the rate equation for the second order reaction of E and S is
what os the diffusion controlled limit in aqueous solution
Enzyme and substrate collides with each other in enzyme catalyzed reactions. The frequency of enzyme-substrate collision is in the range of for a second order enzyme catalyzed reaction.
The ratio of cannot be greater than for a second order reaction to form, which is diffusion-controlled limit.
For a second order reaction between an enzyme (E) and substrate (S) with following mechanism:
Here, and . Michaelis-Menton constantWhen then . The expression for becomes as follows:
The ratio is the second-order rate constant for the formation of .
Following are second rate constants in the given set of rate constants.
The diffusion-controlled limit in aqueous solution is .
Ans:The diffusion-controlled limit in aqueous solution is .
the rate equation for the second order reaction of E and S is what os the...
Calculate the diffusion coefficient for the protein cytochrome c in aqueous solution assuming sphericity and using the Stokes-Einstein equation at 25degree C. The hydrodynamic radius is R =19.0 Angstroms. The viscosity of water is 1.00 cP = 0.00100 kg/m-s. D_cytc =__m^2/s. If the critical reaction distance is the sum of their radii, what value is expected for the Smoluchowski theory second order rate constant for a diffusion controlled reaction between two cytochrome c's? k_d = Lmol^-1s^-1 What would be the...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A B. For substrate A, she determined 30 min that Km 3.0 HM and kcat Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A↽−−⇀B. For substrate A, she determined that ?m=2.5 μM and ?cat=35 min−1. Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows Michaelis–Menten kinetics. 1)...
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Submit The second order reaction A → Products takes 13.5 s for the concentration of A to decrease from 0.740 M to 0.245 M. What is the value of k for this reaction? M-1s-1 1 2 3 4 5 6 7 8 9 0 x 10
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Carbonic anhydrase (CA) has a 25,000-fold higher activity (kcat = 106 s-1) than orotidine monophosphate decarboxylase (OMPD) (kcat 40 s-1). However, OMPD provides more than a 1010 higher "rate acceleration" than CA (Table). Explain how this is possible. Catalytic proficiencies of some enzymes Catalytic Nonenzymatic rate Enzymatic rate constant constant (kn in s-1) (kcat/Am in M-1s-1) proficiency Carbonic anhydrase 7 x 106 10-1 7 X 107 Chymotrypsin 4 x 10-9 9 x 107 2 X 1016 2 x 106 Chorismate...