Question

1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words (drawings OR both) why serine proteases cleave either before or after different amino acid residues. Talk about at least two of the following proteases: Chymotrypsin, Trypsin, or Elastase. mod 2) (10pts) Below is a hypothetical peptide sequence. Give the peptide fragments that will occur by enzymatic degradation using Trypsin and Chymotrypsin DARSKWKSENLIRTY

Answer 1

As per HOMEWORKLIB POLICY for multiple questions 1st one considering...
• Sorine Protease o Sorine endopeptidase • Enzymes that cleave peptede bonds in proteins, in which serine serves as the nucleophile amêno oud at the enzymes active site. • They have different substrate binding sites. & Serine protease is one type of Endo protease which can cleave specific peptide bonds within the protein. • Trypsin : - It is an enzyme which selectivay, deave the bond formed by carbonylee acid of lysine and arginine If the peptide sequence is pro Ala-Lyst Phe-bay-Asp - Top-ser Ange Met-Val-Ang & Tyr-Ten- His So the N-terminal amino a Alanine e-terminal amino - Histedene o so trypsin will break into Ala-Lys phe - Gly-Asp - Torup - Ser-Ang mer- Val-Ang Tyro - Leu - this

• Chymotripsin 8 Set It will breate the formed by acid group of amide bond aromathe amino and Phe, Typ, try So the ameno aud sequence - Ala-Lys - phe t Grey-Asp - Topf ser-Ang-met-va 9 4 Ang - Tyrt Leu-this i cleaved by chymotrypsin into - Ala-Lys- the Gly – Asp - Top ser-Ang-met-val-Arg - Tys. Lot Leu – His