Guide to Media Resources xix
Chapter
Media Type
Title
Text Reference
Page
13 Introduction
to Enzymes
Animated Figure
Kinemage Exercise
The rate of the reaction catalyzed by ATCase as a
function of aspartate concentration
11-1. Structure of ATCase
Figure 13-5
475
Figure 13-7,
13-9
476,
478
Kinemage Exercise
11-2. Conformational changes in ATCase
Figure 13-9
478
Animated Figure
Progress curves for the components of a simple
Michaelis–Menten reaction
Figure 14-7
488
Animated Figure
Lineweaver–Burk plot of the competitively inhibited
Michaelis–Menten enzyme described by Fig. 14-11
Figure 14-12
494
Animated Figure
Lineweaver–Burk plot of a simple Michaelis–Menten
enzyme in the presence of uncompetitive inhibitor
Figure 14-13
495
Animated Figure
Lineweaver–Burk plot of a simple Michaelis–Menten
enzyme in the presence of a mixed inhibitor
Figure 14-14
496
Interactive Exercise
6. HEW lysozyme in complex with (NAG)
6
Figure 15-10
518
Animated Figure
A double-reciprocal (Lineweaver–Burk) plot
Figure 14-9
490
Animated Figure
Plot of the initial velocity v
o
of a simple
Michaelis–Menten reaction versus the substrate
concentration [S]
Figure 14-8
489
14 Rates of
Enzymatic
Reactions
Guided Exploration
12: Michaelis–Menten kinetics, Lineweaver-Burk
plots, and enzyme inhibition
Section 14-2
487
Animated Figure
Reaction coordinate diagrams for a hypothetical
enzymatically catalyzed reaction involving a
single substrate (blue) and the corresponding
uncatalyzed reaction (red)
Figure 15-7
516
15 Enzymatic
Catalysis
Interactive Exercise
3. Human carbonic anhydrase
Figure 15-5
512
Kinemage Exercise
9. Lysozyme
Figure 15-10,
15-12, 15-14,
518,
519,
521
Animated Figure
Chair and half-chair conformations
Figure 15-11
519
Kinemage Exercise
10-1. Structural overview of a trypsin/inhibitor
complex
Figure 15-19
528
Guided Exploration
12:The catalytic mechanism of serine proteases
Section 15-3C
531
Kinemage Exercise
10-2. Evolutionary comparison of trypsin,
chymotrypsin, and subtilisin
Figure 15-22
531
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