Clinical Enzymology 431

Prof. Fahad J. Al-Shammary

Introduction to Enzymes

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Summary

The General Characteristics of Enzymes. Enzymes are highly efficient protein

catalysts which are involved iii almost every biological reaction. They are often quite
specific in terms of the substance acted upon and the type of reaction catalyzed.

Enzyme Nomenclature and Classification. Enzymes are grouped into six major
classes on the basis of the type of reaction catalyzed. Common names for enzymes
often end in -ase and are based on the substrate and/or the type of reaction catalyzed.

Enzyme Cofactors. Cofactors are nonprotein molecules required for an enzyme to be

active. Cofactors are either organic (coenzymes) or inorganic ions.

Mechanism of Enzyme Action. The behavior of enzymes is explained by a theory in

which the formation of an enzyme-substrate complex is assumed to occur. The
specificity of enzymes is explained by the lock and key theory and the induced fit
theory.

Enzyme Activity. The catalytic ability of enzymes is described by turnover number

and enzyme international units. Experiments that measure enzyme activity are
referred to as enzyme assays.

Factors Affecting Enzyme Activity. The catalytic activity of enzymes is influenced

by numerous factors. The most important are substrate concentration, enzyme
concentration, temperature, and pH.

Enzyme Inhibition. Chemical substances called inhibitors decrease the rates of

enzyme catalyzed reactions. irreversible inhibitors render enzymes permanently
inactive and include several very toxic substances such as the cyanide ion and heavy
metal ions. Reversible inhibitors are of two types: competitive and noncompetitive.

Regulation of Enzyme Activity. Three mechanisms of cellular control over enzyme

activity exist. One method involves the synthesis of enzyme precursors called
zymogens, which are activated when needed by the cell. The second mechanism relies
upon the binding of small molecules

(modulators), which increase or decrease enzyme activity. Genetic control of enzyme

synthesis, the third method, regulates the amount of enzyme available.

Medical Applications of Enzymes. Numerous enzymes have become useful as aids

in diagnostic medicine. The presence of specific enzymes in body fluids such as blood
has been related to certain pathological conditions.

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Practice Examination
1. An enzyme is known to move an amine group from one material to
another. It would be referred to as a(n):
j
k
l
m
n lyase
j
k
l
m
n oxioreductase
j
k
l
m
n transferase
j
k
l
m
n hydrolase
j
k
l
m
n movase

2. A catalytically inactive protein formed by removal of the cofactor

from an active enzyme is called a(n):
j
k
l
m
n activator
j
k
l
m
n apoenzyme
j
k
l
m
n proenzyme
j
k
l
m
n preenzyme

3. The inactive precursor of an enzyme is called a(n):

j
k
l
m
n activator
j
k
l
m
n apoenzyme
j
k
l
m
n proenzyme
j
k
l
m
n preenzyme

4. A measure of how many subtrate molecules can be acted on by

an enzyme molecule is called:
j
k
l
m
n heat of reaction
j
k
l
m
n turnover rate
j
k
l
m
n catalytic speed
j
k
l
m
n activation energy

5. Which would you expect to have an effect on activity of an

enzyme.
j
k
l
m
n substrate concentration
j
k
l
m
n pH
j
k
l
m
n temperature

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 j
k
l
m
n enzyme concentration
j
k
l
m
n all of the above

6. A zymogen is classified as an inactive form of an enzyme.

j
k
l
m
n True
j
k
l
m
n False

7. Which enzyme is useful for detecting pancreatic disorders?

j
k
l
m
n amylase
j
k
l
m
n alkaline phosphatase
j
k
l
m
n creatine kinase
j
k
l
m
n lysozyme

8. The enzymatic model that assumes that enzymes have flexable

conformations is called:
j
k
l
m
n lock and key
j
k
l
m
n induced fit
j
k
l
m
n active site modification
j
k
l
m
n noncompetitive inhibition

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