For the equation of competitive inhibition: v= V max [ S ] α K m + [ S ] a) The value of α can ever be less than 1 is to be determined. b) The consequence for the value of α less than 1 is to be explained. Introduction: In the process of competitive inhibition, the inhibitor competes with the substrate for the substrate-binding site of the enzyme. This is because the binding of the substrate and the inhibitor occurs at identical sites. The inhibitor is structurally similar to the substrate. The net result is that the enzyme binds indiscriminately with the inhibitor and is not available to the substrate.

Question

Want to see the full answer?

Answer 1

Question

Chapter 6, Problem 81TQ

Summary Introduction

To review:

For the equation of competitive inhibition:

v=Vmax[S]αKm+[S]

a) The value of α can ever be less than 1 is to be determined.

b) The consequence for the value of α less than 1 is to be explained.

Introduction:

In the process of competitive inhibition, the inhibitor competes with the substrate for the substrate-binding site of the enzyme. This is because the binding of the substrate and the inhibitor occurs at identical sites. The inhibitor is structurally similar to the substrate. The net result is that the enzyme binds indiscriminately with the inhibitor and is not available to the substrate.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Students have asked these similar questions

The standard cost of Product B manufactured by Oriole Company includes 3.5 units of direct materials at $5.40 per unit. During June, 27,300 units of direct materials are purchased at a cost of $5.15 per unit, and 27,300 units of direct materials are used to produce 7,600 units of Product B. (a) Compute the total materials variance and the price and quantity variances. Total materials variance Materials price variance Materials quantity variance $ (b) Compute the total materials variance and the price and quantity variances, assuming the purchase price is $6.35 and the quantity purchased and used is 26,300 units. Total materials variance Materials price variance Materials quantity variance $

The pyruvate dehydrogenase complex catalyzes the oxidative decarboxylation of pyruvate to form acetyl CoA. E₁, E2, and E3 are abbreviations for the enzymes of the complex. Classify the enzyme names, prosthetic groups, and reactions as E1, E2, or E3. E₁ E2 Answer Bank E3 transfer of electrons to FAD and then to NAD+ transfer of acetyl group to coenzyme A formation of hydroxyethyl-TPP hydroxyethyl group transferred to lipoamide thiamine pyrophosphate (TPP) FAD lipoamide dihydrolipoyl transacetylase pyruvate dehydrogenase dihydrolipoyl dehydrogenase

Patients with pyruvate dehydrogenase deficiency show high levels of lactic acid in the blood. However, in some cases, treatment with dichloroacetate (DCA), which inhibits the kinase associated with the pyruvate dehydrogenase complex, lowers lactic acid levels. How does DCA act to stimulate pyruvate dehydrogenase activity? DCA activates pyruvate dehydrogenase kinase. DCA increases phosphorylation levels of pyruvate dehydrogenase. DCA inhibits pyruvate dehydrogenase kinase. ODCA activates pyruvate dehydrogenase phosphatase. What does this suggest about pyruvate dehydrogenase activity in patients who respond to DCA? The pyruvate dehydrogenase complex is active only when phosphorylated by the kinase. The pyruvate dehydrogenase complex is active only in the presence of the kinase. The pyruvate dehydrogenase complex is completely inactive. The pyruvate dehydrogenase complex displays some residual activity.