The study above was done on a wildtype enzyme and three genetically-engineered mutants. The purpose was to find a mutation to improve the catalytic efficiency of the enzyme for industrial use. Which is the most accurate statement concerning the data? M2 is the optimal choice when substrate concentrations are saturating. The wildtype enzyme is still preferable to M3 when S<

The study above was done on a wildtype enzyme and three genetically-engineered mutants. The purpose was to find a mutation to improve the catalytic efficiency of the enzyme for industrial use. Which is the most accurate statement concerning the data? M2 is the optimal choice when substrate concentrations are saturating. The wildtype enzyme is still preferable to M3 when S<

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 9QP: a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein...

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Biochemistry: Site-directed mutagenesis, in which individual amino acid residues are replaced with others, is a powerful method to study enzyme mechanisms. In experiments with particular enzyme, various lysine residues were replaced with aspartate, yielding the results summarized in the table below: Enzyme Form: Enzyme Activity (U/mg) Native enzyme: 1,000 U/mg Recombinant Lys 21 to Asp 21: 970 U/mg Recombinant Lys 86 to Asp 86: 100 U/mg Recombinant Lys 101 to Asp 101: 970 U/mg a. What might be inferred about the role of Lys 21, 86, and 101 in the catalytic mechanism of this enzyme? b. Discuss where within the enzyme one might find Lys 21 and 101. Are these residues likely to be evolutionary conserved in this enzyme? Explain c. Is Lys position 86 likely to be evolutionary conserved? Explain
. Seven E. coli mutants were isolated. The activity ofthe enzyme β-galactosidase produced by cells containing each mutation alone or in combination with othermutations was measured when the cells were grown inmedium with different carbon sources.Lactose +Glycerol Lactose GlucoseWild type 0 1000 10Mutant 1 0 10 10Mutant 2 0 10 10Mutant 3 0 0 0Mutant 4 0 0 0Mutant 5 1000 1000 10Mutant 6 1000 1000 10Mutant 7 0 1000 10F′ lac from mutant 0 1000 101/ mutant 3F′ lac from mutant 0 10 102/ mutant 3Mutants 3 + 7 0 1000 10Mutants 4 + 7 0 0 0Mutants 5 + 7 0 1000 10Mutants 6 + 7 1000 1000 10Assume that each of the seven mutations is one andonly one of the genetic lesions in the following list.Identify the type of alteration each mutation represents.a. superrepressorb. operator deletionc. nonsense (amber) suppressor tRNA gene (assumethat the suppressor tRNA is 100% efficient in suppressing amber mutations)d. defective CRP–cAMP binding sitee. nonsense (amber) mutation in the β-galactosidase genef.…
Beer's Law to determine Protein Concentration You have purified a recombinant form of the p53 protein from E. coli and determined the A280 to be1.35. Calculate the molar and mass concentration of the purified protein if the extinction coefficientand molecular weight of p53 is 35,410 M-1 cm-1 and 43,653 Da, respectively (l = 1 cm).
In a pUC19 digest for 1 ug of pUC19 (DNA conc. 282ng/ul) using 10X Cutsmart buffer, pure water and BamHI enzyme in a total volume of 40 ul, how much of each solution is added to the total volume?
In site-directed mutagenesis experiments of an enzyme, scientists altered an aspartate residue to glutamate, lysine, phenylalanine, or valine. Which substitution is expected to have the least effect on enzymatic acitivity? Group of answer choices Glutamate Valine Lysine Phenylalanine
As stated in the text, bacteriophages have been discovered with the followingbase substitutions in their DNA:(a) dUMP completely substituting for dTMP(b) 5-hydroxymethyl-dUMP completely substituting for dTMP(c) 5-methyl-dCMP completely substituting for dCMPFor any one of these cases, formulate a set of virus-coded enzyme activitiesthat could lead to the observed substitution. Write a balanced equation foreach reaction you propose.
You have purified a recombinant form of the p53 protein from E. coli and determined the A280 to be1.35. Calculate the molar and mass concentration of the purified protein if the extinction coefficientand molecular weight of p53 is 35,410 M-1 cm-1 and 43,653 Da, respectively (l = 1 cm).
A site-directed mutagenesis experiment was done on the catalytic triad of the serine protease subtilisin where all of the amino acids of the catalytic triad were mutated to alanine. The triple mutant enzyme was characterized kinetically and the mutant displayed a thousand-fold (103) rate enhancement over the uncatalyzed reaction. Explain the source of this rate enhancement. (The native wild-type subtilisin has a rate acceleration of 1010, when compared to the uncatalyzed reaction.)
In this problem, just put the order of the intermediates on the pathway, starting with P and ending with Z and explain your reasoning. (So to get you started, notice the class 1 mutants—and there is only mutant in this class, which is mutant #5—won’t grow on minimal medium, but will grow if you give it substance Z. However, giving it substances, p, w, x, or y won’t help. This means that the gene that is mutated lies on the pathway in a place that the Z substances is to its right and all the other substances are to its left. The easiest next one to look at is the line with 2 pluses, and then the line with 3 pluses, and then the line with 4 pluses).
Note that the table provided shows a ligation using a molar ratio of 1:3 vector to insert. Write out the complete recipe for a 5:1 insert: vector ligation reaction, including the volumes of insert and vector you calculated above, and the volumes required for a 20 uL reaction: Ligase buffer Nuclease-free water T4 DNA ligase
b. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Denote the point in the pathway in which each individual is blocked.
a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.