The enzyme required for transcription is *
RNA polymerase
Restriction enzymes
Splicesome
DNA polymerase

In Michaelis-Menten kinetics, what values would make an enzyme “good” at catalysis?

What are retroviruses? How do they reproduce and what is the role of the enzyme reverse transcriptase?

How would a competitive, irreversible inhibitor affect an enzyme? Please explain in detail.

very emergence

When glucose is transported into liver cells, it is modified.

1. Name the type of modification to glucose.                                                                (1 mark)

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2. In which part of liver cell does this modification occur?                                          (1 mark)

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3. Name the enzyme in liver cells responsible for this modification.                           (1 mark)

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4. Name the enzyme in brain and muscle cells with the same activity.                        (1 mark)

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5. What is the significance of this type of modification?                                            

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6. Give TWO differences between the enzymes described in (C) and (D).              

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4. Papain is a protease with a pH optimum of approximately 6.5. The enzyme utilizes a catalytic triad to break peptide bonds. The nucleophile within this triad is a cysteine (Cys25) having a perturbed pKa value of 3.3. Write the Henderson-Hasselbalch equation. Using this equation, calculate the percent deprotonated of papain’s Cys25 side chain at pH 3.7. Why will the enzyme not function maximally at this pH? There will be no partial credit for the calculation, but your work must be shown to receive credit. 


Any substance that will bind to a protein is known as its __________________. Enzymes bind their _______________ at the __________________. The enzyme hexokinase is so specific that it reacts with only one of the two __________________ of glucose. Enzymes catalyze a chemical reaction by lowering the __________________, because they provide conditions favorable for the formation of a __________________ intermediate called the __________________. Once the reaction is completed, the enzyme releases the __________________ of the reaction.
Words: free energy ligand transition state activation energy inhibitors products high-energy low-energy active site isomers substrates

1) The enzyme prostaglandin synthase uses aracadonic acid as the substrate and produces product PGG2. If 10mM Ibuprofin inhibits this enzyme as is seen in the 3rd column..

[S](mM)      PGG2(Vo mM/min)      I (Vo mM/min)

0.5               23.5                              16.67

1.0               32.2                              25.25

1.5               36.9                              30.49

2.5               41.8                              37.04

3.5               44.0                              38.91

What is the Ki' ? (THE ANSWER IS UNDEFINED, EXPLAINS AND SHOW YOUR WORK PLEASE)

Kinetic Properties of a Key Enzyme of Prostaglandin Synthesis

Prostaglandins are derived from the 20-carbon fatty acid arachidonic acid in a reaction catalyzed by the enzyme prostaglandin endoperoxide synthase. The enzyme converts arachidonic acid to PGG₂, the immediate precursor for many prostaglandins. The table below show the result of enzyme activity with or without an inhibitor, ibuprofen.

You need first to determine the V_max and K_m, with and without the inhibitor, and then determine which type of inhibitor Ibuprofen is.   The data given here makes it does not afford convenient assessment of V_max and K_m by conventional Michaelis Menten graph (since saturation is not reached under the experimental conditions). Therefore, a Lineweaver-Burke analysis is required. Fill the table with the reciprocal values. The results then are to be drawn as a non-logarithmic graph (next page).

Please show the equation on how to find the 1/[s], the 1/Vo and the 1/Vo[Ib] in the chart. Thank you

Calculate the pI of ASN (α-carboxyl group pK a= 2.1; : α-amino group pK a=9.0