[Answer] what are competitive inhibitors?

Answer: competitive inhibitors bind to the active site of an enzyme and prevent substrates from binding
what are competitive inhibitors?

In competitive inhibition of enzyme catalysis binding of an inhibitor prevents binding of the target molecule of the enzyme also known as the substrate. This is accomplished by blocking the binding site of the substrate – the active site – by some means. The Vmax indicates the maximum velocity of the reaction while the Km is the amount of substrate needed to reach half of the Vmax. Km also plays a part in indicating the tendency of the substrate to bind the enzyme. Competitive inhibition can be overcome by adding more substrate to the reaction which increases the chances of the enzyme and substr…

In competitive inhibition of enzyme catalysis binding of an inhibitor prevents binding of the target molecule of the enzyme also known as the substrate. This is accomplished by blocking the binding site of the substrate – the active site – by some means. The Vmax indicates the maximum velocity of the reaction while the Km is the amount of substrate needed to reach half of the Vmax. Km also plays a part in indicating the tendency of the substrate to bind the enzyme. Competitive inhibition can be overcome by adding more substrate to the reaction which increases the chances of the enzyme and substrate binding. As a result competitive inhibition alters only the Km leaving the Vmax the same. This can be demonstrated using enzyme kinetics plots such as the Michaelis–Menten or the Lineweaver-Burk plot. Once the inhibitor is bound to the enzyme the slope will be affected as the Km either increases or decreases from the original Km of the reaction. Most competitive inhibitors function by binding reversibly to the active site of the enzyme. As a result many sources state that this is the defining feature of competitive inhibitors. This however is a misleading oversimplification as there are many possible mechanisms by which an enzyme may bind either the inhibitor or the substrate but never both at the same time. For example allosteric inhibitors may display competitive non-competitive or uncompetitive inhibition. In competitive inhibition an inhibitor that resembles the normal substrate binds to the enzyme usually at the active site and prevents the substrate from binding. At any given moment the enzyme may be bound to the inhibitor the substrate or neither but it cannot bind both at the same time. During competitive inhibition the inhibitor and substrate compete for the active site. The active site is a region on an enzyme to which a particular protein or substrate can bind. The active site will thus only allow one of the two co…

Reversible inhibitors attach to enzymes with non-covalent interactions such as hydrogen bonds hydrophobic interactions and ionic bonds. Multiple weak bonds between the inhibitor and the active site combine to produce strong and specific binding. In contrast to substrates and irreversible inhibitors reversible inhibitors generally do not undergo chemical reactions when bound to the enzyme and can be easily removed by dilution or dialysis. There are four kinds of reversible enzyme inhibitors. They are classified according …

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