help with these please The turnover number is defined as the maximum number of substrate molecules...
Determine the value of the turnover number of the enzyme catalase, given that Rmax (Vmax) for catalase is 41 mmol · L-1.5-1 and [E]t equals 3.6 nmol · L-1. Catalase has a single active site. turnover number: 8-1
The maximum catalytic rate of an enzyme is defined as the turnover number (also called kcat)and is the maximum number of reactions a single active site can carry out per second for a given concentration of enzyme. i.Would a competitive inhibitor reduce the turnover number for an enzyme?Why? ii.Would an irreversible inhibitor reduce the turnover number for an enzyme?Why?
Need help with number 13! I already asked about number 12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
1. Protein kinases phosphorylate target enzymes and as a result enzymes become activated or inactivated. Which of the statements are TRUE? (Multiple answers: You can select more than one option) A. Phosphorylated enzymes behave like competitive inhibitors B The presence of a phosphate acts as a non-competitive inhibitor/activator. No change in Km but significant change in Vmax C. The presence of a phosphate group induces a conformational change that modifies the affinity and catalytic ability of a target enzyme D....
1) 2) If the total enzyme concentration was 9 nmol/Lnmol/L, how many molecules of substrate can a molecule of enzyme process in each minute? Express your answer to three significant figures. 3) The kcat for neuraminidase at pH=6.15pH=6.15, 37 ∘C∘C is 26.8 s−1s−1. Calculate KMKM for the hydrolysis of sialic acid. Express your answer with the appropriate units. An enzyme that follows Michaelis-Menten kinetics has a Ky value of 6.00 uM and a keat value of 176 s-1. At an...
Some enzymes have a very flat pH profile m dash that is, they have essentially the same activity over a broad pH range. How might you explain this observation? Michaelis-Menten Kinetics. Figure 6-19 represents a Michaelis-Menten plot for a typical enzyme, with initial reaction velocity plotted as a function of substrate concentration. Three regions of the curve are identified by the letters A, B, and C. For each of the statements that follow, indicate with a single letter which one...
How many tetrahedral intermediates occur during the serine protease mechanism. Which of the following is not a general property of most enzymes. Answer by placing the number in the box. There is only one correct answer. 1. The active site takes up a small portion of the enzyme's surface. 2. The enzyme binds to the substrate via a few strong interactions. 3. Amino acids that make up the active site can be far apart in the primary sequence. Which of...
Please solve Which of the following molecules contains the most chemical potential energy? ADP AMP ATP Adenosine Why is the shape of enzyme activity as a function of temperature shaped like a shark fin and declines above a certain temperature? substrate molecules slow down as temperature increases DNA cannot form hydrogen bonds at high temperatures the enzyme structure is denatured by heat and cannot bind the substrate. the amino acid sequence of the protein changes with heat. You are hired...
1. The turnover number for an enzyme is known to be 5000 min. From the following set of data, calculate the Km, Vmax and the amount of enzyme present in this experiment. Use excel to obtain the lineweaver burk plot. Substrate concentration (MM) 1 Initial velocity (umol/min) 167 250 334 376 498 499 100 1,000
( --/ 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.