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.)

Organic Chemistry
9th Edition
ISBN:9781305080485
Author:John E. McMurry
Publisher:John E. McMurry
Chapter26: Biomolecules: Amino Acids, Peptides, And Proteins
Section26.SE: Something Extra
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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.)
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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