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What else can I help you with?
Why would you expect the rate of an enzyme-catalyzed reaction to increase proportionately to enzyme concentration given an unlimited supply of substrate?
No, since the reaction reaches a max rate depending on the speed of which the Enzyme bonds to the substrate and the speed at which the enzyme catalyzes the reaction to produce enzyme and product (shown below). E + S --> ES (E - enzyme, S - substrate, P - products) ES --> E + P Thus, if each reaction rate is not equal to each other, the rate of the overall reaction is not only proportional to both the concentration of enzyme and substrate.
How many substrates can an enzyme have?
An enzyme can have multiple substrates, as it can bind to more than one substrate molecule at a time. This binding can occur at the active site of the enzyme, where the substrates interact with the enzyme's catalytic residues to facilitate the chemical reaction. The specificity of the enzyme's active site determines which substrates can bind to the enzyme.
The effect of substrate concentration on the rate of reaction of h202 and catalase?
As the substrate concentration increases, so will the enzyme activity and hence there will be a quick reaction. however, only up to a certain point ( where, if you drew a graph of the reaction, the line will level off ) as all the active sites in the enzyme are occupied and the reaction cannot go any faster. Here more enzymes will be needed to speed up the reaction.
Does the active site of an enzyme have a shape that is specfic for its given substrate?
Yes all enzymes have an active site where substance are temporarily bound. All enzymes have shape that may change during catalysis. The active site of an enzyme orients its substrate molecules, thereby promoting interaction of their reactive parts.
What factors affect the rate at which an enzyme works?
Very basically: * specificity - the better 'fit' the substrate, the higher the rate of catalysis. * temperature - higher temp = more kinetic energy = faster eaction. However, too high and the enzyme becomes irreversibly denatured and will not work at all. (denatured = the folding of the peptide chains are disrupted, meaning that the shape changes and the substrates no longer fit). The temperature at which the reaction occurs at the fastest rate is called the optimum temperature. * pH - enzymes have specific pH that they work best at (the optimum/optimal pH), as pH can also affect the bonds holding the tertiary structure together (especially ionic bonds), denaturing the enzyme. * concentration of enzyme and substrate - rate of reaction is proportional to the enzyme/substrate concentration. However, at a given enzyme concentration, substrate conc is proprtional to rate up to a point when the enzyme becomes saturated and the rate remains constant. * cofactors/coenzymes - some enzymes require interaction with other molecules to show full catalytic activity. * inhibitors - the presence of an inhibitor lowers the rate of catalysis. There are competitive, uncompetitive, non-competitive and mixed inhibitors, they can bind reversibly or irreversibly, at the active site or an allosteric site... That's a very simple, school textbook answer (and I may have forgotten a factor?). For more detail, any biochemistry textbook should be able to help.
In an enzyme catalyzed reaction what is the reactant called?
Generally in an enzyme-catalyzed reaction, the reactant is called the substrate, which in association with the enzyme forms the product.
What is the name given to the substance that an enzyme works on?
Oh, dude, that substance is called a substrate. It's like the enzyme's favorite little project to work on. So, when the enzyme is like, "I need something to do," the substrate is there to keep it busy. It's a match made in biochemical heaven.
Calculation fraction of enzyme bound to substrate?
The fraction of enzyme bound to substrate can be calculated using the Michaelis-Menten equation: [ES] / [E]t = [S] / (Km + [S]), where [ES] is the concentration of enzyme-substrate complex, [E]t is the total enzyme concentration, [S] is the substrate concentration, and Km is the Michaelis constant. This equation gives the ratio of the concentration of enzyme bound to substrate to the total enzyme concentration at a given substrate concentration.
The number of molecules with which an enzyme reacts is the?
The number of molecules with which an enzyme reacts is typically one or more substrate molecules. Enzymes bind to their substrates at their active sites to catalyze chemical reactions. The number of substrate molecules that can interact with an enzyme at a given time depends on factors like enzyme concentration, substrate concentration, and the kinetics of the enzyme-substrate complex formation.
A given enzyme works on?
specific substrates to catalyze a biochemical reaction. Each enzyme has a specific substrate or group of substrates that it acts on, and the enzyme's active site is designed to bind to these substrates. This specificity ensures that the enzyme functions effectively in the body.
The reason why an enzyme fits a specific substrate is due to its?
The reason why an enzyme fits a specific substrate is due to its 3rd dimensional shape. Enzymatic competition involves competition among several different available enzymes to combine with a given substrate material.
Why would you expect the rate of an enzyme-catalyzed reaction to increase proportionately to enzyme concentration given an unlimited supply of substrate?
No, since the reaction reaches a max rate depending on the speed of which the Enzyme bonds to the substrate and the speed at which the enzyme catalyzes the reaction to produce enzyme and product (shown below). E + S --> ES (E - enzyme, S - substrate, P - products) ES --> E + P Thus, if each reaction rate is not equal to each other, the rate of the overall reaction is not only proportional to both the concentration of enzyme and substrate.
What is the vmax of ldh?
The vmax of lactate dehydrogenase (LDH) is the maximum velocity at which the enzyme can catalyze the conversion of lactate to pyruvate in a given concentration of substrate. This value represents the rate of the enzyme-catalyzed reaction at saturated substrate concentrations.
What is the optimal pH for maintaining a stable enzyme activity at a given substrate concentration of 10 mM?
The optimal pH for maintaining stable enzyme activity at a substrate concentration of 10 mM is typically around pH 7. Enzymes function best within a specific pH range, and deviations from this range can affect their activity. Maintaining the pH at around 7 helps to ensure that the enzyme is working efficiently at the given substrate concentration.
What name is given to the molecules made in an enzyme controlled reaction?
The molecules made in an enzyme-controlled reaction are usually referred to as products. These products are the result of the substrate molecules being transformed by the enzyme during the reaction.
What is the unit of specificity constant?
The unit of specificity constant is typically expressed in units of M^(-1)·s^(-1) since it represents the efficiency of an enzyme in converting substrate to product per unit time for a given substrate concentration. The lower the value of the specificity constant, the less efficient the enzyme is at converting substrate to product.
How many substrates can an enzyme have?
An enzyme can have multiple substrates, as it can bind to more than one substrate molecule at a time. This binding can occur at the active site of the enzyme, where the substrates interact with the enzyme's catalytic residues to facilitate the chemical reaction. The specificity of the enzyme's active site determines which substrates can bind to the enzyme.
