Catalysis of the cleavage of peptide bonds in small peptides by a proteolytic en

Question

Catalysis of the cleavage of peptide bonds in small peptides by a proteolytic enzyme is described in the following table.

A) If a mixture of these peptides were presented to the enzyme with the concentration of each peptide being the same, which peptide would be digested most rapidly? Most slowly? Briefly explain your reasoning.

B) The experiment is performed again on another peptide with the following results.

EMTI?F 9 18

On the basis of these data, suggest the features of the amino acid sequence that dictate the specificity of the enzyme.

Explanation / Answer

Kcat/Km ratios:

EMTA G = 6000 1/M.s

EMTA A = 20000 1/M.s

EMTA F = 36000 1/M.s

The higher the ratio, the faster the raction is. Thus EMTA F peptide will be digested most rapidly compared to EMTA G.

b) EMTI F = 2000 1/M.s

based on these data, this enzyme is more specific to EMTA F and least specific to EMTI F

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