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Does tight binding between enzyme and its substrate imply rapid catalysis?
Wiki User
∙ 13y ago
All catalysts, enzyme work via the lowering of the activation energy for a reaction this causes the rate of the reaction to increase dramatically. Should be noted that most enzyme with tight binding reactions rates are millions of times faster than those of of catalyst similar reactions. causing rapid catalysis
Wiki User
∙ 13y ago
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Are enzyme catalyzed reactions example of homogeneous or heterogeneous catalysis?
enzyme catalysis is usually homogeneous because the substrate and enzyme are present in aqueous solution
What are the four mechanisms that get substrates to the transition state?
The four mechanisms that get substrates to the transition state are: Acid-base catalysis, where protons are transferred between the enzyme and substrate to stabilize the transition state. Covalent catalysis, where the enzyme forms a transient covalent bond with the substrate to lower the activation energy. Metal ion catalysis, where metal ions in the active site of the enzyme participate in the catalytic reaction. Catalysis by proximity and orientation, where the enzyme brings the substrates in close proximity and in the correct orientation to facilitate the reaction.
The binding together of an enzyme and substrate forms?
It forms an Activation Site.
How can you describe the enzyme-substrate complex?
Enzyme-substrate complex (or ES complex) is the key to understand the kinetic behavior of the enzymes. The ES complex represents just the starting point for the catalysis reaction.The kinetic pattern of enzymes was led by Victor Henri in 1903. He proposed that an enzyme combines with its substrate molecule to form the ES complex as a necessary step in enzyme catalysis. This idea expanded into a general theory of enzyme action, particularly by Leonor Michaelis and Maud Menten in 1913, who postulated that the enzyme (E) first combines reversibly with its substrate to form an enzyme-substrate complex (ES )in a relatively fast reversible step. The ES complex then breaks down in a slower second step to yield the free enzyme and a product (P), according to the following equation:E + S < > ES > E + P
Can enzyme reaction can be slowed or halted using inhibitors?
Yes, enzyme reactions can be slowed or halted using inhibitors. Inhibitors can bind to the enzyme and prevent it from binding to its substrate, thus inhibiting the reaction. There are different types of inhibitors, such as competitive inhibitors that compete with the substrate for binding to the enzyme, and non-competitive inhibitors that bind to a different site on the enzyme and alter its shape or function.
The binding together of an enzyme and a substrate forms a what?
enzyme-substrate complex
What happens to the vmax when a competitive reversible inhibitor is added to an enzyme?
The vmax stays the same as the competitive reversible inhibitor does not affect catalysis in the enzyme-substrate.
Are enzyme catalyzed reactions example of homogeneous or heterogeneous catalysis?
enzyme catalysis is usually homogeneous because the substrate and enzyme are present in aqueous solution
The binding together of an enzyme and a substrate forms a?
The substrates are converted into products, which are released.
What is it called when and enzyme and substrate come together?
The binding of an enzyme and a substrate forms an enzyme-substrate complex. It lowers the activation energy of a chemical reaction
What is the induced fit theory?
The induced fit theory proposes that the active site of an enzyme changes its shape upon binding with the substrate. This change is induced by the interaction with the substrate, leading to a more precise fit and optimal conditions for catalysis to occur. This theory suggests that the binding of a substrate to an enzyme is a dynamic process rather than a static lock-and-key model.
What is the region on an enzyme to which a substrate bind is called?
Binding site.
What are the four mechanisms that get substrates to the transition state?
The four mechanisms that get substrates to the transition state are: Acid-base catalysis, where protons are transferred between the enzyme and substrate to stabilize the transition state. Covalent catalysis, where the enzyme forms a transient covalent bond with the substrate to lower the activation energy. Metal ion catalysis, where metal ions in the active site of the enzyme participate in the catalytic reaction. Catalysis by proximity and orientation, where the enzyme brings the substrates in close proximity and in the correct orientation to facilitate the reaction.
What is the difference between enzyme and active site?
An enzyme is a biological catalyst. An active site is a region on the enzyme molecule where the conversion tales place. The substrate molecule docks at the active site and is converted to the product
The binding together of an enzymes and a substance forms what?
An enzyme-substrate complex.
The binding together of an enzyme and substrate forms?
It forms an Activation Site.
Altering the three-dimensional structure of an enzyme might?
prevent the substrate from binding the enzyme's active site
