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- resemble substrate (TS analogs)
- DOES NOT CHANGE Vmax
- INCREASES Km
- Add CI, Kmapp increases, x-axis shifts Right
- Increase in Km causes steeper slope
- will not bind to empty substrates, binds to ES complex to form ESI complex
- Vmax is decreased
- Kmapp in decreased
- No change in slope, PARALLEL LINES
- Y-INT goes UP
- Slows down reaction because it essentially removes enzyme and therefore inhibits the amount of product that can be made
- DOES NOT AFFECT SUBSTRATE BINDING
- I must come off ESI before S can dissociate or product can be made
- Anything in between competitive and uncompetitive
- Bind at sites other than active site (allosteric)
- Decreases the rate because allows S to bind but inhibits product formation
- can either bind empty enzyme (NOT at active site) or bind ES complexes
- DECREASE Vmax
- Km MAY or MAY NOT change (usually)
- Have a steeper slope
- mixed inhibitors that DO NOT effect ES formation
- alpha and alpha' values are equal
- bind equally to empty E and ESI complex
No Inhibitor and Competitive Inhibitors...
Cross y-axis at the same point
No Inhibitor and Uncompetitive Inhibitors...
No Inhibitor and Noncompetitive Inhibitors...
Cross x-axis at same point
No Inhibitor and Mixed Inhibitors
Do a mix of all of the diff things listed.