TLS Online TPP Program

#Question id: 13091


To express a yeast gene in E. coli, your task is to design a strategy to insert the yeast gene into the bacterial plasmid. Below is a map of the area of the yeast genome surrounding the gene in which you are interested.
 
The distance between each tick mark placed on the line above is 100 bases in length
Below are the enzymes you can use, with their specific cut sites shown 5’-XXXXXX-3’ 3’-XXXXXX-5’
 
The plasmid is 5,000 bases long and the two farthest restriction enzyme sites are 200 bases apart. The plasmid has an ampicillin resistance gene somewhere on the plasmid distal from the restriction cut sites.
                              
You do the digestion of the insert and the vector and then ligate the two digestions together. You then transform the ligation into bacteria and select for ampicillin resistance. You get three colonies on your transformation plate. You isolate plasmid from each one and cut each plasmid with the enzyme XbaI. You then run your three digestions on an agarose gel and see the following patterns of bands. Describe what each plasmid actually was that was contained in each of the three colonies.
 
Which colony’s plasmid do you actually want to use for your studies?

#Section 7: Recombinant DNA technology and Other Tools in Biotechnology
  1. colony-1 because you want the bacterial promoter to drive transcription of the yeast gene in the correct orientation
  2. colony-2 because you want the bacterial promoter to drive transcription of the yeast gene in the correct orientation
  3. colony-3 because you want the bacterial promoter to drive transcription of the yeast gene in the correct orientation
  4. All colonies because the correct strand of DNA is used as a template in transcription.
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TLS Online TPP Program

#Question id: 634

#Section 2: General Biology

An enzyme has a Vmax of 50 micromol product formed (minute x mg protein)-1 and a Km of 10 microM for the substrate. When a reaction mixture contains the enzyme and 5 microM substrate, which of the following percentages of the maximum velocity will be closest to the initial reaction rate?

TLS Online TPP Program

#Question id: 635

#Section 2: General Biology

The enymatic rate constant (kcat/Km) of orotidine 5ʹ-phosphate decarboxylase is 6 x 107 M-1s-1 and the nonenzymatic rate constant (kn) is 3 x 10-16 s-1.  What is the value of the enzymeʹs catalytic proficiency?

TLS Online TPP Program

#Question id: 636

#Section 2: General Biology

DNA polymerase contains a lysine residue that is important for binding to DNA. Mutations were found that converted this lysine to either glutamate, glycine, valine, or arginine. Which mutations would be predicted to be the most and least harmful to the ability of the enzyme to bind DNA?

Most

Least

(A)

Valine

Aspartate

(B)

Glycine

Arginine

(C)

Arginine

Glycine

(D)

Glutamate

Arginine

TLS Online TPP Program

#Question id: 638

#Section 2: General Biology

Match the following class of enzymes with them

EnzymeClass of enzyme
A. Hexokinase1
B. Phosphoglucoisomerase2
C. Glyceraldehyde 3-phosphate dehydrogenase3
D. Phosphoglycerate mutase4
E. Enolase5
F. Aldolase

TLS Online TPP Program

#Question id: 639

#Section 2: General Biology

Match the coenzymes in column I enzymes to class of enzymes in column II

EnzymeReaction Type
A. Phosphofructokinase1. Redox reaction
B. Enolase2. Phosphoryl shift
C. Phosphoglycerate mutase3. Dehydration
D. Glyceraldehyde 3 Phosphate dehydrogenase4. Phosphoryl transfer

TLS Online TPP Program

#Question id: 640

#Section 2: General Biology

The data in the table above were collected for an enzyme-catalyzed reaction. The Km for this enzyme is approximately