What I'd graph between time and enzyme concentration
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Answer:
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Answer:
Enzyme kinetics graphs and inhibitors
Now, what about inhibitors? We discussed two types of inhibitors, competitive and noncompetitive, in the article on enzyme regulation.
- Competitive inhibitors impair reaction progress by binding to an enzyme, often at the active site, and preventing the real substrate from binding. At any given time, only the competitive inhibitor or the substrate can be bound to the enzyme (not both). That is, the inhibitor and substrate compete for the enzyme. Competitive inhibition acts by decreasing the number of enzyme molecules available to bind the substrate.
- Noncompetitive inhibitors don’t prevent the substrate from binding to the enzyme. In fact, the inhibitor and substrate don't affect one another's binding to the enzyme at all. However, when the inhibitor is bound, the enzyme cannot catalyze its reaction to produce a product. Thus, noncompetitive inhibition acts by reducing the number of functional enzyme molecules that can carry out a reaction.
If we wanted to show the effects of these inhibitors on a graph like the one above, we could repeat our whole experiment two more times: once with a certain amount of competitive inhibitor added to each test reaction, and once with a certain amount of noncompetitive inhibitor added instead. We would get results as follows:
With a competitive inhibitor, the reaction can eventually reach its normal V_{max}V
mmax
V, start subscript, m, a, x, end subscript, but it takes a higher concentration of substrate to get it there. In other words, V_{max}V
max
V, start subscript, m, a, x, end subscript is unchanged, but the apparent K_mK
m
K, start subscript, m, end subscript is higher. Why must more substrate be added in order to reach V_{max}V
max
V, start subscript, m, a, x, end subscript? The extra substrate makes the substrate molecules abundant enough to consistently “beat” the inhibitor molecules to the enzyme.
