The enzyme that catalyzes the C-Cg bond cleavage reaction that converts serine to glycine removes the substituent (R) bonded to the a-carbon in the first step of the reaction. Starting with PLP bound to serine in an imine linkage, propose a mechanism for this reaction. (Hint: The first step involves removal of the proton from serine's OH group.)
The enzyme that catalyzes the C-Cg bond cleavage reaction that converts serine to glycine removes the substituent (R) bonded to the a-carbon in the first step of the reaction. Starting with PLP bound to serine in an imine linkage, propose a mechanism for this reaction. (Hint: The first step involves removal of the proton from serine's OH group.)
Chemistry
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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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Transcribed Image Text:The enzyme that catalyzes the C-Cg bond cleavage reaction that converts serine to glycine removes the
substituent (R) bonded to the a-carbon in the first step of the reaction. Starting with PLP bound to serine in
an imine linkage, propose a mechanism for this reaction. (Hint: The first step involves removal of the proton
from serine's OH group.)
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