# Factors affecting ACP enzyme catalysed reaction
# pH; Every enzyme has its own optimum pH to perform their function effectively. Some enzymes are active at physilogical pH 7.4 (salivary amylase) and some are active at acidic pH (pepsin). So pH less or higher than physilogical pH would affect the rate of ACP enzyme catalysed reaction.
# Temperature (Tm); All enzymes function at a range of temperature only. This is called as optimum temperature (37 degree celsius). Higher than this temperature causes denaturation of enzyme and lower than this leads to reduced function.
# Incubation; Rate of reaction increases with increasing incubation time with substrate at the beginning but, after a stage the rate falls down.
# Concentration; Rate of reaction increases with increased concentration of enzymes because of the availability of more active sites for substrate.
# Inhibitor; An inhibitor always interfere with the product formation. It competes with the substrate for active site or it changes the conformation of an enzyme by binding to other than the active site.
# Substrate; Rate of reaction increases with increased substrate concentration but after reaching maximum velocity the rate of reaction remains unchanged (will not increase further). This is because the unavailability of active sites at enzyme for substrate.
introduction about effet of parameters ( ph,Tm,incubation,concentration, inhibitors and substrate ) on ACP enzyme ctalyzed reaction
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase. Which of the following best explains why? O As substrate concentration increases, the substrates preferentially bind with each other instead of the active site of the enzyme, and no additional catalysis occurs. As substrate concentration increases, the active sites of all the enzyme molecules become occupied with substrate molecules, and...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
List and describe the factors that can affect enzymatic reactions. a. Substrate Concentration b. Enzyme Concentration c. pH d. Temperature e. Cofactors f. Inhibitors (I have them listed but do not understand their affects)
6 The graph shows the effect of substrate concentration on the rate of an enzyme- controlled reaction. The enzyme concentration is constant. reaction rate Which statement about the graph is correct? A Between Wand X, the substrate concentration number of enzyme molecules is limiting. Between X and Y, the number of enzyme molecules is limiting. Between X and Y, the number of substrate molecules is limiting. Between X and Y, the product concentration remains the same. Thanh in the nammanni...
Which of the following statements are true about competitive enzyme inhibitors? a)They cause irreversible covalent modification of the target enzyme. b)They lead to a decrease in apparent Km. c)All of these d)They have significant affinity for the enzyme-substrate complex. e)Their effect on reaction rate can be overcome at high substrate concentrations. f)They lead to a decrease in apparent Vmax. g)None of these
5. The Km of an enzyme of an enzyme-catalyzed reaction is 6.5 uM. What substrate concentration will be required to obtain 55% of Vmax for this enzyme? (10 pts)
3. Summarize your findings about the concentration, temperature, and pH sensitivity of lactase. Enzyme Action An Investigation of Lactase Activity 137 PART F. EFFECT OF pH ON ENZYME ACTIVITY Activity of Lactair at Several pHs Observation with Tes Tape Glucose present Lactose pH 7 pH 2 pH 10 Glucose PART G. EFFECT OF AN INHIBITOR ON ENZYME ACTIVITY Inbibitor Efects Observation with Tes Tape Glucose present? Lactose Lactaid Ethanol Glucose 1. What is the optimum pH of the ion reaction,...
The concentration of substrate X is low. What happens to the rate of the enzyme- catalyzed reaction if the concentration of X is doubled? 15. What effect does an increase in the enzyme concentration have on the rate of an enzyme-catalyzed reaction? 16.
If the substrate concentration is varied with a fixed concentration of enzyme, it is observed that at low substrate concentrations that overall order while at high substrate concentrations, the reaction will be overall order. Select one: a. first; second b. first; third order c. first; zero d. second; second e. second; pseudo first order
An enzyme catalyzed reaction is studied at substrate concentration that is equal to 8Km. What will be the value of V0 in terms of fraction of Vmax?