Chemistry 303

Chapter 6

Reading Assignment

Section 6.1
What is the difference between cofactors and coenzymes?
How are enzymes classified? We will learn what criteria put each enzyme into one of these six.
Section 6.2
From a general perspective, enzymes speed up reactions but do not change the equilibrium of these
reactions. Thermodynamically, how do we explain this?
What is considered the rate-limiting step of an enzyme catalyzed reaction?
The activity of enzymes can be summed up in their catalytic power and their specificity. What do these
two things mean?
What is meant by binding energy?
How does this binding energy affect specificity and catalysis?
Three general processes are common ways that enzymes work. These need to be understood: general
acid-base catalysis, covalent catalysis, and metal ion catalysis. How do the names of these mechanisms
describe what they are about?
Section 6.3
There will be a lot of algebra to cover in this section.
Understand these terms: initial rate, maximum velocity, steady state
We will derive the Michaelis-Menten eqn. Can you see how such an equation gives the graph in Fig 612?
What is the popular transformation of this equation that linearizes velocity vs. substrate concentration
data?
We will talk about catalytic efficiency in class.
What are the possible binding orders when two substrates are involved in a reaction mechanism? Steady
state kinetics can be used to elucidate these mechanisms.
Reversible inhibition kinetics will also be covered.
Irreversible inhibitors will be quickly reviewed
pH profiles for enzymes give important information about binding and catalytic functional groups.
Section 6.4
We will work through the chymotrypsin mechanism
Review the how to read reaction mechanisms-a refresher section on p216
Review the nucleophiles & electrophiles listed on p216
We will work through the hexokinase mechanism
We will probably only get to briefly outline the mechanisms for enolase and lysozyme.
Section 6.5
Review the concept of allosteric enzymes and the role of the regulatory subunit for the catalytic subunit.
What are the key components of feedback inhibition?
How do the kinetics of allosteric enzymes compare to normal Michaelis-Menton kinetics?
What kinds of covalent modifications are known for regulating enzymes?
Relevant end of chapter questions:
1, 3,4, 6-8, 11, 13, 15, 17, 18, 19, & 21

More than typical test questions, but good exercises: 10, 12, & 16