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Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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due:substrate interaction and determinant of sub-
To identify the critical enzyme resi-
D(-2)
Arg47
strate specificity, steady-state kinetic studies have D(-4).
been carried out by site-specific mutagenesis of the
enzyme and by systematically changing amino acid
residues in the 11-amino acid phosphotyrosine con-
taining substrate that simulate residues 988 – 998
of the epidermal growth factor receptor
(EGFR988–998).
Asp48
E(-1)
A(-3)
The table below compares the kinetic parameters
of the wild type enzyme with phosphotyrosine pep-
tides in which amino acid residues are substituted.
In the adjacent diagram the structural interactions
L(+1)
Tyr46
Gln262
Y(0)
between active site residues are illustrated for the
first 6 residues of the substrate. Identify which sub-
strate residue is most sensitive to substitution and
Ser216
justify your conclusion on the basis of the kinetic
parameters. Is the decrease in kcat/ KM due to loss
of catalytic reactivity or due to suboptimal position-
ing of the phospho-Tyr residue in the active site?
Phe182
Asp181
PTP1B
Substrate
kcat
K.
kcat/Km
JUM
10-7 x (s-1 M1)
DADEPYLIPQQG
DADAPYLIPQQG
DAAEPYLIPQQG
AAAAPYLIPQQG
44.6 ± 1.8
39.8 + 0.32
3.9 + 0.9
13.7 + 0.46
1.1 + 0.25
0.29 + 0.01
35.3 + 0.22
6.6 ± 0.22
0.53 + 0.02
34.7 + 0.25
52.7 + 0.7
0.066 0.001"
Transcribed Image Text:(c) (
due:substrate interaction and determinant of sub-
To identify the critical enzyme resi-
D(-2)
Arg47
strate specificity, steady-state kinetic studies have D(-4).
been carried out by site-specific mutagenesis of the
enzyme and by systematically changing amino acid
residues in the 11-amino acid phosphotyrosine con-
taining substrate that simulate residues 988 – 998
of the epidermal growth factor receptor
(EGFR988–998).
Asp48
E(-1)
A(-3)
The table below compares the kinetic parameters
of the wild type enzyme with phosphotyrosine pep-
tides in which amino acid residues are substituted.
In the adjacent diagram the structural interactions
L(+1)
Tyr46
Gln262
Y(0)
between active site residues are illustrated for the
first 6 residues of the substrate. Identify which sub-
strate residue is most sensitive to substitution and
Ser216
justify your conclusion on the basis of the kinetic
parameters. Is the decrease in kcat/ KM due to loss
of catalytic reactivity or due to suboptimal position-
ing of the phospho-Tyr residue in the active site?
Phe182
Asp181
PTP1B
Substrate
kcat
K.
kcat/Km
JUM
10-7 x (s-1 M1)
DADEPYLIPQQG
DADAPYLIPQQG
DAAEPYLIPQQG
AAAAPYLIPQQG
44.6 ± 1.8
39.8 + 0.32
3.9 + 0.9
13.7 + 0.46
1.1 + 0.25
0.29 + 0.01
35.3 + 0.22
6.6 ± 0.22
0.53 + 0.02
34.7 + 0.25
52.7 + 0.7
0.066 0.001
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