| what do enzyme inhibitors do | Enzyme activity can be reduced or even stopped (some might say ‘inhibited’) temporarily, by a reversible inhibitor. |
| explain competitive inhibitors | Competitive inhibitors have a similar shape to a substrate and so are able to fit into the active site, blocking the substrate from doing so. |
| explain non-competitive inhibitors | Non-competitive inhibitors do not bind to the active site, but elsewhere on the enzyme (allosteric site). This however, alters the enzyme's shape and so the active site becomes deformed. |
| what is Vmax | its the maximal reaction rate or velocity of an enzymatically catalysed reaction when the enzyme is saturated with its substrate. |
| explain competitive inhibitors with vmax | With a competitive inhibitor, the reaction can eventually reach its normal Vmax but it takes a higher concentration of substrate to get it there. In other words, Vmax is unchanged. |
| explain non-competitve inhibitors with vmax | With a noncompetitive inhibitor, the reaction can never reach its normal Vmax, regardless of how much substrate we add. A subset of the enzyme molecules will always be affected by the inhibitor, so the effective concentration of enzyme (which determines Vmax) is reduced. |
| what does this graph mean | These graphs mean that if we add more substrate, the competitive inhibitors will be less likely to be successful. |
