Based on Michaelis-Menten enzyme kinetics, the initial rate of reaction, vi, is dependent on maximum rate Vmax, substrate concentration [S], and the enzyme's Michaelis constant Km, which represents the the tendency of the substrate/enzyme complex to dissociate. The dependence on enzyme concentration is factored into the maximum rate. The equation to describe this is: vi = Vmax([S]/(Km+[S])) Follow the link below for details.
As the substrate concentration increases so does the reaction rate because there is more substrate for the enzyme react with.
When the substrate concentration is equal to the Michaelis constant (Km), the initial velocity of the enzyme-catalyzed reaction will be half of the maximum velocity (Vmax) of the reaction. At Km, half of the enzyme active sites are filled with substrate, leading to half of maximum velocity being reached.
The enzyme graph shows that the reaction rate of the catalyzed reaction is faster compared to the uncatalyzed reaction. This indicates that the enzyme is effectively speeding up the reaction process.
The enzyme activity curve shows that as enzyme concentration increases, the reaction rate also increases. However, there is a point where adding more enzyme does not further increase the reaction rate, indicating that there is a limit to the effect of enzyme concentration on reaction rate.
The minimum enzyme concentration needed to start a reaction varies depending on the specific enzyme and reaction conditions. In general, a higher enzyme concentration can lead to a faster reaction rate, but there is no fixed minimum concentration that applies universally. The amount of enzyme required to initiate a reaction is typically determined through experimentation and optimization.
3 factors that affect the speed of an enzyme catalysed reaction are: .Temperature .Enzyme Concentartion .Substrate concentration
Delta G (d)
Generally in an enzyme-catalyzed reaction, the reactant is called the substrate, which in association with the enzyme forms the product.
substrateSubstrates.substrate
As the substrate concentration increases so does the reaction rate because there is more substrate for the enzyme react with.
At low substrate concentrations, the rate of enzyme activity is proportional to substrate concentration. The rate eventually reaches a maximum at high substrate concentrations as the active sites become saturated.
By heating the homogenate. proteins are innactivated by heat and enzyme activity is lost
because the enzyme is becoming denatured
The change in ∆G would not be affected by doubling the amount of enzyme in the reaction. The ∆G value of a reaction represents the intrinsic energy difference between the products and the reactants, and it is not altered by enzyme concentration.
It's 350 - I'm n biology HNRS
An Enzyme must always be a protein. Any Enzyme is always categorized as the amine in the amino acid sequences that comprise it, and anything made of amino acids is automatically categorized as a protein. Therefore, not all proteins are enzymes, but all enzymes are proteins.
The Michaelis-Menten curve is a graphical representation of the relationship between the substrate concentration and the initial reaction rate of an enzyme-catalyzed reaction. It helps to determine important kinetic parameters such as the Michaelis constant (Km) and the maximum reaction velocity (Vmax), which are crucial for understanding enzyme-substrate interactions and enzyme efficiency. This curve is instrumental in studying enzyme kinetics and predicting how changes in substrate concentration affect the enzyme's activity.