Biochemical Education 27 (1999) 135 } 136

The enzyme's party: an analogy

Donald J. Bauhs Jr
Department of Cellular and Molecular Pharmacology, Program in Neuroscience, University of California, San Francisco, CA 94143-0450, USA
Received 16 September 1998; accepted 11 November 1998

Abstract

The following enzyme analogy includes concepts such as K , < , activation energy, and competitive inhibition amongst others.

These concepts are described with the host of a party as an enzyme and the guests as the substrates.  1999 IUBMB. Published by
Elsevier Science Ltd. All rights reserved.

tells of his discomfort. Eric tells Sam that he will break

1. Introduction
the ice and introduce him to someone. As Eric takes Sam
The world of biochemistry exists at a molecular level. across the room he spots Ben.
In this world are molecules of proteins, nucleic acid and &&Ben, I'd like you to meet my friend, Sam,''.
lipids. We are allowed only imagination and experi- Sam and Ben feel a brief bit of tension as they begin
mental methods to experience the biochemical world. talking. They soon feel more at ease with each other. Eric
One way to imagine the biochemical world in familiar then departs to greet another friend.
terms is through analogies. Students cannot always de- As more guests arrive Eric becomes more busy. A mo-
pend on familiar senses such as vision and touch in ment is reached where Eric is spending half of his time
learning about the biochemical world. Instead, imagin- speaking with guests and the other half walking around
ation and creativity become the students most sensitive "nding guests. Guests continue to arrive and ultimately
tools. The following enzyme analogy attempts to spark Eric feels like he is walking and talking as fast as he can.
imagination on the biochemical world by making a part Now, even if more people come, Eric cannot introduce
of it more familiar. his guests any faster.
With Eric as busy as can be and more guests mingling,
Irene, Eric's girlfriend, arrives. As Irene peers across the
2. Eric:s party crowded room looking for Eric, they run into each other.
Eric is now occupied by Irene. After minutes of talking
Eric is eager for his party to begin. He invited many with Irene, Eric remembers that he still has many guests
people and a few are now arriving. Eric is determined to who need introducing. He excuses himself from Irene and
make his party successful. At "rst, he is disheartened resumes introducing guests to each other. It does not
because almost no one is talking. He hopes that his take long, however, for his a$nity for Irene to override
guests will soon mingle. But, as more people come the his desire to keep his guests mingling. It would take many
party remains very unsociable. Suddenly Eric realizes more guests for Eric to be diverted from Irene and re-
why. By an amazing coincidence, none of his friends sume his busiest pace.
know each other!
Eric looks around the room and this fact becomes
obvious. He sees almost everyone standing sheepishly by 3. The enzyme:s party
themselves. Eric feels that he must get everyone to know
each other to make the party a success. Eric spots his Eric's party can be described biochemically. Eric is an
friend Sam and begins to make his way across the room. enzyme and his guests are substrates. The reaction
Sam realizes he only knows Eric. He is reluctant to talk catalyzed is the introduction of guests and the product is
to anyone else. Seeing Eric coming towards him, Sam conversing guests (scheme describing enzymatic reaction

0307-4412/98/$20.00#0.00  1999 IUBMB. Published by Elsevier Science Ltd. All rights reserved.
PII: S 0 3 0 7 - 4 4 1 2 ( 9 8 ) 0 0 2 8 7 - 8
136 D.J. Bauhs Jr / Biochemical Education 27 (1999) 135 } 136

Fig. 2. Plot of initial enzyme reaction velocity (l ) versus substrate


Fig. 1. (A) Free energy pro"le of uncatalyzed reaction; (B) Free energy concentration for an enzyme with (dashed curve) and without (solid curve)
pro"le of enzyme-catalyzed reaction. The "rst barrier is for e, S and B to competitive inhibitor. The velocity approaches < as substrate concen-

bind together where the second barrier is the transition state for the tration increases. The K is the substrate concentration where l equals

interaction of S and B. Notice the lowering of the activation energy half < . Notice that the K with inhibitor (K ) is greater than
 
(arrows) from uncatalyzed to catalyzed reactions. without inhibitor (K ) but the < for both conditions is the same.
 

is shown in Eq. (1).

e#S#B { SeBPe#SB
Key: e * Eric; S * Sam; B * Ben;
SB * Sam and Ben talking. (1)
Irene is the enzyme inhibitor. Since none of the guests
know each other, the activation energy for their mingling
is high (Fig. 1a). The enzyme lowers this activation en-
ergy and thereby speeds the reaction (Fig. 1b). Without
enzyme, very few guests are likely to have enough impe-
Fig. 3. Free energy pro"le of competitive enzyme inhibition. The en-
tus to introduce themselves. zyme can bind either substrate or inhibitor. If inhibitor is bound, the
Sam's &&reluctance to talk to anyone'' can be seen in strong a$nity between e and I puts them into a deep free energy well
the high activation energy of the uncatalyzed reaction from which it is di$cult to escape.
(Fig. 1a). Eric recognizes his substrate, Sam, and binds to
(catalyzing) as fast as he can''. At Eric's < there are so
him. This enzyme-substrate complex di!uses across the 
many guests around that when he releases one guest, he
room until the second substrate (Ben) is bound.
immediately "nds another to introduce. Eric is saturated
With Eric bringing them close together, Sam and Ben's
with substrate and even if more guests arrive, he cannot
introduction is catalyzed. The chemistry step can be
get any busier.
thought of as Eric's statement, &&Ben, I'd like you to meet
Irene, like many competitive enzyme inhibitors, has
my friend, Sam.'' The &&brief tension'' Sam and Ben feel is
much stronger &&a$nity'' for Eric than do substrates. This
at the transition state (indicated by the vertical arrows in
a$nity results in a stable well on a reaction diagram
Fig. 1). Their &&feeling more at ease'' is analogous to the
(Fig. 3). Once Eric binds Irene and falls into this stable
stability of the product that follows the transition state.
well, he is unlikely to have enough desire to escape. When
The enzyme releases product as Eric &&departs'' to
bound, Irene keeps Eric from introducing guests, lower-
catalyze another introduction.
ing his l. However, Eric could still reach his usual < if
As the party continues more substrate (guests) arrives. 
he was &&diverted from Irene'' with the addition of much
A point is reached where the enzyme is occupied half the
more substrate. Increasing substrate relative to inhibitor
time. At this point, Eric is spending half his time "nding
increases the likelihood of free Eric encountering a guest
guests and the other half introducing them. In fact, at this
instead of Irene. There is a point where there are simply
half-occupied point, Eric is catalyzing at exactly half of
too many guests for Irene to successfully compete for
his maximum rate (< ). This substrate concentration
 Eric. In kinetic terms, Irene increases Eric's K but does
where the velocity (l) is half < is called the K (Fig. 2,
 not a!ect his < (Fig. 2, dashed curve).
solid curve). If the K is very low, the enzyme has strong 

a$nity for its substrate and it takes little substrate for
l to reach half < . Acknowledgements

As time goes on, the concentration of substrate con-
tinues to increase. Eric approaches his < (Fig. 2, solid The author is grateful to Ron Raines and Peter Chivers

curve) when he &&is walking (di!using) and talking for their thoughts on this article.