How do you expect the KM determined with a substrate that is preferred by the enzyme to differ from the KM determined with a general enzyme substrate?
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We all know that enzymes are substrate specific so the substrate
that is preferred by the enzyme will catalyzed faster than the
general substrate.
Km is the michaelis menten constant can be defined as the substrate concentration required for the enzyme to attain half maximum velocity of the reaction or 1/2 Vmax.
So it is understandable and acceptable that the substrate that is preferred by the enzyme will react faster and will attain Vmax early than the other substrate. As Vmax is short so value of Km also will be less as it is directly proportional to Vmax. So the value of Km of the substrate that is preferred by the enzyme will be less than the Km determined with a general enzyme substrate.
Find the attached image file for graphical explanation

How do you expect the KM determined with a substrate that is preferred by the enzyme...
Why might PNPA might be a substrate for a hydrolase? Your answer should address the subject of enzyme substrate specificity. Correct, detailed (paragraph explanation) needed for thumbs up
How do competitive inhibitors affect the KM and Vmax of an enzyme? Draw a plot of velocity as a function of substrate concentration, both with and without inhibitor added.
Calculate the KM and Vmax for the
enzymatic reaction graphed below.
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Wn [s] 005 006 006 002 001 vfumol/min)
Problem 3: A) Draw the mechanistic modifications associated with chymotripsin enzyme and its substrate up to the formation of acyl enzyme intermediate. Specify the role of each of the amino acids in the catalytic triad. B) Provide a Michaelis-Menten rate-law equation. Subsequently, on the same graph draw Lineweaver-Burk plots for i) enzyme which is not inhibited: ii) enzyme inhibited by a non-competitive inhibitor, C) The Km and kcat for hexokinase with as a glucose substarte are 5-10 M and 8-10²...
You are trying to determine the Km for an enzyme. Due to a lab mishap, you have only two usable data points: Substrate concentraion (microM) Reaction Velocity (microM .s^-1) 1)1 5 2)100 50 Please help not sure what to do but I know this answer can be obtained from the Michaelis equation and a Line-Weaver Burk equation isnt needed. Thank you
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a series of assays where you measured the rate of reactions as you varied the concentration of substrate in each assay (Table A). Estimate from a Michaelis-Menten plot approximate values for Vmax, KM, Kcat, and the specificity constant for this enzyme and substrate. (The only information that is given is this paragraph and the table below). Table 1: [S] (μM) v (μmol/L/min) 0 0 5...
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Q1. WHAT ARE ENZYMES? HOW DOES ENZYME-SUBSTRATE BINDING TAKES PLACE? Q2. IN MICHAELIS -MENTEN GRAPH, WHY DOES THE CURVE REACHES PLATEAU? Vmax Reaction velocity (v) Vm/2 Km Substrate concentration (S) Q3. IN MICHAELIS MENTEN GRAPH, HOW WOULD YOU INCREASE VELOCITY BEYOND Vmax? Q4. SMALLER VALUE OF THE MICHAELIS CONSTANT (Km) REFLECTS HIGHER EFFICIENCY OF THE ENZYME. (TRUE/FALSE).
(a) After spending a few weeks isolating the enzyme, you have enough pure enzyme to do some kinetic experiments, using a chromogenic substrate. The product produced by the enzyme from this substrate has an extinction coefficient of 20,500cm−1M−1 at 486nm, whereas the substrate does not absorb light significantly at this wavelength. For these experiments, you have used an enzyme concentration of 1.75µg/mL and monitored the change of absorbance at 486nm, using cuvettes with a path length of 1cm. The initial...
4. What does enzyme kinetics study? What is Vo, km, Vmax, Kcat, respectively? If you plot Vo versus (substrate), or 1/Vo versus 1/[substrate], how the curves would look like, and how to get Vmax and Km values?
A.Your summer research project is to study the kinetics of a newly discovered enzyme. You have already identified the substrate and optimal reaction conditions. Propose how you would set up experiments to characterize the maximum velocity (Vmax) and Michaelis constant (KM) of this enzyme, assuming that it will display Michaelis-Menten kinetics. B. How would you compare the specificity of the enzyme for its natural substrate versus its specificity for a chromogenic substrate analog that was synthesized in the lab