ENZYME KINETICS A MODERN APPROACH – PART 5 pptx
ENZYME KINETICS A MODERN APPROACH – PART 5 pptx
... cooperativity, which can have noninteger values.
Estimates of the parameters k
and n are obtained using standard non-
linear regression procedures available in most modern graphical software
packages. ... as
v
V
max
=
[B]
K
+ [B]
(7.12)
where
V
max
=
V
max
[A]
K
BA
+ [A]
(7.13)
and
K
=
K
A
s
K
AB
+ K
AB
[A]
K
BA
+ [A]
=
K
AB
(K
A
s
+ [A] )
K
BA
+ [A]
(7.14)
From determi...
ENZYME KINETICS A MODERN APPROACH – PART 2 pptx
... hydroxyl ion–catalyzed reaction, k
HA
is the rate constant
for the undissociated acid-catalyzed reaction, and k
A
−
is the rate constant
for the conjugate base–catalyzed reaction.
32 TOOLS AND TECHNIQUES ... TOOLS AND TECHNIQUES OF KINETIC ANALYSIS
1.4 ACID–BASE CHEMICAL CATALYSIS
Many homogeneous reactions in solution are catalyzed by acids and bases.
ABr
¨
onsted acid is a proton donor,...
ENZYME KINETICS A MODERN APPROACH – PART 4 pptx
... the
comparison of two values, a two-tailed t -test is appropriate. When more
than two values are compared, a one-way analysis of variance (ANOVA),
TABLE 4.2 Rate of Hydration of Fumarate to Malate ... V
∗
max
and K
∗
s
correspond, respectively, to apparent enzyme maxi-
mum velocity and apparent enzyme substrate dissociation constant at a
particular pH. For the model above, V
∗
max
=...
ENZYME KINETICS A MODERN APPROACH – PART 6 pptx
... exponential term, and the shape of the
curve approaches that of a straight line. Valuable information can be
gained from analysis of the early and late stages of this reaction.
11.2.1 Early Stages ... plot for an interfa-
cial enzyme.
various parameters in Eq. (10.9) on the velocity of a reaction catalyzed
by an interfacial enzyme. As the enzyme interface dissociation constant
increas...
ENZYME KINETICS A MODERN APPROACH – PART 1 pps
... call 1-800-CALL-WILEY.
Library of Congress Cataloging-in-Publication Data:
Marangoni, Alejandro G., 19 65-
Enzyme kinetics : a modern approach / Alejandro G. Marangoni.
p. ; cm.
ISBN 0-471- 159 85- 9 ... V
max
/52
3.4 Practical Example / 53
3 .5 Determination of Enzyme Catalytic Parameters
from the Progress Curve / 58
ENZYME KINETICS
A Modern Approach
ALEJANDRO G....
ENZYME KINETICS A MODERN APPROACH – PART 3 pps
... scattered randomly about zero. A large positive value of the
SCC is indicative of a systematic deviation of the model from the data.
PRACTICAL EXAMPLE 55
TABLE 3.2 Average and Standard Deviation ... derivation
of an enzyme catalysis model. A steady-state approximation can also be
used to obtain the rate equation for an enzyme- catalyzed reaction.
3.2.2 Steady-State Model
The main a...
ENZYME KINETICS A MODERN APPROACH – PART 7 ppsx
... reaction
TABLE 12.1 Relative Activity of Two Enzymes as a
Function of Temperature
Temperature
(
◦
C) Enzyme 1 Enzyme 2
10 25 10
15 37 .5 15
20 50 20
25 75 25
30 100 30
35 100 50
40 95 75
45 85 ... the
kinetic characterization of enzyme stability.
150 CHARACTERIZATION OF ENZYME STABILITY
Alternatively, S
◦
D
could be calculated from knowledge of G
◦
D
at a
part...
ENZYME KINETICS A MODERN APPROACH – PART 8 ppt
... K
i
of an alter-
nate substrate. Addition of an alternate substrate inhibitor to an enzyme
assay results in an exponential decrease in rate to some final steady-
state turnover of substrate (Fig. ... 1.7 ±0 .5. The
partition ratio was also determined from the ratio of rates: k
3
/k
4
= 1 .5.
That the inactivation was active-site directed was also established in
several ways. As mentioned ab...
ENZYME KINETICS A MODERN APPROACH – PART 9 docx
... than either valine
and serine mutants, which had comparable catalytic constants. Compared
to valine and serine, alanine has the smallest van der Waals volume and
accessible surface area. Therefore, ... mean of a minimum of two deter-
minations ± standard deviation.
b
ss1, substrate consisting of the peptide lysine–proline–alanine–glutamic acid–phenylalanine–
phenylalanine (NO
2
)–alanine–le...
ENZYME KINETICS A MODERN APPROACH – PART 10 pps
... enzymes, 14 0–1 57 , 20 5 2 12
Standard-state enthalpy of denaturation,
14 7–1 50 , 155
Standard-state entropy of denaturation,
14 7–1 50 , 155
Standard-state free energy of denaturation,
14 7–1 50
Standard-state ... entries
acid–base, 2 0–2 3
enzyme, 4 1–4 3, 4 8 5 2, 5 2 5 3
in mechanism-based inhibition, 15 8–1 59
models of, 4 8 5 2
pH dependence of, 7 9–8 9
pr...
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