In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher    lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.

Biochemistry
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Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme).

Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher    lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.

CH2OPI
C=NH-
CH2OPI
229
NH,-Lys
H20
229
C=0
-Lys
но-с-н
но-с-н
33
Asp
H-C2o-H
H-C-OH
ČH2OPI
Н-с-о-н
„Asp
33
Schif Base
Formation
H-C-OH
ČH2OPI
Fructose 1,6-bisphosphate
Transcribed Image Text:CH2OPI C=NH- CH2OPI 229 NH,-Lys H20 229 C=0 -Lys но-с-н но-с-н 33 Asp H-C2o-H H-C-OH ČH2OPI Н-с-о-н „Asp 33 Schif Base Formation H-C-OH ČH2OPI Fructose 1,6-bisphosphate
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