Question 5 O coenzymeO holoenzymeO cofactorQUESTION 5The rate of a reaction, catalyzed by a Michaelis-Menten enzyme, was measured using several substrate concentrations that were much lower than Km. The dependence of reaction rate (velocity) at these lowsubstrate concentrations can best be described asO independent of substrate concentrationO equal to V maxO equal to KmO dependent on the overall free energy change of the reactionO proportional or dependent to the substrate concentrationQUESTION 6Which of the following reactions is correctly represented?C+DAG°- 13.6 kj/molABO A+BAG°= -16 4 kJ/molC+DOAB -AG°--17.8 kJ/molAG°- 0.0 k/molC+DClick Save and Submit to save and submit. Click Save All Answers to save all answers.acer

Enzymes are a class of proteins that serves as a biological catalyst during the chemical reactions…

Answered: QUESTION 5 The rate of a reaction,…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 12P

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when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.
126 nmol of enzyme catalyzes the conversion of 2.8 ugram of substrate (molar mass- 350 g/mol) in t second at 37C at Vman what is the turnover number kcat for the enzyme in units of s R Show all your work to recenve credit. For the toolbar, press ALTF10 (P) or ALTFNF10 (Mac). %3B .... BIUS Paragraph Arial 14px
Maximum velocity of an enzyme-catalyzed reaction dolgomsH 7 T (8 a. Is determined from the slope of the line of product formation zouza11 901 ml,0,.201 over time for a particular substrate concentration. vx011(e b. Is determined from reaction rate late in the reaction d c. Is the rate where addition of more substrate does not cause a rate increase. SO 121 91 to ydinitis of zomit 001 vainitts d. Changes with increases in substrate concentration (II Which of the following is not an assumption in Michaelis Mentens kinetics?91 21 noi to 926 v basylsts noitsbyri riguard (SE a. [ES]~ constant b. [E] >> [S] 00 to fu291 6 26 9022it ni[*] 92691 T (EI c. [E] << [S]gnul art ni a.. Hq o bot Hq edt 1swol in d. [S] + [ES] [Sbaid atidinni slusslom 398-E 900 T antern anibnid yd 29tie gnibnid
Catalane in un enzyme that speeds up the decomposition ot hydrogen peroxide H0) to waler and axvgen. Students conducted two investigationa to determine the ideal conditions for the function of catalane. One wetigation compared catalase activity at diferent values of pH. The other imvestigation compared catalane activity al diferent temperatures. Enayme Activity ve pH Enzyme Aetivity vs Temperature Teate C) According to the data in the graphs, which pH and temperature combination provides the BEST conditions for catalase to tunction? Anury lag a
1. A gluscose trasporter in teh liver cell binds with Km of 40mM. Calculate what fraction of vmax the Vo operating when blood glucose is 10mM 2. Draw a Michaelis-Menten kinetic curve and identify Vmax and Km. Indicate on the curve where the reaction is first order, where the reaction is zero order, where the reaction operates at half-saturation, and the range where most enzymes operate Be very clear about your labels.
The following data were obtained in a study of an enzyme that is known to follow the Michaelis-Menten kinetics. Approximately, what is the value of Km tor this enzyme? Substrate added, umol/L Vo uM/sec 48 97 175 187 192 197 2 16 100 1000 198 OA 1 uM O8.2 pM OC 4 uM. OD. 8 uM OE 16 IM OF 1000 uM OG 97 uM/sec OH 175 UM/sec
Select the incorrect statement. With regards to free energy ΔG of the reaction below E+S ⇌ ES Negative ΔG mean the reaction toward is facourable More negative value of ΔG indicates stronger binding to S to E It is possible to compute disassociation constant from the ΔG value alone It is possible to calculate the term ( ΔH – T ΔS) from the value of ΔGalone ΔG = 0 indicates (ES)/(E)(S) =1 None of the above
An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each substrate concentration. [S] = 1.75 mM MM-s-1 [S] = 7.50 mM [S] = 11.0 mM DO mM-s mM-s
What is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1
23. An important step in glycolysis is the formation of ATP and pyruvate from phosphoenol-pyruvate (PEP) and ADP. PEP ADP pyruvate+ATP The equilibrium constant (Keq) for this reaction is approximately 2.5x10°. Calculate standard free energy change (AG°') for this reaction. Show your work. onege b. Is the reaction exergonic or endergonic at standard conditions? If, at equilibrium, the concentrations of ADP and ATP are 0.2 mM and 2.0 mM, respectively, what is the equilibrium concentration ratio of [pyruvate] to [PEP]? Show your work. с.
An enzyme catalyzes a reaction with a Km of 7.50 mM and a Vmax of 2.90 mM - s-1. Calculate the reaction velocity, un, for each substrate concentration. [S] = 2.75 mM mM · s- * TOOLS x10 [S] = 7.50 mM mM · s-! [S] = 11.0 mM mM - s-
Given the conditions below A (Enz A)→ B-(Enz B) C (Enz C) D (Enz D) →E Enzyme Reaction Rate @ Q1o Reaction Rate at 20 C 30 C A 1.38 1.68 1.44 2.78 C 1.23 1.84 1.58 1.96 If tissue D exhibits a reaction rate of 1.58 umol CO2 gFW-1 hr-1 at 20 C and has a Q10 of 1.96, what is the reaction rate at 30 C?

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