D What substrate concentration yields Vo=0.5*Vmax? O [S]-3 KM O [S]-4 KM O [S]-KM O [S]=2*KM Question 2 The KM and keat values have been measured for two substrates of aspartate carbamoyltransferase: Substrate A: KM= 3.8 M and keat = 16 s¹ Substrate B: KM-0.9 M and keat = 24 s¹ For which substrate does aspartate carbamoyltransferase have the highest specificity? substrate B O substrate A

D What substrate concentration yields Vo=0.5Vmax? O [S]-3 KM O [S]-4 KM O [S]-KM O [S]=2KM Question 2 The KM and keat values have been measured for two substrates of aspartate carbamoyltransferase: Substrate A: KM= 3.8 M and keat = 16 s¹ Substrate B: KM-0.9 M and keat = 24 s¹ For which substrate does aspartate carbamoyltransferase have the highest specificity? substrate B O substrate A

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter23: Enzymes

Section: Chapter Questions

Problem 23.15P: 5 At a very low concentration of a certain substrate, we find that when the substrate concentration...

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Enzyme X can act on either substrate A or B; the Km on A < Km on B. Vmax for A > Vmax on B.Sketch 1 plot for 1/v vs. 1/[S] plot for Enzyme X in the presence of A and in the presence of B.
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5 At a very low concentration of a certain substrate, we find that when the substrate concentration doubles, the rate of the enzyme-catalyzed reaction also doubles. Would you expect the same finding at a very high substrate concentration? Explain.
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0 Explain the relationship between transition-state analogs and abzymes.