 *- & 7 8. 4. #3

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