Select an enzyme that is Km controlled, one that is kcat controlled, and one that seems to have evolved with both in mind. Why?
Acetylcholinesterase, Carbonic Anhydrase, Catalase, Chymotrypsin, Fumarase, Urease
The Km constant of an enzyme helps in determining the affinity of an enzyme to a substrate. This value helps in determining how efficiently an enzyme can convert a substrate into product. The carbonic anhydrase is an example of an enzyme which is Km controlled. It is found that at the Km value of 9mM and hence it has the lowest Km value amongst all the option given. When the Km value is low, it is able to bind to the HCO3- and hence is able to convert the substrate into its product at a rapid rate.
The Kcat is the turnover number which means the number of substrate molecule which binds to the each of the active site of the enzyme and converts it into product per unit time. Hence it helps in finding out the rate of reaction when negligible amount of substrate is present. Catalase is the enzyme which is controlled by Kcat because it has a very high Kcat value and this means that the enzyme has maximum catalytic activity and hence it is able to convert huge amount of substrate into product
The acetylcholisterase is the one which is controlled by both its kcat as well as Km value and hence it helps in converting the substrate into product depending on its value and when the Km value is low, it will convert maximum product and a low Km value will reduce the conversion.
Select an enzyme that is Km controlled, one that is kcat controlled, and one that seems...
This is a Biochemistry 200 level question, please answer neatly and as soon as possible. Thank you! QUESTION 2 The kinetics parameters of several enzymes are listed below. Arrange the enzymes in order of decreasing catalytic efficiency. Enzyme Substrate kcat (s-1 Km Triosephosphate isomerase Glyceraldehyde-3-phosphate 4.3 x 103 0.47 mm Catalase H202 1.1 M Fumarase fumarate 5.0 x 10-6 M 4.0 x 107 8.0 x 102 5.7 x 103 1.0 x 106 Crotonase crotonyl-CoA 2.0 x 10-2 mm 1.2 x...
please help!! please please "Looking at table 6-8 on Enzyme Reactions from the lecture, which achieves an excellent specificity constant with a very favorable kcat (insert answer here) , which with a favorable Km (insert answer here) , and which with moderate values for each (insert answer here) ? (pick from acetyl cholinesterase, B-lactamase, and catalase)" Question 2: "The units of Vmax are (insert answer here) and the units of Km are (insert answer here) (pick from M, M-1, M/s, s/M...
Below are the Kcat and Km values for 5 hypothetical enzymes. Which enzyme would have the largest specificity constant? Enzyme A - Kcat = 2.6 x 103 , Km = 4 x 10-4 Enzyme B - Kcat = 9 x 102 , Km = 6.1 x 10-6 Enzyme C - Kcat = 1.7 x 10-3 , Km = 3.2 x 105 Enzyme D - Kcat = 2.6 x 10-7 , Km = 4 x 104 Enzyme E - Kcat =...
Does increasing enzyme concentration changes the value of Vmax, Km and Kcat? Why?
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menton plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. see for instance: http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 1 µM and a different variant has a Km of 10 µM....
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
help with these please The turnover number is defined as the maximum number of substrate molecules that can be converted into product molecules per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily equal to the concentration of enzyme molecules, because some enzyme molecules have more than one active site. If the enzyme molecule has one active site, the turnover number is given by turnover number = - -=k2 (Rmax is often written as...
We discussed the substrate preference of chymotrypsin several times. Let's imagine that we are comparing the ability of this enzyme to cleave peptide bonds next to phenylalanine vs. next to alanine. As we know, chymotrypsin prefers to cleave next to phenylalanine, as shown by the kcat/Km values. The kcat/Km values also tell us that the enzyme does not prefer to cleave next to alanin Because kcat/Km is a ratio, it is hard to choose one single reason (kcat vs. km)...
The role of an enzyme in an enzyme-catalyzed reaction is to: Select one: a. make the free-energy change for the reaction more favorable. b. ensure that the product is more stable than the substrate. c. ensure that all the substrate is converted to product. d. increase the rate at which substrate is converted into product. e. do none of the above. The focus of the online practical lesson was the enzyme chymotrypsin. The catalytic mechanism by which chymotrypsin reactions occur:...
What is the enzyme that is responsible for this positive test result? Select one: a. Cytochrome Oxidase b. Catalase c. Gelatinase d. Proteinase