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Enzyme

• Globular Proteins
• Biological Catalyst

1. Substrate
2. Enzyme-Substrate Complex
3. Product
4. Active Site
5. Substrate Binding Site
6. Allosteric Site
7. Apoenzyme/Holoenzyme
8. Coenzymes/Cofactors
9. Zymogens
10. Isozymes
11. Lock and Key-Model
12. Induced-Fit Model

The Response of Enzymatic Activity to

Enzymatic Activity is Strongly Influenced by pH
Temperature is Complex

Optimum pH Optimum Temperature

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1. Oxidoreductases acetaldehyde + NADH ethanol + NAD+

2. Transferases
Glucose + ATP glucose 6-P + ADP
3. Hydrolases triglycerides + H2O fatty acid + glycerol

4. Lyases

5. Isomerases

6. Ligases

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Linear Plots

The Lineweaver-Burk double-

reciprocal plot.

Other Linear Plots
• Eadie-Hostee Plot
• Hanes-Woolf Plot
• Cornish-Bowden Plot
Enzyme Inhibitors
• Enzymes may be inhibited reversibly or
irreversibly
• Reversible inhibitors may bind at the active
site or at some other site
• Enzymes may also be inhibited in an
irreversible manner

Irreversible Inhibitors

Penicillin is an irreversible
inhibitor of the enzyme
glycoprotein peptidease,
which catalyzes an
essential step in bacterial
cell all synthesis.

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Reversible Inhibitors May Bind at the Active Site

or at Some Other Site
Reversible Inhibitors
• Competitive
• Non-competitive
• Uncompetitive

Competitive Inhibitors Compete With Substrate for Succinate Dehydrogenase – a Classic Example
the Same Site on the Enzyme of Competitive Inhibition

Figure 13.13 Lineweaver-Burk plot of competitive inhibition,

showing lines for no I, [I], and 2[I].

Figure 13.14 Structures of succinate, the substrate of succinate

dehydrogenase (SDH), and malonate, the competitive inhibitor.
Fumarate (the product of SDH) is also shown.

Pure Noncompetitive Inhibition – where S and I Mixed Noncompetitive Inhibition: binding of I by E

bind to different sites on the enzyme influences binding of S by E

Figure 13.15 Lineweaver-Burk plot of pure noncompetitive Figure 13.16 Lineweaver-Burk plot of mixed noncompetitive
inhibition. Note that I does not alter Km but that it decreases inhibition. Note that both intercepts and the slope change in
Vmax. the presence of I.

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Uncompetitive Inhibition, where I combines only

with E, but not with ES
Are all enzymes proteins?

Figure 13.17 Lineweaver-Burk plot of

1)
uncompetitive inhibition. Note that
both intercepts change but the slope Ribozymes
(Km/Vmax) remains constant in the
presence of I.

2) Abzymes
Science, Vol. 269, pages 1835-
1842 (1995)

RNA Molecules That Are Catalytic Have

Antibody Molecules Can Have Catalytic Activity
Been Termed Ribozymes

Figure 13.28 (a) Intramolecular hydrolysis of a hydroxy ester

yields a -lactone.

(b) The cyclic

Figure 13.26 (a) The 50S subunit from H. marismortui. (b) The
phosphonate ester
aminoacyl-tRNA (yellow) and the peptidyl-tRNA (orange) in the
analog of the cyclic
peptidyl transferase active site.
transition state.