we're removing substrate from the environmnet because the enzyme is bound by the inhibitor, causing the substrate to be locked into an inactive enzyme
- There is a reduction in vmax short of the uninhibited Vmax.
- If we have 100 enzymes, for example, and inhibitor inactivates by binding, it's almost as if they don't exist. So, Vmax goes down
Km changes as well because, as we add inhibitor, it is binding substrate as wel, causing less substrate to be present