Learning Objectives, Chapter 7

# Chapter 7, Enzyme Kinetics and Inhibition

## 7.1 Introduction to Enzyme Kinetics

Given an elementary step for a reaction, write the step’s
rate equation. 3, 5, 7

Relate reaction velocity to enzyme concentration.

Describe when an enzyme will become saturated in terms of
substrate concentration.

## 7.2 Derivation and Meaning of the
Michaelis-Menten Equation

Understand the derivation of the Michaelis-Menten
equation. 21

Relate *V*_{max}
to *K*_{M}. 13, 15, 17, 27

Know what *k*_{cat}
is.

Justify the use of *k*_{cat}
and *K*_{M} in the best measure of enzyme efficiency.

Know what a Lineweaver-Burk plot
is. 23

State three cases where the Michaelis-Menten rate equation
is not applicable.

## 7.3 Enzyme Inhibition

Explain why all irreversible inhibitors are not suicide
substrates.

Describe how a competitive inhibitor affects *K*_{M} and *V*_{max}.

Be able to calculate *K*_{I},
given the equation

39

Recognize transition state analogs, and relate them to
competitive inhibition. 35, 41

Relate the effect of mixed inhibitors and competitive
inhibitors on *K*_{M} and *V*_{max}, and to enzyme binding
sites. 43

Know that allosteric regulation includes positive and
negative effectors. 49

Describe how feedback inhibition works.