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 …

This article discusses the specific effects of various enzyme inhibitors on kinetic graphs, highlighting how these visual tools can be used to pinpoint the type of inhibition involved.

If an inhibitor is competitive, it will decrease reaction rate when there's not much substrate, but can be "out-competed" by lots of substrate. That is, the enzyme can still reach its maximum …

So the classic case of competitive inhibition: if there's some molecule that competes for the substrate at the active site, as we'll see this isn't the only form of competitive inhibition, but this …

Competitive inhibition occurs when the inhibitor has a similar shape and/or charge with the substrate, thus allowing it to bind to the active site on the enzyme.

There are four different kinds of inhibitors; competitive inhibitors, noncompetitive inhibitors (allosteric inhibitors), irreversible inhibitors, and feedback inhibitors. Competitive inhibitors …

Enzymes are "specific." Each type of enzyme typically only reacts with one, or a couple, of substrates. Some enzymes are more specific than others and will only accept one particular …

Learn Enzyme cofactors and coenzymes Competitive inhibition Noncompetitive inhibition Enzyme regulation Basics of enzyme kinetics graphs

Seeing how a noncompetitive inhibitor can bind whether or not the substrate is bound, and vice versa.

In this first graph, I've drawn three different curves. The blue curve represents the enzyme functioning without an allosteric regulator at all. The red curve represents the enzyme with an …