For nucleophilic attack on a carbonyl in the substrate,an enzyme uses the deprotonated thiolate ofcysteine. At pH 7.0, 9% of the enzyme is active, whichcorrelates with the ionization state of cysteine. If theratio of active to inactive enzyme is 1:10, what is thepka of the active site cysteine?а. 6.05. 6.5C. 7.0d. 7.5е. 8.0f. 8.5

The enzymes have an active site to which the substrate binds. The amino acid sequence at the active…

Answered: For nucleophilic attack on a carbonyl…

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter10: Reconstitution Of Powdered Drugs

Section: Chapter Questions

Problem 30SST

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Ethylene glycol (HO−CH2−CH2−OH) is a major component of antifreeze. In the body, it is first converted to HOOC−CHO (oxoethanoic acid) and then to HOOC−COOH (oxalic acid), which is toxic. What class of enzyme catalyzes both of the reactions of ethylene glycol? The treatment for the ingestion of ethylene glycol is an intravenous solution of ethanol. How might this help prevent toxic levels of oxalic acid in the body?
The pKa for histidine is pKa = 6.1 while that for cysteine is pKa = 8.0 2. Assume that both histidine and cysteine are catalytic groups for a particular enzyme. Assume also that the side chain of cysteine must be in the deprotonated form. Estimate the pH at which the catalytic activity of this enzyme is the maximum and sketch a pH-activity graph.
A particular reaction has a ΔG‡ of 37.0 kJ mol-1. In the presence of an enzyme, the same reaction has a ΔG‡ of 5.70 kJ mol-1. Calculate the value of ΔΔG‡ in kJ mol-1.
The free energy of hydrolysis for acetic anhydride is221.8 kJ/ mol. The conversion of ATP to ADP also involvesthe cleavage of an anhydride bond. Its free energy of hydrolysis is 230 kJ/ mol. Explain the difference in these values.
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The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.
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