What is the catalytic efficiency of Catalase ?Table. The values of KM and kcat for some Enzymes and SubstratesEnzymeCarbonic anhydraseSubstrateCO2HCO3KM (M)1.2 x 10-22.6 x 10-2Kcat (s-1)1.0 x 1064.0 x 105CatalaseH2O22.5 x 10-21.0 x 107UreaseUrea2.5 x 10-24.0 x 105O A. 4 x 108 M-s-1O B. 4 x 108 M-1.s-1OC25x 10-9 M-s1D. 2.5 x 102 M-1.s-1OE 1.0 x 107 s1

Enzymes are the catalytic molecules that are used to i ncrease the speed of the chemical reaction.…

Answered: What is the catalytic efficiency 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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Fozyme Action: An Investigation of Lactase Activity 137 PART F EFFECT OF pH ON ENZYME ACTIVITY Activity of Lactaid at Several pls Observation with Tes Tape" Glucose present? Lactose 90 change More Grean tello Green Hellow NO change Green NO pH 7 Yes, 100 mgloL pH 2 Yes 7100 mglaL pH 10 NO Glucose tes 300 mglaL RART G. EFFECT OF AN INHIBITOR ON ENZYME ACTIVITY Inhibitor Effects Observation with Tes Tape Glucose present? Light Green Teal Yellow IGreen Dark Brown Lactose Yes Lactaid" NO Ethanol Yes Yes Glucose 1. What is the optimum pH of the lactose-conversion reaction, as shown by your data? 2 Did ethanol act as an efficient inhibitor of the lactose conversion to glucose and galactose? 3. Summarize your findings about the concentration, temperature, and pH sensititivity of lactase.
please include all data in answer set
a 2D gel electrophoresis was done on the proteins found in the chart. create a chart with the correct parameters on both dimensions using 1-6 to indicate the position of each protein on teh 2D gel.
Comparison between simple enzymes and complex enzymes. In the table are the characteristics for comparison. I guessed a few of them (added a check mark)
KINETIC CONSTANT No Na2HPO4 25mM Na2HPO4 50mM Na2HPO4 Vmax nmol p-NP. Min- 20.3252 14.30615 17.30104 Km mM -0.819106 -0.46495 -0.352941 1. What does this suggest about the structure of the active side of the enzyme?
I only need a
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
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
4
The glyceraldehyde-3-phosphate dehydrogenase reaction of glycolysis, (glyceraldehyde-3- phosphate → 1,3 bisphosphoglycerate) (Choose all that apply) O conserves energy by transfer of a proton H* to NAD+ forming NADH O has a high energy thioester intermediate on the enzyme/substrate complex O mechanistically uses covalent catalysis O conserves energy in the formation of a oxygen phosphoric ester O conserves energy in the formation of a carboxylic-phosphoric mixed anhydride O mechanistically requires the coenzyme thiamine pyrophosphate (TPP) to act as an electron sink
This is for an ungraded practice exam which I would like to know the reasoning behind
With a ∆G°´ of -16.7 kJ/mol, the reaction catalyzed by hexokinase is considered to be _____. at equilibrium substrate and product concentration dependent freely reversible metabolically irreversible none of the above

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