Jordan Johnson

Mrs. Sintich
Advanced Placement Biology
January 11, 2016
Summary
Essential knowledge 4.B.1: Interactions between molecules affect their structure and function.
a. Change in the structure of a molecular system may result in a change of the function of
the system.
b. The shape of enzymes, active sites and interaction with specific molecules are essential
for basic functioning of the enzyme.
1. For an enzyme-mediated chemical reaction to occur, the substrate must be
complementary to the surface properties (shape and charge) of the active site. In
other words, the substrate must fit into the enzymes active site.
2. Cofactors and coenzymes affect enzyme function; this interaction relates to a
structural change that alters the activity rate of the enzyme. The enzyme may only
become active when all the appropriate cofactors or coenzymes are present and
bind to the appropriate sites on the enzyme.
c. Other molecules and the environment in which the enzyme
acts can enhance or inhibit enzyme activity. Molecules can bind reversibly or irreversibly
to the active or allosteric sites, changing the activity of the enzyme.
d. The change in function of an enzyme can be interpreted from data regarding the
concentrations of product or substrate as a function of time. These representations
demonstrate the relationship between an enzymes activity, the disappearance of
substrate, and/ or presence of a competitive inhibitor.
Artifact
Enzymes

- catalyst (speed up chemical reactions, but

are not used up)

- protein
- lower activation energy of a reaction
Substrate

- reactant enzyme acts upon

Active Site

- restricted region of enzyme where enzyme

Induced Fit Model

- forms an enzyme-substrate complex

- slight change in shape to better fit the

binds to substrate

substrate

How do enzymes lower activation energy?

- arranges reactants into the proper

-

Factors Affecting Enzyme Activity

- Temperature (up to a certain point the

-

Enzyme Inhibitors

reaction rate increases as the temperature

also increases)
pH (up to a certain point the reaction rate
increases as the pH increases)
Salinity (reaction rate decreases as salinity
increases)
Cofactors (needed by enzymes for some
catalytic activity)- also includes coenzymes
Enzyme Inhibitors
Substrate Concentration

- Irreversible Inhibition (irreversible-

Allosteric Regulation

orientation
stretches substrate to break bonds
creates a microenvironment
may bind to substrate temporarily

attaches to enzyme using covalent bonds)

Reversible Inhibition (attaches to enzyme
using weak bonds/interactions)can be
competitive and noncompetitive

- binds a molecule to an enzyme other than

its active site

- can cause the enzyme to be stimulated or

inhibited
Cooperativity

- amplification of enzyme activity when one

substrate binds to one active site and
stimulates the other subunits

Feedback Inhibition

- when a metabolic pathway is switched off

-

by the inhibitory binding of the end product

to an enzyme
stops pathway

4.B.1: b, c, d
Reflection
From this artifact I learned several things. First, the substate (the reactant the enzyme acts on)
binds to the enzyme on the active site. Also, I learned that cofactors and coenzymes (organic
cofactors) are important for certain reactions to occur. Furthermore, an allosteric regulation
involves a molecule binding to an enzyme other than its active site. Finally, enzyme inhibitors
can be irreversible or reversible, which can be competitive or noncompetitive. I feel like I

struggled that most with understanding temperature, pH, or salinity can denature an enzyme. In
other words, what occurs when the enzyme is denatured?