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stealth61 [152]
3 years ago
10

One member of the serine protease family is trypsin. Trypsin cleaves the polypeptide chain by breaking the peptide bond after a

lysine (lys) or arginine (arg) amino acid. What would be the product(s) if each of the following peptide molecules were treated with trypsin?
a. leu-thr-phe-ala-ser
b. trp-tyr-lys+ala-phe
c. 2lys+2-arg-va

Biology
2 answers:
abruzzese [7]3 years ago
4 0

Answer is below

Explanation:

Oksi-84 [34.3K]3 years ago
4 0

Answer:

The protease Trypsin would cleave the peptide molecules in the following ways below.

Explanation:

Each member of the serine protease family cleaves/cuts the bond after a specific amino acid of the substrate due to that specific amino  acid being recognized by a binding structure of the enzyme that is specifically created to bind that  specific amino acid. Therefore the protease would cleave the following peptide molecules in the following ways:

  1. leu-thr-phe-ala-ser would remain unaffected by the protease trypsin as lysine and arginine amino acids to not form part of the peptide molecule.
  2. trp-tyr-lys-ala-phe would be cleaved by trypsin and become: trp-tyr-lys + ala-phe.
  3. lys-arg-lys-arg-va would be cleaved to have a product of 2lys + 2arg +va.

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