Aspartate aminotransferase (AspAT) catalyzes the followingreaction:COONH3-CH-COO-a-Amino acidTAspATC=OCH₂CH₂COOa-Keto acidCOOAspartateOxaloacetateMutant AspAT enzyme was constructed. The kinetic parametersfor the wildtype enzyme and mutant enzyme are shown in thetable.KM Aspartate(mm)Enzymekcat (S-¹)4530Wild-type AspAT (Arg 292 Arg 386)Mutant AspAT (Lys 292 Arg 386)3264.5(a) Compare the ability of aspartate to bind to the wild-typeand mutant enzyme.(b) Evaluate the catalytic efficiency of the wild-type and mutantenzyme.

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Answered: (a) Compare the ability of aspartate to…

(a) Compare the ability of aspartate to bind to the wild-type and mutant enzyme. (b) Evaluate the catalytic efficiency of the wild-type and mutant enzyme.

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...

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Question

Aspartate aminotransferase (AspAT) catalyzes the following
reaction:
COO
NH3-CH-COO-
a-Amino acid
T
AspAT
C=O
CH₂
CH₂
COO
a-Keto acid
COO
Aspartate
Oxaloacetate
Mutant AspAT enzyme was constructed. The kinetic parameters
for the wildtype enzyme and mutant enzyme are shown in the
table.
KM Aspartate
(mm)
Enzyme
kcat (S-¹)
4
530
Wild-type AspAT (Arg 292 Arg 386)
Mutant AspAT (Lys 292 Arg 386)
326
4.5
(a) Compare the ability of aspartate to bind to the wild-type
and mutant enzyme.
(b) Evaluate the catalytic efficiency of the wild-type and mutant
enzyme.

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