What is the consequence of a high Km value of an enzyme?
High concentration of the substrate is needed for the maximal enzyme activity.
The enzyme is present in a large concentration in the cell.
Moderate concentration of the substrate will be enough for maximal enzyme activity.
This enzyme has high maximal velocity.
Answer) High concentration of the substrate is needed for the maximal enzyme activity.
The consequence of having a high Km value for enzymes is that it needs high concentration of the substrate for it's activity. Those enzymes which have high Km values will have low affinity for its substrate and the saturation with substrate is low and as a result more addition of substrate concentration is necessary. The Km value( Michaelis constant) can be defined as the concentration of substrate were the reaction rate will be half of its maximal value. The Km value of substrate will help the enzyme to achieve the Vmax. Vmax is the point where the substrate and enzymes are completely saturated. An enzyme with low Km value will have a high affinity for substrate and will be easily saturated with substrate.For a reaction to occur, it is important to know about the Km value and the Vmax value because sometimes the rate of production of products will be dependent on the substrate concentration.
The other options are wrong because Km value is not the indicator of concentration of enzyme, it is the concentration of substrate and also high Km value of enzymes need high concentration of substrate, not in moderate amounts. To achieve high maximal velocity the saturation of substrate and enzymes should be faster.
Enzyme activity will be high when substrate concentration is equal to KM b. below KM c. above KM d. none of the above Metalloproteases mostly use the element Cu b. Fe c. Zn d. Mn
( --/ Question 1 What is the incorrect statement about catalysis? The enzyme-substrate complex has lower free energy than the free substrate The stronger the enzyme-substrate interaction, the higher the Km value. At very high substrate concentrations, the reaction rate is independent of the substrate concentration. The enzyme-substrate complex is not the transition-state molecule. The higher the turnover number of a catalyst, the lower the catalyst concentration needed to reach a certain maximum reaction rate.
If an enzyme has a Km of 10 micromolar, what fraction of the enzyme is active at 100 micromolar substrate concentration?
Part A An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 uM and a kcat value of 201 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures. ► View Available Hint(s) PO ALO O O ? [S]; = MM UM
high and detecting one product at a time Question 77 The initial velocity of an enzyme reaction (vo) describes A) The concentration of the enzyme at maximal velocity B) The concentration of substrate at maximal velocity C) The concentration of both at the start of the reaction D) The rate of the reaction when the substrate and enzyme are first med Question 78 What is the shape of a typical plot of initial rate vs substrate concentration tres kinetics? A)...
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the concentration of the substrate of the reaction ([S]). In Damon's Michaelis-Menten experiment, the highest concentration of substrate used was 500 UM. What do you think will happen to the reaction velocity if higher concentrations of substrate were used? Select one: a. Vo will reach a plateau at higher (S) values O b. Vo will increase exponentially as (S) is increased O c. Vo will...
If the enzyme concentration is 3.8 X 10-8, what concentration of substrate would generate a velocity equal to 0.25 Vmax? Km is not needed. Km= 15.42M
c. 0.6 sec d. 1.67 sec 16. Which of the following about Michaelis-Menten enzyme kinetics is CORRECT? a. It assumes that the maximum reaction rate is proportional to the catalytic constant multiplied by the total enzyme concentration. b. It assumes that the enzyme-substrate complex concentration remains steady state. c. KM is defined as the substrate concentration at which the velocity of the reaction is maximal, so the unit is M. d. The KM is assigned to each enzyme regardless of...
If the enzyme concentration is 3.8 X 10-8, what concentration of substrate would generate a velocity equal to 0.25 Vmax? Km is not needed.
At what substrate concentration would an enzyme with a kcat of 30.0 sec-1 and a Km of 0.0030 M have an initial velocity that is 25% of the maximum velocity? a. 0.0010M b 0.0090 M c. 0.0015 M d. 0.0060 M e.Cannot be determined