What is the function of Histidine and Aspartic Acid in Chymotrypsin?

Expert Solution

Not only Histidine and Aspartic Acid, there is a catalytic triad specifically with residue numbers in chymotripsin as serine 195, histidine 57, and aspartate 102. These residues are distributed throughout the 240 amino acid residues found in chymotrypsin, but are located in close proximity in the active three-dimensional conformation of the enzyme as shown in below figure. (This 3D model is reproduced from Reference text book - Lehninger, biochemistry, otherwise i can't build it, hence it is easy to understand pictorially than in words)

Chymotrypsin enzyme belongs to serine proteases family, mainly its function is to hydrolysis of peptides, the mechanism is shown below for clear understanding how it will be function. The peptide bond (-CO-NH-) split by this enzyme is 10¹⁰ times faster than without this enzyme.

Thank You So Much! Please Rate this answer as you wish.

queen_honey_blossom answered 2 years ago

Calculate (show the calculations) the pI for histidine, and aspartic acid.

A pentapeptide that contains histidine, two glycines, tryptophan, and alanine is incubated with the protease chymotrypsin....

A pentapeptide that contains histidine, two glycines, tryptophan, and alanine is incubated with the protease chymotrypsin. A dipeptide and a tripeptide result, and the dipeptide contains tryptophan while the tripeptide contains histidine and two glycines. Brief treatment with carboxypeptidase A yields free histidine. What is the sequence of the peptapeptide? Answer options: GGWAH GGHWA AWGGH GGHAW GWAGH

How does Aspartic acid mutated to glycine? What are the effects of the mutation to a...

How does Aspartic acid mutated to glycine? What are the effects of the mutation to a protein? What would is change

What kind of enzyme is chymotrypsin? What are the specific substrates of chymotrypsin? • What features...

What kind of enzyme is chymotrypsin? What are the specific substrates of chymotrypsin? • What features of chymotrypsin make it specific to particular substrates ? • Can you describe the main features of the reaction mechanism? • What is a catalytic triad and what is its role in the active site of chymotrypsin? • What is an acyl-enzyme intermediate? • What is conformational selection vs. “induced fit”?

Which amino acid is the most hydrophobic? (1pt) Arginine Aspartic Acid Leucine Serine Tyrosine

calculate the Pi value of aspartic acid and lysine compare the two values

From these 3 molecules: maltose, linoleic acid and histidine, completely solve: 2. What is the energy...

From these 3 molecules: maltose, linoleic acid and histidine, completely solve: 2. What is the energy efficiency of the metabolism of these three molecules (total number of ATP molecules generated)? 3. What is the balance of coenzymes of great reducing power NADH and FADH2 in this metabolic integration of the 3 molecules? 4. Identify the regulatory points that occur in the metabolism of the three molecules. 5. Identify the cellular compartments where each of the phases of the metabolism of...

Which of the following located in the active site of the enzyme chymotrypsin participates in acid-base...

Which of the following located in the active site of the enzyme chymotrypsin participates in acid-base chemistry? The side chain oxygen of serine The amide group of glycine The hydrophobic pocket Histidine The amide group of serine

An enzyme contains an active site aspartic acid with a pka=5.0 which acts as a general...

An enzyme contains an active site aspartic acid with a pka=5.0 which acts as a general acid catalyst. Draw the curve of enzyme activity vs. pH for the enzyme (assume the protein is stably folded between pH 2-12 and that the active site Asp is the only ionizable residue involved in catalysis).Explain the shape of the curve

How do I draw the predominant form of aspartic acid when the pH is 5? How...

How do I draw the predominant form of aspartic acid when the pH is 5? How do I draw all the forms or arginine that would be seen between the pH values of 1 and 12?

Question