Chymotrypsin (Mr 21,600) degrades peptides by cleaving the amide bond on, Chymot

Question

Chymotrypsin (Mr 21,600) degrades peptides by cleaving the amide bond on,

Chymotrypsin (Mr 21,600) degrades peptides by cleaving the amide bond on the carboxyl side of aromatic amino acids. The following amino acids play important roles in the mechanism of catalysis: G_193, S_195, H_57, A_102. Under saturation conditions, the substrate glycyltyrosinylglycine, is cleaved at a rate of 4.1 moles/min, kcat is 100 sec^-1, and Km is 90 mM. The rate of the uncatalyzed reaction is 65 nmoles/min. The temperature is 37 degree C. What is the catalytic triad? What amino acid is involved in covalent catalysis? What amino acid is involved in general acid and general base catalysis? What is role of the hydrophobic pocket? What is the role of the oxyanion hole? What amino acids form the oxyanion hole? What is the difference in activation energy for the catalyzed vs uncatalyzed reaction.

Explanation / Answer

a)group of 3 amino acid present in active site of chymotrpsin involved in catalysis

b) aspartic aci(acidic),histidine (basic) and cystein (nuclephlic)

D)hydrophobic pocket shows specificity for aromatic amino acid like phenylalanine, tyrosine,and tryptophan.

e) Oxyanion hole pocket in active site of an enzymes stabilize transition state negative charge on deprotonated oxygen..amino acids are mentioned above.

f) In catalyzed reaction.low activation energy is required and in uncatalyzed reaction more activation energy

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