D Question 1 A catalytic triad is best described as O an allosteric site for enz

Question

D Question 1 A catalytic triad is best described as O an allosteric site for enzyme reglation O three amino acids that function together at the center of an enzyme active site O an inhibitor of serine proteases O three amino acids on adjacent peptides that stabilize catalytic intermediates O three compounds that coordinate to regulate proteases D Question 2 What creates the difference in specificity between trypsin and chymotrypsin? O different interactions are used in the oxyanion hole different residues are found in the S1 pocket different residues are used to form a catalytic quad produced by different organs different metals arc needed in the catalytic site

Explanation / Answer

Question 1 - A catalytic triad is best described as

- three amino acids that function together at the center of an enzyme active site.

A catalytic triad is a group of three amino acids that are found in the active sites of some proteases involved in catalysis.

Question 2 - What creates the difference in the specificity between trypsin and chymotrypsin

- Different residues are found in the S1 Pocket.

Trypsin favors basic residues like lysine and arginine; chymotrypsin favors aromatic residues like phenylalanine, tyrosine, and tryptophan. The S1 binding pocket in trypsin and chymotrypsin are almost identical in primary sequences and backbone tertiary structures. An important difference is that residue 189 is a negatively charged Asp in trypsin and a polar Ser in chymotrypsin.

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