Consider the hypothetical serine protease below, which shows the specificity pockets. The S1 pocket has a…
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Question “Consider the hypothetical serine protease below, which shows the specificity pockets. The S1 pocket has a…”
Consider the hypothetical serine protease
below, which shows the specificity pockets. The S1 pocket has a
glutamic acid in the bottom, the S2 pocket is small and
hydrophobic, and the S1\’ pocket is deep and hydrophobic. Suggest a
3 amino acid sequence that this protease would cleave and indicate
between which sites the peptide bond would be broken.
Answer
Enzymes are biological catalysts that increase the rate of biological reaction by lowering activation energy. They do not consume any reaction product. Anselme Payen, a French chemist, discovered diastase, an enzyme in 1833. Wilhelm Kuhne was the first to use enzyme in 1877.
Most enzymes are proteins and can catalyze over 5,000 biochemical reactions. Enzymes act on substrates to convert them into products. To form an enzyme substrate combination, the active site of the enzyme reacts with the substrate. The enzymes known as serine proteases act on the peptide links between proteins. Serine proteases can be identified by Chymotrypsin and trypsin as well as elastase.
This is the hypothetical structure:
The hypothetical structure shown contains pockets S 1, S 2, and S1′. The bottom of the S1 pocket contains glutamic acid. The S1 pocket is hydrophobic and can hold bulky side chains. The S2 pocket, on the other hand, is smaller and more hydrophobic. Therefore, the sequence that the protease would cleave is Glycine-Lysine-Phenylalanine (Gly-Lys-Phe).
The amino acid end and carboxyl ends of an amino acids sequence are cleaved. This sequence has an amino acid end at S1′ and a carboxyl end near the S1′. The cleavage takes place between S1 (S1′).
Ans:
Conclusion
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