How do competitive and non-competitive enzyme inhibitors affect reaction velocity?

competitive inhibitors are basically like someone trying to steal the seat you're aiming for. they look a lot like the actual substrate, so they rush to the active site of the enzyme first. since they're blocking the path, the enzyme can't do its job properly. but here's the kicker: if you just throw enough substrate at the situation, you can eventually outcompete them. this means your Vmax stays the same because the enzyme can still work fine once the inhibitor gets kicked off, but your Km goes up because it takes way more substrate to hit half that speed.

non-competitive ones are a bit more annoying. they don't care about the active site at all; they bind somewhere else entirely, which we call the allosteric site. once they latch on, they change the whole shape of the enzyme, so even if the substrate shows up, it just won't fit right. since they aren't competing for the same spot, adding more substrate won't help you at all. in this case, your Vmax drops because you've effectively taken a chunk of your enzymes out of commission, but your Km usually stays the same since the enzymes that aren't inhibited are still functioning like normal.