The hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 umol of pyrophosphate in 15 minutes. The purified enzyme has a Vnax of 2800 U per milligram of enzyme. When (S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second? Vnax = umol -s. mg- If cach enzyme subunit has one active site, how many micromoles of active sites, or (E]r, are there in 1 mg of enzyme? (Er = umol - mg-

The hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 umol of pyrophosphate in 15 minutes. The purified enzyme has a Vnax of 2800 U per milligram of enzyme. When (S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second? Vnax = umol -s. mg- If cach enzyme subunit has one active site, how many micromoles of active sites, or (E]r, are there in 1 mg of enzyme? (Er = umol - mg-

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

Based on the following information for phosphoglucoisomerase, calculate the equilbrium constant and round to the nearest tenths place. R = 8.3145 J/mol⋅K ΔG∘’ = -14.2 kJ/mol
Consider a drug molecule that binds to an enzyme with a Kd of 20.281 nM. If the intracellular concentration of the free drug in a patient is 19.225 nM at equilibrium, what percentage of enzyme molecules are bound to the drug?
In this reaction does equilibrium favor the products or reactants? C6H5COOH + NaOH → (C6H5COONa) + H2O
In biological cells, the energy released by the oxidation of foods is stored in adenosine triphosphate (ATP or ATP4). The essence of ATP's action is its ability to lose its terminal phosphate group by hydrolysis and to form adenosine diphosphate (ADP or ADP³-) ATP+ (aq) + H₂0 (1)→ ADP³- (aq) + HPO¯(aq) + H₂O+ (aq) At physiological conditions, pH = 7 and T = 310K (blood temperature), the enthalpy and Gibbs energy of hydrolysis are A, H = -20 and AG = -31, respectively. The hydrolysis of 1.00 mol of ATP, at these conditions, results in the extraction of 31 kJ of energy that can be used to do non-expansion work such as the synthesis of proteins or activation of neurons. mol Calculate the entropy of hydrolysis at pH = 7 and T = 310K
And which reaction is nitrogen reduced
According to Le Chatelier’s Principle, does the following reaction shift towards reactants, towards products, or have no shift when carbon is removed from the following reaction? C(s) + CO2(g) ⇆ 2CO(g) + heat
Write the equilibrium-constant expression for the reaction shown in terms of [SO2], [CO2], [CS2], and [O2] 2SO2(g)+CO2(g)↽−−⇀CS2(g)+3O2(g) , which is sometimes symbolized as ?K or ?eqKeq, denotes that the equilibrium constant is expressed using molar concentrations. For this question, ?cKc means the same thing as ?K and ?eqKeq.
Name the substances that are produced by the complete hydrolysis of this substance
(a) The catalytic hydrogenation of CO2 to methanol is considered as a possible route for creating a circular fuel economy. Where would the CO, for this process come from? What is meant by the term 'circular economy’ within this context? Does the source of H2 for this process lead to a circular economy or not?
Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout, several medications are used to inhibit the activity of xanthine oxidase and reduce the production of uric acid. You are a biochemist and just discovered a chemical that can inhibit the activity of the human xanthine oxidase. When analyzing its mode of inhibition, you found that the enzyme inhibitor complex requires 450 J.mol-1 to dissociate and that it displays kinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministry of health for approval as a medication for gout. Based on the data provided, are they going to authorize it as a medication or not? Explain?
Coenzyme F430 is a nickel-containing tetrapyrrole that is required by methyl-coenzyme M reductase. It is one of a class of nickel chlorins found in nature. Each molecule of cofactor 430 contains 1 atom of nickel. By mass, nickel is 6.47 % of the molecular formula. What is the molar mass of Coenzyme F430?
Which statement does NOT apply to the lock-and-key theory? O explains the functioning of enzymes explains the need for a specific three dimensional structure found in proteins explains the reason why a particular enzyme is involved with one substrate explains why a substrate-enzyme complex is so difficult to separate