Question

Based on what we've learned about the enzyme chymotrypsin: a) Explain the general role of each catalytic residue in the chymotrypsin catalytic triad. b) Describe the catalytic strategy or strategies used by chymotrypsin. c) Identify the class of enzymes chymotrypsin belongs to. 7. At a molecular level, how do carbon dioxide and hydrogen ions regulate oxygen binding to hemoglobin?

Answer 1

6.

a)

Certain amino acids that are straight away implicated in the chemical catalysis are called as the chemical residues of the enzyme involved. A catalytic triad is reffered to as the arrangement of three amino acids which are present at the active site of the enzyme un question. For chymotripsin, the catalytic triad is created of serine 195, histidine 57, and aspartate 102. Serine is attached sideways to the imidazole ring of the histidine residue that further receives a proton from the serine under the existance of the substrate. The residue of the aspartate aligns histidine, in order to create an advanced proton acceptor. Seine is attached to histadine which lends support attachemnt to aspartate.

b)

Covalent catalysis is the catalytic strategies being used by chymotrypsin. It involves functional groups present in the enzymes being used as a neucleophile. For example : OH group of serine, SH group of cysteine and imidazole group of histidine.