Kinetic Parameters of Enzyme-Catalyzed ReactionsTABLE 12-1 The Values of KM, Keat, and Keat/KM for Some Enzymes and SubstratesEnzymeSubstrateKM (M)9.5 x 10-51.2 x 10-²2.6 x 10-22.5 x 10-24.4 x 10-18.8 x 10-26.6 x 10-4AcetylcholinesteraseCarbonic anhydraseCatalaseChymotrypsinFumaraseUreaseAcetylcholineCO₂HCO₁H₂O₂N-Acetylglycine ethyl esterN-Acetylvaline ethyl esterN-Acetyltyrosine ethyl esterFumarateMalateUrea5.0 x 10-62.5 x 10-52.5 x 10-2Keat (S-¹)1.4 x 1041.0 × 1064.0 × 1051.0 X 1075.1 x 10-21.7 × 10-11.9 X 10²8.0 x 10²9.0 × 10²1.0 X 104Keat/KM (M¹s¹)1.5 × 1088.3 x 1071.5 x 1074.0 X 1081.2 x 10-11.92.9 × 1051.6 × 1083.6 X 1074.0 X 105Which enzyme is the most catalytically efficient?Which substrate does chymotrypsin bind to most tightly (assume k_₁ >> K₂)?Is fumarate or malate a better substrate of fumarase?Is it possible to have a kcat/KM of greater than 1 x 10⁹ M-¹ s-¹? Why or why not?

For a one-substrate enzyme catalyzed reaction, the Michaelis-Menton equation shows the quantitative…

Answered: Kinetic Parameters of Enzyme-Catalyzed…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter19: The Tricarboxylic Acid Cycle

Section: Chapter Questions

Problem 19P

See similar textbooks

Similar questions

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?
1. pH Effects a. In the enzyme mechanism of lysozyme, two acidic amino acid residues, Asp52 and Glu35, are critical for catalytic activity. If we assume normal side chain pKa values for Asp (pKar = 3.90) and for Glu (pKar = 4.07), what proportion of enzyme molecules will have both Asp52 and Glu35 in the correct ionization state at pH 5.0 (the pH optimum for lysozyme)? b. Are the traditional pKa values likely to be correct within the protein? What pKa changes might be present within lysozyme?
6-25 substrate-band enzyme concentrations. The the turnover number is equal to umax- b) V=Umax •57(Km+S) anstont For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM C) d) e) [S] = 0.5KM [S] = = 0.1KM [S] = 2KM [S] = 10KM w reactores -maximumrate of reaction boteles conc. Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?
BSC1010C Enzymes & Cellular Regulation Dr. Harris Amylase is an enzyme found primarily in saliva and pancreatic secretions. It catalyzes the breakdown of starch into sugars. A Rate of reaction 0 20 60 40 Temperature, C C Rate of reaction 80 100 B Rate of reaction Enzyme concentration (Substrate concentration always in excess) Substrate concentration (Enzyme concentration constant) The above graphs (A, B & C) provide data on several factors that affect the activity and function of amylase in living organisms. 11. What variables are compared in graph A? What information can be obtained from this data?
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
Calculcate Kcat for PNP substrate for both enzyme concentrations. enzyme volume: 20 ul Bovine Intensince Alkaline phosphatase molecular weight: 140,000 Bovine intenstine Alkaline phosphatase activity: 300 units/ml and 14 units/mg extinction coefficient PNP: 18.5 abs (mM-1 cm-1) Vmax: 0.332 moles/sec a) enzyme 1 concentration: undiluted b) enzyme 2 concentration: 1:1 dilution
ACTIVITY 6.3.1 Complete the table Polysaccharide Chondroitin Heparin Hyaluronate Dermatan Sulfate Keratan Sulfate Mucin Unique Feature Important Function
Velocity (mmol/minute) [S], (mM) No inhibitor Inhibitor 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8 The kinetics of an enzyme are measured as a function of substrate in the presence and the in absence of 2mM inhibitor (I). What are the values of Vmax and KM in the absence of inhibitor? In its presence? In its presence? What is the type of inhibition?
Case Study: Enzyme Kinetics Data for new statin drug (inhibits HMG CoA reductase): ● ● I Substrate (UM) 0.5 1.0 1.5 2.5 3.5 || Rate of reaction (mm/min) 23.5 32.2 36.9 41.8 44 What are the Kms of the uninhibited and inhibited reactions? Rate of reaction in presence of 5.0 nM statin Using the above date, create a double-reciprocal (Lineweaver Burk) plot. What type of inhibition is shown by the new statin? What are the Vmax of the uninhibited and inhibited reactions? 16.67 25.25 30.49 37.04 38.91
What is the Vmax of an enzyme at 1 μM with -4G RT k = 6.2x 10¹2 s-1 (Ideal gas constant R = 8.314 J K-1 mol-1) cat 0.14 μM S-1 1.4 µM s-1 14 μM s-1 0.14 mM s-1 1.4 mM s-1 activation energy (AG) of 55000 J/mol at 298K?
Enzyme Kinetics question Enzyme used is 10uL of a 10 ng/uL solution to a reaction mix in a final volume of 2.0 mL. (Enzyme used is 20kDa monomeric enzyme if matters) Based off lineweaver burk where 300 uM of inhibitor is used noninhibited formula is y= 4x + 0.1 (x axis is 1/S 1/mM) (y axis is 1/Vo sec/mM) inhibited formula is y = 4x + 1 I found Km as 1 mM for inhibited Vmax as 1mM/sec for inhibited How would I find Kcat? How would I find Ki?
Substrate KM (M) N-Acetylvaline ethyl ether 8.8 X 10 -2 N-Acetyltyrosine ethyl ether 6.6 X 10-4 Which substrate has the higher apparent affinity for the enzyme? Explain. Which substrate is likely to give a higher value for Vmax?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

3-2-1 Code It

Biology

ISBN:

9781337660549

Author:

GREEN

Publisher:

Cengage

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

3-2-1 Code It

Biology

ISBN:

9781337660549

Author:

GREEN

Publisher:

Cengage

SEE MORE TEXTBOOKS